UniProtKB - P54317 (LIPR2_HUMAN)
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>sp|P54317|LIPR2_HUMAN Pancreatic lipase-related protein 2 OS=Homo sapiens OX=9606 GN=PNLIPRP2 PE=1 SV=2 MLPPWTLGLLLLATVRGKEVCYGQLGCFSDEKPWAGTLQRPVKLLPWSPEDIDTRFLLYT NENPNNFQLITGTEPDTIEASNFQLDRKTRFIIHGFLDKAEDSWPSDMCKKMFEVEKVNC ICVDWRHGSRAMYTQAVQNIRVVGAETAFLIQALSTQLGYSLEDVHVIGHSLGAHTAAEA GRRLGGRVGRITGLDPAGPCFQDEPEEVRLDPSDAVFVDVIHTDSSPIVPSLGFGMSQKV GHLDFFPNGGKEMPGCKKNVLSTITDIDGIWEGIGGFVSCNHLRSFEYYSSSVLNPDGFL GYPCASYDEFQESKCFPCPAEGCPKMGHYADQFKGKTSAVEQTFFLNTGESGNFTSWRYK ISVTLSGKEKVNGYIRIALYGSNENSKQYEIFKGSLKPDASHTCAIDVDFNVGKIQKVKF LWNKRGINLSEPKLGASQITVQSGEDGTEYNFCSSDTVEENVLQSLYPCCommunity curation ()Add a publicationFeedback
Pancreatic lipase-related protein 2
PNLIPRP2
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:15287741, PubMed:17401110, PubMed:19451396, PubMed:21865348, PubMed:20083229, PubMed:26494624, PubMed:18702514).
In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (PubMed:23732775, PubMed:19824014, PubMed:21652702).
Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:15287741, PubMed:17401110, PubMed:21865348, PubMed:21652702, PubMed:18702514).
Can completely deacylate triacylglycerols (PubMed:21865348).
When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (PubMed:15287741, PubMed:17401110, PubMed:20083229, PubMed:26494624, PubMed:18702514).
Hydrolyzes medium- and long-chain fatty acyls in galactolipids (PubMed:20083229, PubMed:18702514).
May act together with LIPF to hydrolyze partially digested triglycerides (PubMed:23732775).
Hydrolyzes long-chain monoglycerides with high efficiency (PubMed:17401110, PubMed:21652702, PubMed:23732775).
In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity).
Also has low phospholipase activity (PubMed:17401110, PubMed:18702514).
In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity).
The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity).
By similarity<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
10 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.10"Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic T lymphocytes (CTLs) and reevaluation of the negative effects of its gene ablation on cytotoxicity."
Alves B.N., Leong J., Tamang D.L., Elliott V., Edelnant J., Redelman D., Singer C.A., Kuhn A.R., Miller R., Lowe M.E., Hudig D.
J. Leukoc. Biol. 86:701-712(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.11"Individual and combined action of pancreatic lipase and pancreatic lipase-related proteins 1 and 2 on native versus homogenized milk fat globules."
Berton A., Sebban-Kreuzer C., Rouvellac S., Lopez C., Crenon I.
Mol. Nutr. Food Res. 53:1592-1602(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.15"Pancreatic lipase-related protein 2 digests fats in human milk and formula in concert with gastric lipase and carboxyl ester lipase."
Johnson K., Ross L., Miller R., Xiao X., Lowe M.E.
Pediatr. Res. 74:127-132(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- a triacylglycerolEC:3.1.1.3
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- See the description of this molecule in ChEBI.
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- See the description of this molecule in ChEBI.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.10"Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic T lymphocytes (CTLs) and reevaluation of the negative effects of its gene ablation on cytotoxicity."
Alves B.N., Leong J., Tamang D.L., Elliott V., Edelnant J., Redelman D., Singer C.A., Kuhn A.R., Miller R., Lowe M.E., Hudig D.
J. Leukoc. Biol. 86:701-712(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
- Search proteins in UniProtKB for this EC number.
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Manual assertion based on experiment ini
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.10"Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic T lymphocytes (CTLs) and reevaluation of the negative effects of its gene ablation on cytotoxicity."
Alves B.N., Leong J., Tamang D.L., Elliott V., Edelnant J., Redelman D., Singer C.A., Kuhn A.R., Miller R., Lowe M.E., Hudig D.
J. Leukoc. Biol. 86:701-712(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.10"Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic T lymphocytes (CTLs) and reevaluation of the negative effects of its gene ablation on cytotoxicity."
Alves B.N., Leong J., Tamang D.L., Elliott V., Edelnant J., Redelman D., Singer C.A., Kuhn A.R., Miller R., Lowe M.E., Hudig D.
J. Leukoc. Biol. 86:701-712(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
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a triacylglycerol- Search proteins in UniProtKB for this molecule.
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=a diacylglycerol- Search proteins in UniProtKB for this molecule.
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- a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerolEC:3.1.1.26
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
Manual assertion based on experiment ini
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
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+2H2O- Search proteins in UniProtKB for this molecule.
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=3-β-D-galactosyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+2a fatty acid- Search proteins in UniProtKB for this molecule.
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+2H+- Search proteins in UniProtKB for this molecule.
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- 1,2,3-tri-(9Z-octadecenoyl)-glycerol
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.10"Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic T lymphocytes (CTLs) and reevaluation of the negative effects of its gene ablation on cytotoxicity."
Alves B.N., Leong J., Tamang D.L., Elliott V., Edelnant J., Redelman D., Singer C.A., Kuhn A.R., Miller R., Lowe M.E., Hudig D.
J. Leukoc. Biol. 86:701-712(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.10"Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic T lymphocytes (CTLs) and reevaluation of the negative effects of its gene ablation on cytotoxicity."
Alves B.N., Leong J., Tamang D.L., Elliott V., Edelnant J., Redelman D., Singer C.A., Kuhn A.R., Miller R., Lowe M.E., Hudig D.
J. Leukoc. Biol. 86:701-712(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2,3-tri-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+H2O- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
=(9Z)-octadecenoate- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
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+di-(9Z)-octadecenoylglycerol- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
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+H+- Search proteins in UniProtKB for this molecule.
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- di-(9Z)-octadecenoylglycerol
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
di-(9Z)-octadecenoylglycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
=(9Z)-octadecenoate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
zoom
+H+- Search proteins in UniProtKB for this molecule.
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- (9Z-octadecenoyl)-glycerol
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
=(9Z)-octadecenoate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+glycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
+H+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- 1-(9Z-octadecenoyl)-glycerol
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
=(9Z)-octadecenoate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+glycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
+H+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- 1,2,3-tripropanoylglycerol
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2,3-tripropanoylglycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
=dipropanoylglycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+H+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+propanoate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
- 1,2,3-tributanoylglycerol
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2,3-tributanoylglycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
=butanoate- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
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+dibutanoylglycerol- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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- 1,2,3-trioctanoylglycerol
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
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1,2,3-trioctanoylglycerol- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=dioctanoylglycerol- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+octanoate- Search proteins in UniProtKB for this molecule.
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- 1,2-didecanoylglycerol
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2-didecanoylglycerol- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=decanoate- Search proteins in UniProtKB for this molecule.
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+decanoylglycerol- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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- H2O
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion inferred by curator fromi
- Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
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+long chain 1,2-diacyl-3-O-β-D-galactosyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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=a fatty acid- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+long chain acyl-3-O-β-D-galactosyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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- 1,2-dioctanoyl-3-O-β-D-galactosyl-sn-glycerol
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2-dioctanoyl-3-O-β-D-galactosyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=H+- Search proteins in UniProtKB for this molecule.
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+octanoate- Search proteins in UniProtKB for this molecule.
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+octanoyl-3-(β-D-galactosyl)-sn-glycerol- Search proteins in UniProtKB for this molecule.
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- 1,2-didodecanoyl-3-β-D-galactosyl-sn-glycerol
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- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2-didodecanoyl-3-β-D-galactosyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
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=dodecanoate- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
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+dodecanoyl-3-β-D-galactosyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
zoom
+H+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- 1-β-D-galactosyl-2,3-didodecanoyl-sn-glycerol
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1-β-D-galactosyl-2,3-didodecanoyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=1-β-D-galactosyl-dodecanoyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+dodecanoate- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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- 1,2-diacyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2-diacyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=a fatty acid- Search proteins in UniProtKB for this molecule.
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+acyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol- Search proteins in UniProtKB for this molecule.
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zoom
+H+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- H2O
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
+long chain 1,2-diacyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol- Search proteins in UniProtKB for this molecule.
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=a fatty acid- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+long chain acyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol- Search proteins in UniProtKB for this molecule.
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- 1,2-dioctanoyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2-dioctanoyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=H+- Search proteins in UniProtKB for this molecule.
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+octanoate- Search proteins in UniProtKB for this molecule.
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+octanoyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol- Search proteins in UniProtKB for this molecule.
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- 1,2-didodecanoyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
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Manual assertion based on experiment ini
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2-didodecanoyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
=dodecanoate- Search proteins in UniProtKB for this molecule.
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+dodecanoyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- a 1,2-diacyl-sn-glycero-3-phosphocholine
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
a 1,2-diacyl-sn-glycero-3-phosphocholine- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+H2O- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
=a fatty acid- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+a monoacyl-sn-glycero-3-phosphocholine- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
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+H+- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Manual assertion based on experiment ini
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY. - Ref.13"Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat digestion in human newborns."
Xiao X., Mukherjee A., Ross L.E., Lowe M.E.
J. Biol. Chem. 286:26353-26363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, VARIANT 357-TRP--CYS-469 DEL. - Ref.15"Pancreatic lipase-related protein 2 digests fats in human milk and formula in concert with gastric lipase and carboxyl ester lipase."
Johnson K., Ross L., Miller R., Xiao X., Lowe M.E.
Pediatr. Res. 74:127-132(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION. - Ref.16"The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of Pancreatic Lipase-related Protein 2 (PNLIPRP2)."
Xiao X., Lowe M.E.
J. Biol. Chem. 290:28847-28856(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REGION.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei
Manual assertion based on experiment ini
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: triacylglycerol degradation
This protein is involved in the pathway triacylglycerol degradation, which is part of Glycerolipid metabolism.1 PublicationManual assertion based on experiment ini
- Ref.14"BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line."
Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.
J. Lipid Res. 52:1949-1956(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
View all proteins of this organism that are known to be involved in the pathway triacylglycerol degradation and in Glycerolipid metabolism.
Pathwayi: Glycolipid metabolism
This protein is involved in Glycolipid metabolism.1 PublicationManual assertion based on experiment ini
- Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY.
View all proteins of this organism that are known to be involved in Glycolipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 171 | Nucleophile1 Publication Manual assertion based on experiment ini
| 1 | |
Active sitei | 195 | Charge relay systemPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 206 | Calcium; via carbonyl oxygenCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Metal bindingi | 209 | Calcium; via carbonyl oxygenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Metal bindingi | 211 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Metal bindingi | 214 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Active sitei | 282 | Charge relay systemPROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- 1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity Source: UniProtKB-EC
- acylglycerol lipase activity Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
- calcium ion binding Source: UniProtKBInferred from direct assayi
- Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
- galactolipase activity Source: UniProtKBInferred from direct assayi
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS. - Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY.
- lipase activity Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- phospholipase activity Source: UniProtKBInferred from direct assayi
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
- triglyceride lipase activity Source: UniProtKBInferred from direct assayi
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
GO - Biological processi
- cellular defense response Source: Ensembl
- galactolipid catabolic process Source: UniProtKBInferred from direct assayi
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS. - Ref.12"Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY.
- intestinal lipid catabolic process Source: Ensembl
- lipid catabolic process Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- lipid digestion Source: Reactome
- phosphatidylcholine catabolic process Source: UniProtKBInferred from direct assayi
- Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
- phospholipid catabolic process Source: UniProtKBInferred from direct assayi
- Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
- response to bacterium Source: Ensembl
- triglyceride catabolic process Source: UniProtKBInferred from direct assayi
- Ref.8"Human pancreatic lipase-related protein 2 is a galactolipase."
Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A., Leboeuf B., Verger R., Carriere F.
Biochemistry 43:10138-10148(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.9"Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells."
Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R., Carriere F., De Caro A.
J. Lipid Res. 48:1539-1549(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
- triglyceride metabolic process Source: ProtInc
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p>
Traceable author statementi
- Ref.1"Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity."
Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.
J. Biol. Chem. 267:16509-16516(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-361.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Molecular function | Hydrolase |
Biological process | Lipid degradation, Lipid metabolism |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.1.26, 2681 |
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | P54317 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-192456, Digestion of dietary lipid |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P54317 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00256 |
Protein family/group databases
ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins More...ESTHERi | human-PNLIPRP2, Pancreatic_lipase |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000001434 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Pancreatic lipase-related protein 2Imported<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi Short name: PL-RP21 Publication Manual assertion inferred by curator fromi
Alternative name(s): Cytotoxic T lymphocyte lipaseBy similarity Manual assertion inferred from sequence similarity toi Galactolipase (EC:3.1.1.26
Manual assertion based on experiment ini
Triacylglycerol lipase (EC:3.1.1.3
Manual assertion based on experiment ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:PNLIPRP2Imported Manual assertion inferred from database entriesi Synonyms:PLRP21 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:9157, PNLIPRP2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604423, gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P54317 |
Eukaryotic Pathogen, Vector and Host Database Resources More...VEuPathDBi | HostDB:ENSG00000266200 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Extracellular region or secreted
- Secreted 2 Publications
Manual assertion based on experiment ini
- Ref.11"Individual and combined action of pancreatic lipase and pancreatic lipase-related proteins 1 and 2 on native versus homogenized milk fat globules."
Berton A., Sebban-Kreuzer C., Rouvellac S., Lopez C., Crenon I.
Mol. Nutr. Food Res. 53:1592-1602(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
- Secreted 2 Publications
Other locations
- Zymogen granule membrane By similarity
Manual assertion inferred from sequence similarity toi
; Peripheral membrane protein By similarityManual assertion inferred from sequence similarity toi
- neuron projection By similarity
Manual assertion inferred from sequence similarity toi
Note: Localizes to neurite tips in neuronal cells.By similarity- Zymogen granule membrane By similarity
Manual assertion inferred from sequence similarity toi
Extracellular region or secreted
- extracellular region Source: Reactome
- extracellular space Source: UniProtKBInferred from direct assayi
- Ref.17"Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
Other locations
- cytoplasmic vesicle Source: UniProtKB-KW
- membrane Source: UniProtKB-KW
- neuron projection Source: UniProtKB
Keywords - Cellular componenti
Cell projection, Cytoplasmic vesicle, Membrane, Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 353 | N → Q: Loss of N-glycosylation. 1 Publication Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 5408 |
Open Targets More...OpenTargetsi | ENSG00000266200 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33480 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | P54317, Tbio |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2169728 |
Drug and drug target database More...DrugBanki | DB02613, Capric dimethyl amine oxide |
Genetic variation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PNLIPRP2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1708840 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 17 | Sequence analysisAdd BLAST | 17 | |
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000017793 | 18 – 469 | Pancreatic lipase-related protein 2Add BLAST | 452 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 21 ↔ 27 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
Disulfide bondi | 109 ↔ 120 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
Disulfide bondi | 256 ↔ 280 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
Disulfide bondi | 304 ↔ 315 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
Disulfide bondi | 318 ↔ 323 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 353 | N-linked (GlcNAc...) asparagineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Glycosylationi | 428 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 453 ↔ 469 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
|
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | P54317 |
PeptideAtlas More...PeptideAtlasi | P54317 |
PRoteomics IDEntifications database More...PRIDEi | P54317 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 56684 |
PTM databases
GlyGen: Computational and Informatics Resources for Glycoscience More...GlyGeni | P54317, 2 sites |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P54317 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P54317 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Manual assertion based on experiment ini
- Ref.7"Discoordinate expression of pancreatic lipase and two related proteins in the human fetal pancreas."
Yang Y., Sanchez D., Figarella C., Lowe M.E.
Pediatr. Res. 47:184-188(2000) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei
Manual assertion based on experiment ini
- Ref.7"Discoordinate expression of pancreatic lipase and two related proteins in the human fetal pancreas."
Yang Y., Sanchez D., Figarella C., Lowe M.E.
Pediatr. Res. 47:184-188(2000) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000266200, Expressed in body of pancreas and 110 other tissues |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P54317, baseline and differential |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 111409, 13 interactors |
Protein interaction database and analysis system More...IntActi | P54317, 1 interactor |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | P54317, protein |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 19 – 21 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 23 – 25 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 27 – 29 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 32 – 34 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 35 – 37 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 49 – 52 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 55 – 59 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 61 – 66 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 68 – 70 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 72 – 74 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 76 – 80 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 87 – 93 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 104 – 112 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Turni | 113 – 115 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 118 – 124 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 126 – 129 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 133 – 158 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 26 | |
Helixi | 162 – 164 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 165 – 170 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 173 – 183 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Turni | 184 – 186 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 188 – 195 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Turni | 199 – 203 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Turni | 206 – 208 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 212 – 214 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 215 – 221 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 223 – 226 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 228 – 230 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 234 – 236 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 241 – 247 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Turni | 248 – 251 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 276 – 278 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 280 – 294 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
Beta strandi | 298 – 300 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 307 – 311 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Turni | 312 – 315 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 325 – 327 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 330 – 332 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 334 – 337 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 338 – 346 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 357 – 369 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
Beta strandi | 371 – 380 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 385 – 396 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
Beta strandi | 401 – 410 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 417 – 423 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 434 – 443 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Turni | 444 – 446 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 449 – 453 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 464 – 468 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P54317 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P54317 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 357 – 469 | PLATPROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 113 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 93 – 105 | Required for galactolipase activity1 Publication Manual assertion based on experiment ini
| 13 | |
Regioni | 257 – 279 | Required for galactolipase activity1 Publication Manual assertion based on experiment ini
| 23 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
Ensembl GeneTree More...GeneTreei | ENSGT00940000155139 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P54317 |
Identification of Orthologs from Complete Genome Data More...OMAi | FTRWRYK |
Database of Orthologous Groups More...OrthoDBi | 534956at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P54317 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00707, Pancreat_lipase_like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.50.1820, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR013818, Lipase IPR016272, Lipase_LIPH IPR033906, Lipase_N IPR002331, Lipase_panc IPR001024, PLAT/LH2_dom IPR036392, PLAT/LH2_dom_sf IPR000734, TAG_lipase |
The PANTHER Classification System More...PANTHERi | PTHR11610, PTHR11610, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00151, Lipase, 1 hit PF01477, PLAT, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000865, Lipoprotein_lipase_LIPH, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00823, PANCLIPASE PR00821, TAGLIPASE |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00308, LH2, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF49723, SSF49723, 1 hit SSF53474, SSF53474, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00120, LIPASE_SER, 1 hit PS50095, PLAT, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
10 20 30 40 50
MLPPWTLGLL LLATVRGKEV CYGQLGCFSD EKPWAGTLQR PVKLLPWSPE
60 70 80 90 100
DIDTRFLLYT NENPNNFQLI TGTEPDTIEA SNFQLDRKTR FIIHGFLDKA
110 120 130 140 150
EDSWPSDMCK KMFEVEKVNC ICVDWRHGSR AMYTQAVQNI RVVGAETAFL
160 170 180 190 200
IQALSTQLGY SLEDVHVIGH SLGAHTAAEA GRRLGGRVGR ITGLDPAGPC
210 220 230 240 250
FQDEPEEVRL DPSDAVFVDV IHTDSSPIVP SLGFGMSQKV GHLDFFPNGG
260 270 280 290 300
KEMPGCKKNV LSTITDIDGI WEGIGGFVSC NHLRSFEYYS SSVLNPDGFL
310 320 330 340 350
GYPCASYDEF QESKCFPCPA EGCPKMGHYA DQFKGKTSAV EQTFFLNTGE
360 370 380 390 400
SGNFTSWRYK ISVTLSGKEK VNGYIRIALY GSNENSKQYE IFKGSLKPDA
410 420 430 440 450
SHTCAIDVDF NVGKIQKVKF LWNKRGINLS EPKLGASQIT VQSGEDGTEY
460
NFCSSDTVEE NVLQSLYPC
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketEntry | Entry name | Protein names | Gene names | Length | Annotation | ||
---|---|---|---|---|---|---|---|
A0A087WX88 | A0A087WX88_HUMAN | Triacylglycerol lipase Triacylglycerol lipase, EC 3.1.1.3 (Pancreatic lipase) | PNLIPRP2 | 468 | Annotation score: Annotation score:3 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 239 | K → R in BAF84181 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 352 | G → V in BAF84181 (PubMed:14702039).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_083661 | 357 – 469 | Missing Associated with adaptation to cereal-based diet and found in different populations with high allele frequencies; expected to result in near complete absence of the protein and loss of function; if expressed is weakly secreted, mostly intracellularly retained and degraded. 3 Publications Manual assertion based on experiment ini
| 113 | |
Natural variantiVAR_080185 | 361 | I → V1 Publication Manual assertion based on experiment ini
| 1 |
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M93284 mRNA Translation: AAA59533.1 AK291492 mRNA Translation: BAF84181.1 CR456949 mRNA Translation: CAG33230.1 AC016825 Genomic DNA No translation available. FO082044 Genomic DNA No translation available. CH471066 Genomic DNA Translation: EAW49448.1 BC005989 mRNA Translation: AAH05989.1 |
Protein sequence database of the Protein Information Resource More...PIRi | B43357 |
NCBI Reference Sequences More...RefSeqi | NP_005387.2, NM_005396.4 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000591655; ENSP00000468117; ENSG00000266200 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5408 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5408 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P54317 | Triacylglycerol lipase | 469 | UniRef90_P54317 | |||
Triacylglycerol lipase | 469 | |||||
Triacylglycerol lipase | 469 | |||||
Triacylglycerol lipase | 469 | |||||
Triacylglycerol lipase | 469 | |||||
+12 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P54317 | Pancreatic lipase-related protein 2 | 469 | UniRef50_P54317 | |||
Pancreatic lipase-related protein 2 | 471 | |||||
Pancreatic lipase-related protein 2 | 470 | |||||
Triacylglycerol lipase | 469 | |||||
Triacylglycerol lipase | 469 | |||||
+352 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M93284 mRNA Translation: AAA59533.1 AK291492 mRNA Translation: BAF84181.1 CR456949 mRNA Translation: CAG33230.1 AC016825 Genomic DNA No translation available. FO082044 Genomic DNA No translation available. CH471066 Genomic DNA Translation: EAW49448.1 BC005989 mRNA Translation: AAH05989.1 |
PIRi | B43357 |
RefSeqi | NP_005387.2, NM_005396.4 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2OXE | X-ray | 2.80 | A/B | 18-469 | [»] | |
2PVS | X-ray | 3.00 | A/B | 18-469 | [»] | |
SMRi | P54317 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111409, 13 interactors |
IntActi | P54317, 1 interactor |
Chemistry databases
ChEMBLi | CHEMBL2169728 |
DrugBanki | DB02613, Capric dimethyl amine oxide |
SwissLipidsi | SLP:000001434 |
Protein family/group databases
ESTHERi | human-PNLIPRP2, Pancreatic_lipase |
PTM databases
GlyGeni | P54317, 2 sites |
iPTMneti | P54317 |
PhosphoSitePlusi | P54317 |
Genetic variation databases
BioMutai | PNLIPRP2 |
DMDMi | 1708840 |
Proteomic databases
MassIVEi | P54317 |
PeptideAtlasi | P54317 |
PRIDEi | P54317 |
ProteomicsDBi | 56684 |
Protocols and materials databases
Antibodypedia a portal for validated antibodies More...Antibodypediai | 73327, 75 antibodies from 14 providers |
The DNASU plasmid repository More...DNASUi | 5408 |
Genome annotation databases
Ensembli | ENST00000591655; ENSP00000468117; ENSG00000266200 |
GeneIDi | 5408 |
KEGGi | hsa:5408 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5408 |
DisGeNETi | 5408 |
GeneCards: human genes, protein and diseases More...GeneCardsi | PNLIPRP2 |
HGNCi | HGNC:9157, PNLIPRP2 |
MIMi | 604423, gene |
neXtProti | NX_P54317 |
OpenTargetsi | ENSG00000266200 |
PharmGKBi | PA33480 |
VEuPathDBi | HostDB:ENSG00000266200 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
GeneTreei | ENSGT00940000155139 |
InParanoidi | P54317 |
OMAi | FTRWRYK |
OrthoDBi | 534956at2759 |
PhylomeDBi | P54317 |
Enzyme and pathway databases
UniPathwayi | UPA00256 |
BRENDAi | 3.1.1.26, 2681 |
PathwayCommonsi | P54317 |
Reactomei | R-HSA-192456, Digestion of dietary lipid |
SignaLinki | P54317 |
Miscellaneous databases
BioGRID ORCS database of CRISPR phenotype screens More...BioGRID-ORCSi | 5408, 5 hits in 225 CRISPR screens |
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | PNLIPRP2, human |
EvolutionaryTracei | P54317 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 5408 |
Pharosi | P54317, Tbio |
Protein Ontology More...PROi | PR:P54317 |
RNActi | P54317, protein |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000266200, Expressed in body of pancreas and 110 other tissues |
ExpressionAtlasi | P54317, baseline and differential |
Family and domain databases
CDDi | cd00707, Pancreat_lipase_like, 1 hit |
Gene3Di | 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR013818, Lipase IPR016272, Lipase_LIPH IPR033906, Lipase_N IPR002331, Lipase_panc IPR001024, PLAT/LH2_dom IPR036392, PLAT/LH2_dom_sf IPR000734, TAG_lipase |
PANTHERi | PTHR11610, PTHR11610, 1 hit |
Pfami | View protein in Pfam PF00151, Lipase, 1 hit PF01477, PLAT, 1 hit |
PIRSFi | PIRSF000865, Lipoprotein_lipase_LIPH, 1 hit |
PRINTSi | PR00823, PANCLIPASE PR00821, TAGLIPASE |
SMARTi | View protein in SMART SM00308, LH2, 1 hit |
SUPFAMi | SSF49723, SSF49723, 1 hit SSF53474, SSF53474, 1 hit |
PROSITEi | View protein in PROSITE PS00120, LIPASE_SER, 1 hit PS50095, PLAT, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | LIPR2_HUMAN | |
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P54317Primary (citable) accession number: P54317 Secondary accession number(s): A0A075B781, A8K627, Q6IB55 | |
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | March 28, 2018 | |
Last modified: | February 23, 2022 | |
This is version 167 of the entry and version 2 of the sequence. See complete history. | ||
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families