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P54318 (LIPR2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Secretory glycoprotein GP-3
Gene names
Name:Pnliprp2
Synonyms:Plrp2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length468 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. Shows a preference for 1,2-didodecanoylphosphatidylethanolamine and 1,2-didodecanoylphosphatidylglycerol, and has low activity towards 1,2-didodecanoylphosphatidylcholine (in vitro). Ref.3

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate. Ref.3

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

Subcellular location

Secreted. Membrane.

Tissue specificity

Pancreatic secretory (zymogen) granule.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Sequence caution

The sequence AAA41250.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentMembrane
Secreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processgalactolipid catabolic process

Inferred from direct assay PubMed 8765145. Source: RGD

phospholipid catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

post-embryonic development

Inferred from expression pattern Ref.2. Source: RGD

response to food

Inferred from expression pattern PubMed 17936733. Source: RGD

response to glucocorticoid stimulus

Inferred from expression pattern PubMed 8967484. Source: RGD

response to peptide hormone stimulus

Inferred from expression pattern PubMed 17010228. Source: RGD

   Cellular_componentextracellular space

Inferred from direct assay PubMed 9748646. Source: RGD

zymogen granule membrane

Inferred from direct assay Ref.1. Source: RGD

   Molecular_functionacylglycerol lipase activity

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

galactolipase activity

Inferred from direct assay PubMed 8765145. Source: RGD

phospholipase activity

Inferred from direct assay PubMed 8656075. Source: RGD

retinyl-palmitate esterase activity

Inferred from electronic annotation. Source: EC

triglyceride lipase activity

Inferred from direct assay PubMed 8656075. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.1
Chain17 – 468452Pancreatic lipase-related protein 2
PRO_0000017796

Regions

Domain356 – 468113PLAT

Sites

Active site1701Nucleophile Ref.3
Active site1941Charge relay system Ref.3
Active site2811Charge relay system Ref.3
Metal binding2051Calcium; via carbonyl oxygen By similarity
Metal binding2081Calcium; via carbonyl oxygen By similarity
Metal binding2101Calcium By similarity
Metal binding2131Calcium By similarity

Amino acid modifications

Glycosylation3521N-linked (GlcNAc...) Ref.3
Disulfide bond20 ↔ 26 Ref.3
Disulfide bond108 ↔ 119 Ref.3
Disulfide bond255 ↔ 279 Ref.3
Disulfide bond303 ↔ 314 Ref.3
Disulfide bond317 ↔ 322 Ref.3
Disulfide bond452 ↔ 468 Ref.3

Secondary structure

1 ............................................................................... 468
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54318 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: B41FB0B339BA9A6F

FASTA46852,535
        10         20         30         40         50         60 
MLLCWIVSLL LATVGGKEVC YGHLGCFSND KPWAGMLQRP LKIFPWSPED IDTRFLLYTN 

        70         80         90        100        110        120 
ENPNNYQKIS ATEPDTIKFS NFQLDRKTRF IVHGFIDKGE DGWLLDMCKK MFQVEKVNCI 

       130        140        150        160        170        180 
CVDWRRGSRT EYTQASYNTR VVGAEIAFLV QVLSTEMGYS PENVHLIGHS LGAHVVGEAG 

       190        200        210        220        230        240 
RRLEGHVGRI TGLDPAEPCF QGLPEEVRLD PSDAMFVDVI HTDSAPIIPY LGFGMSQKVG 

       250        260        270        280        290        300 
HLDFFPNGGK EMPGCQKNIL STIVDINGIW EGTQNFVACN HLRSYKYYAS SILNPDGFLG 

       310        320        330        340        350        360 
YPCSSYEKFQ QNDCFPCPEE GCPKMGHYAD QFEGKTATVE QTVYLNTGDS GNFTRWRYKV 

       370        380        390        400        410        420 
SVTLSGAKKL SGYILVALYG NNGNSKQYEI FKGSLKPEAR HVRDIDVDIN VGEIQKVKFL 

       430        440        450        460 
WNNKVINLFR PTLGASQITV QSGVDGKEYN FCSSDTVRED VLQSLYPC

« Hide

References

[1]"Identification and cloning of GP-3 from rat pancreatic acinar zymogen granules as a glycosylated membrane-associated lipase."
Wishart M.J., Andrews P.C., Nichols R., Blevins G.T. Jr., Logsdon C.D., Williams J.A.
J. Biol. Chem. 268:10303-10311(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-46.
Strain: Sprague-Dawley.
Tissue: Pancreas.
[2]"Rat pancreatic lipase and two related proteins: enzymatic properties and mRNA expression during development."
Payne R.M., Sims H.F., Jennens M.L., Lowe M.E.
Am. J. Physiol. 266:G914-G921(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure and activity of rat pancreatic lipase-related protein 2."
Roussel A., Yang Y., Ferrato F., Verger R., Cambillau C., Lowe M.
J. Biol. Chem. 273:32121-32128(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 17-468, DISULFIDE BONDS, GLYCOSYLATION AT ASN-352, CATALYTIC ACTIVITY, ACTIVE SITE, FUNCTION.
Tissue: Pancreas.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L09216 mRNA. Translation: AAA41250.1. Different initiation.
IPIIPI00947872.
PIRA46696.
RefSeqNP_476554.1. NM_057206.1.
UniGeneRn.87688.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BU8X-ray1.80A17-468[»]
ProteinModelPortalP54318.
SMRP54318. Positions 17-468.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000024223.

Proteomic databases

PaxDbP54318.
PRIDEP54318.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID117554.
KEGGrno:117554.

Organism-specific databases

CTD5408.
RGD620793. Pnliprp2.

Phylogenomic databases

eggNOGNOG40923.
HOVERGENHBG003243.
KOK14075.

Gene expression databases

GenevestigatorP54318.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. LipOase_LH2.
IPR016272. Lipoprotein_lipase_LIPH.
[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. Lipase_LipOase. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54318.
NextBio620403.

Entry information

Entry nameLIPR2_RAT
AccessionPrimary (citable) accession number: P54318
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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