Pancreatic triacylglycerol lipase precursor

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P27657 (LIPP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Pancreatic triacylglycerol lipase
Short name=PL
Short name=Pancreatic lipase
EC=3.1.1.3

Gene names

Name:

Pnlip

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid metabolic process Inferred from direct assay PubMed 15181189. Source: RGD post-embryonic development Inferred from direct assay PubMed 15181189. Source: RGD response to lipid Inferred from expression pattern PubMed 15181189. Source: RGD response to peptide hormone stimulus Inferred from expression pattern PubMed 17010228. Source: RGD
Cellular_component	extracellular space Inferred from direct assay PubMed 17010228 PubMed 8967484. Source: RGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

Ref.2

Chain

17 – 465

449

Pancreatic triacylglycerol lipase

PRO_0000017788

Regions

Domain

355 – 465

111

PLAT

Sites

Active site

169

Nucleophile By similarity

Active site

193

Charge relay system By similarity

Active site

280

Charge relay system By similarity

Metal binding

204

Calcium; via carbonyl oxygen By similarity

Metal binding

207

Calcium; via carbonyl oxygen By similarity

Metal binding

209

Calcium By similarity

Metal binding

212

Calcium By similarity

Amino acid modifications

Disulfide bond

20 ↔ 26

By similarity

Disulfide bond

107 ↔ 118

By similarity

Disulfide bond

254 ↔ 278

By similarity

Disulfide bond

302 ↔ 313

By similarity

Disulfide bond

316 ↔ 321

By similarity

Disulfide bond

449 ↔ 465

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P27657 [UniParc].

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

FASTA

465

51,440

        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

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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.
IPI	IPI00198916.
RefSeq	NP_037293.1. NM_013161.2.
UniGene	Rn.10130.
3D structure databases
ProteinModelPortal	P27657.
SMR	P27657. Positions 18-465.
ModBase	Search...
Proteomic databases
PaxDb	P27657.
PRIDE	P27657.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	25702.
KEGG	rno:25702.
Organism-specific databases
CTD	5406.
RGD	3360. Pnlip.
Phylogenomic databases
eggNOG	NOG40923.
HOGENOM	HOG000038552.
HOVERGEN	HBG003243.
InParanoid	P27657.
KO	K14073.
OrthoDB	EOG4WH8KM.
Gene expression databases
ArrayExpress	P27657.
Genevestigator	P27657.
GermOnline	ENSRNOG00000017725. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.60.20. 1 hit.
InterPro	IPR000734. Lipase. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR002331. Lipase_panc. IPR001024. LipOase_LH2. IPR016272. Lipoprotein_lipase_LIPH. [Graphical view]
PANTHER	PTHR11610. PTHR11610. 1 hit. PTHR11610:SF8. PTHR11610:SF8. 1 hit.
Pfam	PF00151. Lipase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PIRSF	PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTS	PR00823. PANCLIPASE. PR00821. TAGLIPASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
SUPFAM	SSF49723. Lipase_LipOase. 1 hit.
PROSITE	PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	607735.

Entry information

Entry name

LIPP_RAT

Accession

Primary (citable) accession number: P27657

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents