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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)DescriptionActionsGraphical viewLength
Active sitei154NucleophileBy similarity1
Active sitei178Charge relay systemPROSITE-ProRule annotationBy similarity1
Metal bindingi189Calcium; via carbonyl oxygenBy similarity1
Metal bindingi192Calcium; via carbonyl oxygenBy similarity1
Metal bindingi194CalciumBy similarity1
Metal bindingi197CalciumBy similarity1
Active sitei247Charge relay systemPROSITE-ProRule annotationBy similarity1

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 databases

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 databases

ChEMBLiCHEMBL2169729.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000903571 – 434Pancreatic lipase-related protein 2Add BLAST434

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Glycosylationi318N-linked (GlcNAc...)Sequence analysis1
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

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi6 – 8Combined sources3
Beta strandi9 – 12Combined sources4
Beta strandi17 – 23Combined sources7
Helixi32 – 35Combined sources4
Beta strandi38 – 43Combined sources6
Beta strandi46 – 53Combined sources8
Helixi58 – 63Combined sources6
Beta strandi70 – 76Combined sources7
Helixi86 – 98Combined sources13
Beta strandi101 – 107Combined sources7
Helixi109 – 112Combined sources4
Helixi116 – 141Combined sources26
Helixi145 – 147Combined sources3
Beta strandi148 – 153Combined sources6
Helixi155 – 165Combined sources11
Turni166 – 169Combined sources4
Beta strandi171 – 178Combined sources8
Turni182 – 186Combined sources5
Turni189 – 191Combined sources3
Helixi195 – 197Combined sources3
Beta strandi198 – 204Combined sources7
Helixi211 – 214Combined sources4
Beta strandi224 – 230Combined sources7
Helixi231 – 233Combined sources3
Helixi245 – 259Combined sources15
Helixi261 – 264Combined sources4
Helixi272 – 276Combined sources5
Beta strandi290 – 292Combined sources3
Helixi295 – 297Combined sources3
Turni299 – 302Combined sources4
Beta strandi303 – 311Combined sources9
Beta strandi322 – 332Combined sources11
Beta strandi336 – 340Combined sources5
Beta strandi342 – 348Combined sources7
Beta strandi350 – 361Combined sources12
Beta strandi366 – 375Combined sources10
Beta strandi379 – 381Combined sources3
Beta strandi383 – 387Combined sources5
Beta strandi389 – 392Combined sources4
Beta strandi398 – 404Combined sources7
Beta strandi406 – 408Combined sources3
Beta strandi414 – 418Combined sources5
Beta strandi430 – 433Combined sources4

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini322 – 434PLATPROSITE-ProRule annotationAdd BLAST113

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

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013818. Lipase/vitellogenin.
IPR016272. Lipase_LIPH.
IPR033906. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GPLX-ray2.01A1-434[»]
ProteinModelPortaliP81139.
SMRiP81139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000020465.

Chemistry databases

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

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013818. Lipase/vitellogenin.
IPR016272. Lipase_LIPH.
IPR033906. 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...

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: November 30, 2016
This is version 89 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.