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Protein

Pancreatic lipase-related protein 2

Gene

PNLIPRP2

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Acts preferentially on monoglycerides, phospholipids and galactolipids. Contributes to milk fat hydrolysis (By similarity).By similarity

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

Enzyme regulationi

Not inhibited by bile salts or colipase. CLPS stimulates triacylglycerol lipase activity (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei154 – 1541NucleophileBy similarity
Active sitei178 – 1781Charge relay systemPROSITE-ProRule annotationBy similarity
Metal bindingi189 – 1891Calcium; via carbonyl oxygenBy similarity
Metal bindingi192 – 1921Calcium; via carbonyl oxygenBy similarity
Metal bindingi194 – 1941CalciumBy similarity
Metal bindingi197 – 1971CalciumBy similarity
Active sitei247 – 2471Charge relay systemPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.26. 1225.
SABIO-RKP81139.

Protein family/group databases

ESTHERicavpo-2plrp. Pancreatic_lipase.

Chemistry

SwissLipidsiSLP:000001439.

Names & Taxonomyi

Protein namesi
Recommended name:
Pancreatic lipase-related protein 2By similarity (EC:3.1.1.26, EC:3.1.1.3)
Short name:
PL-RP2By similarity
Alternative name(s):
GPL1 Publication
Galactolipase
Gene namesi
Name:PNLIPRP2By similarity
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2169729.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Pancreatic lipase-related protein 2PRO_0000090357Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 10PROSITE-ProRule annotationBy similarity
Disulfide bondi92 ↔ 103PROSITE-ProRule annotationBy similarity
Disulfide bondi239 ↔ 245PROSITE-ProRule annotationBy similarity
Disulfide bondi269 ↔ 280PROSITE-ProRule annotationBy similarity
Disulfide bondi283 ↔ 288PROSITE-ProRule annotationBy similarity
Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi418 ↔ 434PROSITE-ProRule annotationBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Pancreas.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000020465.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi6 – 83Combined sources
Beta strandi9 – 124Combined sources
Beta strandi17 – 237Combined sources
Helixi32 – 354Combined sources
Beta strandi38 – 436Combined sources
Beta strandi46 – 538Combined sources
Helixi58 – 636Combined sources
Beta strandi70 – 767Combined sources
Helixi86 – 9813Combined sources
Beta strandi101 – 1077Combined sources
Helixi109 – 1124Combined sources
Helixi116 – 14126Combined sources
Helixi145 – 1473Combined sources
Beta strandi148 – 1536Combined sources
Helixi155 – 16511Combined sources
Turni166 – 1694Combined sources
Beta strandi171 – 1788Combined sources
Turni182 – 1865Combined sources
Turni189 – 1913Combined sources
Helixi195 – 1973Combined sources
Beta strandi198 – 2047Combined sources
Helixi211 – 2144Combined sources
Beta strandi224 – 2307Combined sources
Helixi231 – 2333Combined sources
Helixi245 – 25915Combined sources
Helixi261 – 2644Combined sources
Helixi272 – 2765Combined sources
Beta strandi290 – 2923Combined sources
Helixi295 – 2973Combined sources
Turni299 – 3024Combined sources
Beta strandi303 – 3119Combined sources
Beta strandi322 – 33211Combined sources
Beta strandi336 – 3405Combined sources
Beta strandi342 – 3487Combined sources
Beta strandi350 – 36112Combined sources
Beta strandi366 – 37510Combined sources
Beta strandi379 – 3813Combined sources
Beta strandi383 – 3875Combined sources
Beta strandi389 – 3924Combined sources
Beta strandi398 – 4047Combined sources
Beta strandi406 – 4083Combined sources
Beta strandi414 – 4185Combined sources
Beta strandi430 – 4334Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPLX-ray2.01A1-434[»]
ProteinModelPortaliP81139.
SMRiP81139. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini322 – 434113PLATPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IHRX. Eukaryota.
ENOG410Y92X. LUCA.
HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiP81139.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[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.

P81139-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AEVCYSHLGC FSDEKPWAGT SQRPIKSLPS DPKKINTRFL LYTNENQNSY
60 70 80 90 100
QLITATDIAT IKASNFNLNR KTRFIIHGFT DSGENSWLSD MCKNMFQVEK
110 120 130 140 150
VNCICVDWKG GSKAQYSQAS QNIRVVGAEV AYLVQVLSTS LNYAPENVHI
160 170 180 190 200
IGHSLGAHTA GEAGKRLNGL VGRITGLDPA EPYFQDTPEE VRLDPSDAKF
210 220 230 240 250
VDVIHTDISP ILPSLGFGMS QKVGHMDFFP NGGKDMPGCK TGISCNHHRS
260 270 280 290 300
IEYYHSSILN PEGFLGYPCA SYDEFQESGC FPCPAKGCPK MGHFADQYPG
310 320 330 340 350
KTNAVEQTFF LNTGASDNFT RWRYKVTVTL SGEKDPSGNI NVALLGKNGN
360 370 380 390 400
SAQYQVFKGT LKPDASYTNS IDVELNVGTI QKVTFLWKRS GISVSKPKMG
410 420 430
ASRITVQSGK DGTKYNFCSS DIVQENVEQT LSPC
Length:434
Mass (Da):47,678
Last modified:January 1, 1998 - v1
Checksum:iE15EED77F3DD59D2
GO

Sequence databases

PIRiA49488.

Cross-referencesi

Sequence databases

PIRiA49488.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPLX-ray2.01A1-434[»]
ProteinModelPortaliP81139.
SMRiP81139. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000020465.

Chemistry

ChEMBLiCHEMBL2169729.
SwissLipidsiSLP:000001439.

Protein family/group databases

ESTHERicavpo-2plrp. Pancreatic_lipase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IHRX. Eukaryota.
ENOG410Y92X. LUCA.
HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiP81139.

Enzyme and pathway databases

BRENDAi3.1.1.26. 1225.
SABIO-RKP81139.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[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]
ProtoNetiSearch...

Publicationsi

  1. "A structural domain (the lid) found in pancreatic lipases is absent in the guinea pig (phospho)lipase."
    Hjorth A., Carriere F., Cudrey C., Woldike H., Boel E., Lawson D.M., Ferrato F., Cambillau C., Dodson G.G., Thim L., Verger R.
    Biochemistry 32:4702-4707(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-23 AND 415-432, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
    Tissue: Pancreas1 Publication.

Entry informationi

Entry nameiLIPR2_CAVPO
AccessioniPrimary (citable) accession number: P81139
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.