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P54317 (LIPR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pancreatic lipase-related protein 2

Short name=PL-RP2
EC=3.1.1.26
EC=3.1.1.3
Alternative name(s):
Galactolipase
Gene names
Name:PNLIPRP2
Synonyms:PLRP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Acts preferentially on monoglycerides, phospholipids and galactolipids. Contributes to milk fat hydrolysis. Ref.6 Ref.7 Ref.8

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate. Ref.8

1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates. Ref.8

Subcellular location

Secreted Ref.6 Ref.8.

Tissue specificity

Pancreas.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 469452Pancreatic lipase-related protein 2
PRO_0000017793

Regions

Domain357 – 469113PLAT

Sites

Active site1711Nucleophile Ref.8
Active site1951Charge relay system Ref.8
Active site2821Charge relay system Ref.8
Metal binding2061Calcium; via carbonyl oxygen
Metal binding2091Calcium; via carbonyl oxygen
Metal binding2111Calcium
Metal binding2141Calcium

Amino acid modifications

Glycosylation3531N-linked (GlcNAc...) Ref.8
Glycosylation4281N-linked (GlcNAc...) Potential
Disulfide bond21 ↔ 27 Ref.8
Disulfide bond109 ↔ 120 Ref.8
Disulfide bond256 ↔ 280 Ref.8
Disulfide bond304 ↔ 315 Ref.8
Disulfide bond318 ↔ 323 Ref.8
Disulfide bond453 ↔ 469 Ref.8

Experimental info

Mutagenesis3531N → Q: Loss of N-glycosylation. Ref.8
Sequence conflict2391K → R in BAF84181. Ref.2
Sequence conflict3521G → V in BAF84181. Ref.2

Secondary structure

.......................................................................................... 469
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54317 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D0E130295A94A725

FASTA46951,947
        10         20         30         40         50         60 
MLPPWTLGLL LLATVRGKEV CYGQLGCFSD EKPWAGTLQR PVKLLPWSPE DIDTRFLLYT 

        70         80         90        100        110        120 
NENPNNFQLI TGTEPDTIEA SNFQLDRKTR FIIHGFLDKA EDSWPSDMCK KMFEVEKVNC 

       130        140        150        160        170        180 
ICVDWRHGSR AMYTQAVQNI RVVGAETAFL IQALSTQLGY SLEDVHVIGH SLGAHTAAEA 

       190        200        210        220        230        240 
GRRLGGRVGR ITGLDPAGPC FQDEPEEVRL DPSDAVFVDV IHTDSSPIVP SLGFGMSQKV 

       250        260        270        280        290        300 
GHLDFFPNGG KEMPGCKKNV LSTITDIDGI WEGIGGFVSC NHLRSFEYYS SSVLNPDGFL 

       310        320        330        340        350        360 
GYPCASYDEF QESKCFPCPA EGCPKMGHYA DQFKGKTSAV EQTFFLNTGE SGNFTSWRYK 

       370        380        390        400        410        420 
VSVTLSGKEK VNGYIRIALY GSNENSKQYE IFKGSLKPDA SHTCAIDVDF NVGKIQKVKF 

       430        440        450        460 
LWNKRGINLS EPKLGASQIT VQSGEDGTEY NFCSSDTVEE NVLQSLYPC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB43357.
RefSeqNP_005387.2. NM_005396.4.
UniGeneHs.423598.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OXEX-ray2.80A/B18-469[»]
2PVSX-ray3.00A/B18-469[»]
ProteinModelPortalP54317.
SMRP54317. Positions 18-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111409. 2 interactions.

Chemistry

ChEMBLCHEMBL2169728.

Polymorphism databases

DMDM1708840.

Proteomic databases

PRIDEP54317.

Protocols and materials databases

DNASU5408.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5408.
KEGGhsa:5408.
UCSCuc001lcq.3. human.

Organism-specific databases

CTD5408.
GeneCardsGC10P118370.
H-InvDBHIX0009237.
HGNCHGNC:9157. PNLIPRP2.
MIM604423. gene.
neXtProtNX_P54317.
PharmGKBPA33480.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG139430.
HOVERGENHBG003243.
InParanoidP54317.
KOK14075.
PhylomeDBP54317.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

CleanExHS_PNLIPRP2.
GenevestigatorP54317.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF8. PTHR11610:SF8. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. SSF49723. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54317.
GenomeRNAi5408.
NextBio20939.
PROP54317.
SOURCESearch...

Entry information

Entry nameLIPR2_HUMAN
AccessionPrimary (citable) accession number: P54317
Secondary accession number(s): A8K627, Q6IB55
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM