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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei170 – 1701Nucleophile1 Publication
Active sitei194 – 1941Charge relay systemPROSITE-ProRule annotation1 Publication
Metal bindingi205 – 2051Calcium; via carbonyl oxygenBy similarity
Metal bindingi208 – 2081Calcium; via carbonyl oxygenBy similarity
Metal bindingi210 – 2101CalciumBy similarity
Metal bindingi213 – 2131CalciumBy similarity
Active sitei281 – 2811Charge relay systemPROSITE-ProRule annotation1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Chaini17 – 468452Pancreatic lipase-related protein 2PRO_0000017796Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Glycosylationi352 – 3521N-linked (GlcNAc...)1 Publication
Disulfide bondi452 ↔ 468PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP54318.

Expressioni

Tissue specificityi

Pancreatic secretory (zymogen) granule.

Structurei

Secondary structure

1
468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 203Combined sources
Helixi22 – 243Combined sources
Beta strandi26 – 283Combined sources
Beta strandi33 – 364Combined sources
Helixi48 – 514Combined sources
Beta strandi54 – 596Combined sources
Beta strandi62 – 698Combined sources
Beta strandi71 – 733Combined sources
Helixi75 – 784Combined sources
Beta strandi86 – 927Combined sources
Helixi103 – 11210Combined sources
Beta strandi117 – 1237Combined sources
Helixi125 – 1284Combined sources
Helixi132 – 15726Combined sources
Helixi161 – 1633Combined sources
Beta strandi164 – 1696Combined sources
Helixi172 – 18211Combined sources
Turni183 – 1853Combined sources
Beta strandi187 – 1948Combined sources
Turni198 – 2025Combined sources
Helixi205 – 2073Combined sources
Helixi211 – 2133Combined sources
Beta strandi214 – 2207Combined sources
Helixi227 – 2304Combined sources
Beta strandi240 – 2467Combined sources
Helixi266 – 2705Combined sources
Helixi279 – 29315Combined sources
Helixi295 – 2973Combined sources
Helixi306 – 3105Combined sources
Beta strandi324 – 3263Combined sources
Helixi327 – 3315Combined sources
Turni333 – 3364Combined sources
Beta strandi337 – 3459Combined sources
Beta strandi356 – 36510Combined sources
Beta strandi370 – 38011Combined sources
Beta strandi388 – 3958Combined sources
Beta strandi400 – 40910Combined sources
Beta strandi413 – 42210Combined sources
Beta strandi433 – 44210Combined sources
Turni443 – 4453Combined sources
Beta strandi448 – 4525Combined sources
Beta strandi463 – 4675Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BU8X-ray1.80A17-468[»]
ProteinModelPortaliP54318.
SMRiP54318. Positions 17-468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54318.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini356 – 468113PLATPROSITE-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

HOVERGENiHBG003243.
InParanoidiP54318.
KOiK14075.

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1BU8X-ray1.80A17-468[»]
ProteinModelPortaliP54318.
SMRiP54318. Positions 17-468.
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

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...

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: June 8, 2016
This is version 117 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.