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P27657 (LIPP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pancreatic triacylglycerol lipase

Short name=PL
Short name=Pancreatic lipase
EC=3.1.1.3
Gene names
Name:Pnlip
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones.

Catalytic activity

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

Subcellular location

Secreted.

Tissue specificity

Pancreatic secretory (zymogen) granule.

Induction

By colipase/CLPS in the presence of bile salts.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.2
Chain17 – 465449Pancreatic triacylglycerol lipase
PRO_0000017788

Regions

Domain355 – 465111PLAT

Sites

Active site1691Nucleophile By similarity
Active site1931Charge relay system By similarity
Active site2801Charge relay system By similarity
Metal binding2041Calcium; via carbonyl oxygen By similarity
Metal binding2071Calcium; via carbonyl oxygen By similarity
Metal binding2091Calcium By similarity
Metal binding2121Calcium By similarity

Amino acid modifications

Disulfide bond20 ↔ 26 By similarity
Disulfide bond107 ↔ 118 By similarity
Disulfide bond254 ↔ 278 By similarity
Disulfide bond302 ↔ 313 By similarity
Disulfide bond316 ↔ 321 By similarity
Disulfide bond449 ↔ 465 By similarity

Sequences

Sequence LengthMass (Da)Tools
P27657 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: CF014D58AA09A6A2

FASTA46551,440
        10         20         30         40         50         60 
MLMLWTFAVL LGAVAGKEVC FDKLGCFSDD APWSGTIDRP LKALPWSPAQ INTRFLLYTN 

        70         80         90        100        110        120 
ENQDNYQKIT SDASSIRNSN FKTNRKTRII IHGFIDKGEE NWLSDMCKNM FKVESVNCIC 

       130        140        150        160        170        180 
VDWKGGSRAT YTQATQNVRV VGAEVALLVN VLKSDLGHPP DNVHLIGHSL GSHVAGEAGK 

       190        200        210        220        230        240 
RTFGAIGRIT GLDAAEPYFQ GTPEEVRLDP TDAQFVDAIH TDAAPIIPNL GFGMSQTVGH 

       250        260        270        280        290        300 
LDFFPNGGME MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFSGF 

       310        320        330        340        350        360 
SCSSYNVFSA NKCFPCGSEG CPQMGHYADK YPGKTKELYQ KFYLNTGDKS NFARWRYQVT 

       370        380        390        400        410        420 
VTLSGQKVTG HILVSLFGNG GNSKQYEVFK GSLHPGDTHV KEFDSDMDVG DLQKVKFIWY 

       430        440        450        460 
NNVINPTLPK VGASRISVER NDGRVFNFCS QDTVREDVLL TLSAC 

« Hide

References

[1]"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].
[2]"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 17-37.
Strain: Sprague-Dawley.
Tissue: Pancreas.
[3]"Hydrolysis of retinyl esters by pancreatic triglyceride lipase."
van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.
Biochemistry 39:4900-4906(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58369 mRNA. Translation: AAA79888.1.
RefSeqNP_037293.1. NM_013161.2.
UniGeneRn.10130.

3D structure databases

ProteinModelPortalP27657.
SMRP27657. Positions 18-465.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP27657.
PRIDEP27657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25702.
KEGGrno:25702.

Organism-specific databases

CTD5406.
RGD3360. Pnlip.

Phylogenomic databases

eggNOGNOG40923.
HOGENOMHOG000038552.
HOVERGENHBG003243.
InParanoidP27657.
KOK14073.
PhylomeDBP27657.

Gene expression databases

GenevestigatorP27657.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 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. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio607735.
PROP27657.

Entry information

Entry nameLIPP_RAT
AccessionPrimary (citable) accession number: P27657
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families