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P54317

- LIPR2_HUMAN

UniProt

P54317 - LIPR2_HUMAN

Protein

Pancreatic lipase-related protein 2

Gene

PNLIPRP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Acts preferentially on monoglycerides, phospholipids and galactolipids. Contributes to milk fat hydrolysis.3 Publications

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication
    1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei171 – 1711Nucleophile1 Publication
    Active sitei195 – 1951Charge relay system1 PublicationPROSITE-ProRule annotation
    Metal bindingi206 – 2061Calcium; via carbonyl oxygen
    Metal bindingi209 – 2091Calcium; via carbonyl oxygen
    Metal bindingi211 – 2111Calcium
    Metal bindingi214 – 2141Calcium
    Active sitei282 – 2821Charge relay system1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acylglycerol lipase activity Source: UniProtKB
    2. calcium ion binding Source: UniProtKB
    3. galactolipase activity Source: UniProtKB
    4. phospholipase activity Source: UniProtKB
    5. triglyceride lipase activity Source: ProtInc

    GO - Biological processi

    1. galactolipid catabolic process Source: UniProtKB
    2. lipid digestion Source: Reactome
    3. phospholipid catabolic process Source: UniProtKB
    4. small molecule metabolic process Source: Reactome
    5. triglyceride metabolic process Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_9518. Digestion of dietary lipid.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pancreatic lipase-related protein 2 (EC:3.1.1.26, EC:3.1.1.3)
    Short name:
    PL-RP2
    Alternative name(s):
    Galactolipase
    Gene namesi
    Name:PNLIPRP2
    Synonyms:PLRP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:9157. PNLIPRP2.

    Subcellular locationi

    Secreted 2 Publications

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi353 – 3531N → Q: Loss of N-glycosylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA33480.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 469452Pancreatic lipase-related protein 2PRO_0000017793Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 271 PublicationPROSITE-ProRule annotation
    Disulfide bondi109 ↔ 1201 PublicationPROSITE-ProRule annotation
    Disulfide bondi256 ↔ 2801 PublicationPROSITE-ProRule annotation
    Disulfide bondi304 ↔ 3151 PublicationPROSITE-ProRule annotation
    Disulfide bondi318 ↔ 3231 PublicationPROSITE-ProRule annotation
    Glycosylationi353 – 3531N-linked (GlcNAc...)1 Publication
    Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi453 ↔ 4691 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiP54317.

    Expressioni

    Tissue specificityi

    Pancreas.

    Gene expression databases

    CleanExiHS_PNLIPRP2.
    GenevestigatoriP54317.

    Interactioni

    Protein-protein interaction databases

    BioGridi111409. 2 interactions.

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 213
    Helixi23 – 253
    Beta strandi27 – 293
    Turni32 – 343
    Beta strandi35 – 373
    Helixi49 – 524
    Beta strandi55 – 595
    Beta strandi61 – 666
    Beta strandi68 – 703
    Beta strandi72 – 743
    Helixi76 – 805
    Beta strandi87 – 937
    Helixi104 – 1129
    Turni113 – 1153
    Beta strandi118 – 1247
    Helixi126 – 1294
    Helixi133 – 15826
    Helixi162 – 1643
    Beta strandi165 – 1706
    Helixi173 – 18311
    Turni184 – 1863
    Beta strandi188 – 1958
    Turni199 – 2035
    Turni206 – 2083
    Helixi212 – 2143
    Beta strandi215 – 2217
    Beta strandi223 – 2264
    Beta strandi228 – 2303
    Beta strandi234 – 2363
    Beta strandi241 – 2477
    Turni248 – 2514
    Helixi276 – 2783
    Helixi280 – 29415
    Beta strandi298 – 3003
    Helixi307 – 3115
    Turni312 – 3154
    Beta strandi325 – 3273
    Helixi330 – 3323
    Turni334 – 3374
    Beta strandi338 – 3469
    Beta strandi357 – 36913
    Beta strandi371 – 38010
    Beta strandi385 – 39612
    Beta strandi401 – 41010
    Beta strandi417 – 4237
    Beta strandi434 – 44310
    Turni444 – 4463
    Beta strandi449 – 4535
    Beta strandi464 – 4685

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OXEX-ray2.80A/B18-469[»]
    2PVSX-ray3.00A/B18-469[»]
    ProteinModelPortaliP54317.
    SMRiP54317. Positions 18-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54317.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini357 – 469113PLATPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. Lipase family.Curated
    Contains 1 PLAT domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG139430.
    HOVERGENiHBG003243.
    InParanoidiP54317.
    KOiK14075.
    PhylomeDBiP54317.

    Family and domain databases

    Gene3Di2.60.60.20. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR008976. Lipase_LipOase.
    IPR013818. Lipase_N.
    IPR002331. Lipase_panc.
    IPR016272. Lipoprotein_lipase_LIPH.
    IPR001024. PLAT/LH2_dom.
    [Graphical view]
    PANTHERiPTHR11610. PTHR11610. 1 hit.
    PfamiPF00151. Lipase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSiPR00823. PANCLIPASE.
    PR00821. TAGLIPASE.
    SMARTiSM00308. LH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49723. SSF49723. 1 hit.
    SSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P54317-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPPWTLGLL LLATVRGKEV CYGQLGCFSD EKPWAGTLQR PVKLLPWSPE    50
    DIDTRFLLYT NENPNNFQLI TGTEPDTIEA SNFQLDRKTR FIIHGFLDKA 100
    EDSWPSDMCK KMFEVEKVNC ICVDWRHGSR AMYTQAVQNI RVVGAETAFL 150
    IQALSTQLGY SLEDVHVIGH SLGAHTAAEA GRRLGGRVGR ITGLDPAGPC 200
    FQDEPEEVRL DPSDAVFVDV IHTDSSPIVP SLGFGMSQKV GHLDFFPNGG 250
    KEMPGCKKNV LSTITDIDGI WEGIGGFVSC NHLRSFEYYS SSVLNPDGFL 300
    GYPCASYDEF QESKCFPCPA EGCPKMGHYA DQFKGKTSAV EQTFFLNTGE 350
    SGNFTSWRYK VSVTLSGKEK VNGYIRIALY GSNENSKQYE IFKGSLKPDA 400
    SHTCAIDVDF NVGKIQKVKF LWNKRGINLS EPKLGASQIT VQSGEDGTEY 450
    NFCSSDTVEE NVLQSLYPC 469
    Length:469
    Mass (Da):51,947
    Last modified:October 1, 1996 - v1
    Checksum:iD0E130295A94A725
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti239 – 2391K → R in BAF84181. (PubMed:14702039)Curated
    Sequence conflicti352 – 3521G → V in BAF84181. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93284 mRNA. Translation: AAA59533.1.
    AK291492 mRNA. Translation: BAF84181.1.
    CR456949 mRNA. Translation: CAG33230.1.
    CH471066 Genomic DNA. Translation: EAW49448.1.
    BC005989 mRNA. Translation: AAH05989.1.
    PIRiB43357.
    RefSeqiNP_005387.2. NM_005396.4.
    UniGeneiHs.423598.

    Genome annotation databases

    GeneIDi5408.
    KEGGihsa:5408.
    UCSCiuc001lcq.3. human.

    Polymorphism databases

    DMDMi1708840.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93284 mRNA. Translation: AAA59533.1 .
    AK291492 mRNA. Translation: BAF84181.1 .
    CR456949 mRNA. Translation: CAG33230.1 .
    CH471066 Genomic DNA. Translation: EAW49448.1 .
    BC005989 mRNA. Translation: AAH05989.1 .
    PIRi B43357.
    RefSeqi NP_005387.2. NM_005396.4.
    UniGenei Hs.423598.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P54317.
    SMRi P54317. Positions 18-469.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111409. 2 interactions.

    Chemistry

    ChEMBLi CHEMBL2169728.

    Polymorphism databases

    DMDMi 1708840.

    Proteomic databases

    PRIDEi P54317.

    Protocols and materials databases

    DNASUi 5408.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5408.
    KEGGi hsa:5408.
    UCSCi uc001lcq.3. human.

    Organism-specific databases

    CTDi 5408.
    GeneCardsi GC10P118370.
    H-InvDB HIX0009237.
    HGNCi HGNC:9157. PNLIPRP2.
    MIMi 604423. gene.
    neXtProti NX_P54317.
    PharmGKBi PA33480.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG139430.
    HOVERGENi HBG003243.
    InParanoidi P54317.
    KOi K14075.
    PhylomeDBi P54317.

    Enzyme and pathway databases

    Reactomei REACT_9518. Digestion of dietary lipid.

    Miscellaneous databases

    EvolutionaryTracei P54317.
    GenomeRNAii 5408.
    NextBioi 20939.
    PROi P54317.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_PNLIPRP2.
    Genevestigatori P54317.

    Family and domain databases

    Gene3Di 2.60.60.20. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR008976. Lipase_LipOase.
    IPR013818. Lipase_N.
    IPR002331. Lipase_panc.
    IPR016272. Lipoprotein_lipase_LIPH.
    IPR001024. PLAT/LH2_dom.
    [Graphical view ]
    PANTHERi PTHR11610. PTHR11610. 1 hit.
    Pfami PF00151. Lipase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSi PR00823. PANCLIPASE.
    PR00821. TAGLIPASE.
    SMARTi SM00308. LH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49723. SSF49723. 1 hit.
    SSF53474. SSF53474. 1 hit.
    PROSITEi PS00120. LIPASE_SER. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
      Tissue: Pancreas.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pancreas.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pancreas.
    6. "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.
    7. "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.
    8. "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.

    Entry informationi

    Entry nameiLIPR2_HUMAN
    AccessioniPrimary (citable) accession number: P54317
    Secondary accession number(s): A8K627, Q6IB55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3