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Protein

Pancreatic lipase-related protein 2

Gene

Pnliprp2

Organism
Rattus norvegicus (Rat)
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. Shows a preference for 1,2-didodecanoylphosphatidylethanolamine and 1,2-didodecanoylphosphatidylglycerol, and has low activity towards 1,2-didodecanoylphosphatidylcholine (in vitro).By similarity1 Publication

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

CLPS stimulates triacylglycerol lipase activity. Triacylglycerol lipase activity is not inhibited by increasing bile salt concentration.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei170Nucleophile1 Publication1
Active sitei194Charge relay systemPROSITE-ProRule annotation1 Publication1
Metal bindingi205Calcium; via carbonyl oxygenBy similarity1
Metal bindingi208Calcium; via carbonyl oxygenBy similarity1
Metal bindingi210CalciumBy similarity1
Metal bindingi213CalciumBy similarity1
Active sitei281Charge relay systemPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

  • acylglycerol lipase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • galactolipase activity Source: RGD
  • lipase activity Source: RGD
  • phospholipase activity Source: RGD
  • triglyceride lipase activity Source: RGD

GO - Biological processi

  • galactolipid catabolic process Source: RGD
  • phospholipid catabolic process Source: UniProtKB
  • post-embryonic development Source: RGD
  • response to food Source: RGD
  • response to glucocorticoid Source: RGD
  • response to lipid Source: RGD
  • response to peptide hormone Source: RGD
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. 5301.

Protein family/group databases

ESTHERiratno-4plip. Pancreatic_lipase.

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):
Galactolipase
Secretory glycoprotein GP-31 Publication
Gene namesi
Name:Pnliprp2Imported
Synonyms:Plrp2By similarity
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620793. Pnliprp2.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: RGD
  • zymogen granule membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 161 PublicationAdd BLAST16
ChainiPRO_000001779617 – 468Pancreatic lipase-related protein 2Add BLAST452

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi20 ↔ 26PROSITE-ProRule annotation1 Publication
Disulfide bondi108 ↔ 119PROSITE-ProRule annotation1 Publication
Disulfide bondi255 ↔ 279PROSITE-ProRule annotation1 Publication
Disulfide bondi303 ↔ 314PROSITE-ProRule annotation1 Publication
Disulfide bondi317 ↔ 322PROSITE-ProRule annotation1 Publication
Glycosylationi352N-linked (GlcNAc...)1 Publication1
Disulfide bondi452 ↔ 468PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP54318.

Expressioni

Tissue specificityi

Pancreatic secretory (zymogen) granule.

Structurei

Secondary structure

1468
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 20Combined sources3
Helixi22 – 24Combined sources3
Beta strandi26 – 28Combined sources3
Beta strandi33 – 36Combined sources4
Helixi48 – 51Combined sources4
Beta strandi54 – 59Combined sources6
Beta strandi62 – 69Combined sources8
Beta strandi71 – 73Combined sources3
Helixi75 – 78Combined sources4
Beta strandi86 – 92Combined sources7
Helixi103 – 112Combined sources10
Beta strandi117 – 123Combined sources7
Helixi125 – 128Combined sources4
Helixi132 – 157Combined sources26
Helixi161 – 163Combined sources3
Beta strandi164 – 169Combined sources6
Helixi172 – 182Combined sources11
Turni183 – 185Combined sources3
Beta strandi187 – 194Combined sources8
Turni198 – 202Combined sources5
Helixi205 – 207Combined sources3
Helixi211 – 213Combined sources3
Beta strandi214 – 220Combined sources7
Helixi227 – 230Combined sources4
Beta strandi240 – 246Combined sources7
Helixi266 – 270Combined sources5
Helixi279 – 293Combined sources15
Helixi295 – 297Combined sources3
Helixi306 – 310Combined sources5
Beta strandi324 – 326Combined sources3
Helixi327 – 331Combined sources5
Turni333 – 336Combined sources4
Beta strandi337 – 345Combined sources9
Beta strandi356 – 365Combined sources10
Beta strandi370 – 380Combined sources11
Beta strandi388 – 395Combined sources8
Beta strandi400 – 409Combined sources10
Beta strandi413 – 422Combined sources10
Beta strandi433 – 442Combined sources10
Turni443 – 445Combined sources3
Beta strandi448 – 452Combined sources5
Beta strandi463 – 467Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BU8X-ray1.80A17-468[»]
ProteinModelPortaliP54318.
SMRiP54318.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54318.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini356 – 468PLATPROSITE-ProRule annotationAdd BLAST113

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG003243.
InParanoidiP54318.
KOiK14075.

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.

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

P54318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLCWIVSLL LATVGGKEVC YGHLGCFSND KPWAGMLQRP LKIFPWSPED
60 70 80 90 100
IDTRFLLYTN ENPNNYQKIS ATEPDTIKFS NFQLDRKTRF IVHGFIDKGE
110 120 130 140 150
DGWLLDMCKK MFQVEKVNCI CVDWRRGSRT EYTQASYNTR VVGAEIAFLV
160 170 180 190 200
QVLSTEMGYS PENVHLIGHS LGAHVVGEAG RRLEGHVGRI TGLDPAEPCF
210 220 230 240 250
QGLPEEVRLD PSDAMFVDVI HTDSAPIIPY LGFGMSQKVG HLDFFPNGGK
260 270 280 290 300
EMPGCQKNIL STIVDINGIW EGTQNFVACN HLRSYKYYAS SILNPDGFLG
310 320 330 340 350
YPCSSYEKFQ QNDCFPCPEE GCPKMGHYAD QFEGKTATVE QTVYLNTGDS
360 370 380 390 400
GNFTRWRYKV SVTLSGAKKL SGYILVALYG NNGNSKQYEI FKGSLKPEAR
410 420 430 440 450
HVRDIDVDIN VGEIQKVKFL WNNKVINLFR PTLGASQITV QSGVDGKEYN
460
FCSSDTVRED VLQSLYPC
Length:468
Mass (Da):52,535
Last modified:October 1, 1996 - v1
Checksum:iB41FB0B339BA9A6F
GO

Sequence cautioni

The sequence AAA41250 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09216 mRNA. Translation: AAA41250.1. Different initiation.
PIRiA46696.
RefSeqiNP_476554.1. NM_057206.1.
UniGeneiRn.87688.

Genome annotation databases

GeneIDi117554.
KEGGirno:117554.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09216 mRNA. Translation: AAA41250.1. Different initiation.
PIRiA46696.
RefSeqiNP_476554.1. NM_057206.1.
UniGeneiRn.87688.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BU8X-ray1.80A17-468[»]
ProteinModelPortaliP54318.
SMRiP54318.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiratno-4plip. Pancreatic_lipase.

Proteomic databases

PRIDEiP54318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi117554.
KEGGirno:117554.

Organism-specific databases

CTDi5408.
RGDi620793. Pnliprp2.

Phylogenomic databases

HOVERGENiHBG003243.
InParanoidiP54318.
KOiK14075.

Enzyme and pathway databases

BRENDAi3.1.1.26. 5301.

Miscellaneous databases

EvolutionaryTraceiP54318.
PROiP54318.

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_RAT
AccessioniPrimary (citable) accession number: P54318
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
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

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.