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O88354 (LIPP_SPETR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. 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=PTL
Short name=Pancreatic lipase
EC=3.1.1.3
Alternative name(s):
Heart pancreatic lipase
PL-h
Gene names
Name:PNLIP
Synonyms:PTL
OrganismSpermophilus tridecemlineatus (Thirteen-lined ground squirrel) (Ictidomys tridecemlineatus) [Reference proteome]
Taxonomic identifier43179 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiSciuridaeXerinaeMarmotiniIctidomys

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 By similarity. Plays a role in hibernation as a key enzyme that shows high activity at low temperatures. When expressed in the hibernating heart it liberates fatty acids from triglycerides at temperatures as low as 0 degrees Celsius. Ref.1

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed in many tissues with highest expression in liver. During hibernation there is a significant increases in expression in heart, white adipose tissue (WAT), and testis; but not in pancreas. Ref.4

Induction

By colipase/CLPS in the presence of bile salts. Up-regulated during hibernation. Ref.1

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processHibernation
Lipid degradation
Lipid metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhibernation

Inferred from electronic annotation. Source: UniProtKB-KW

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

triglyceride lipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 By similarity
Chain17 – 465449Pancreatic triacylglycerol lipase
PRO_0000250516

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

Experimental info

Sequence conflict1331Q → H in AAD51123. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O88354 [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: A152FB00CD01169B

FASTA46551,227
        10         20         30         40         50         60 
MLLVWSLALL LGAVAGKEVC YDRLGCFSDD SPWSGIVERP LKVLPWSPAD VNTRFLLYTN 

        70         80         90        100        110        120 
ENQDNYQQIT ADSSRIQSSN FKTNRKTRFI IHGFIDKGEE SWLANMCKKM FQVESVNCIC 

       130        140        150        160        170        180 
VDWKGGSRTG YTQASQNIRI VGAEVAYFVD FLRTQLGYSP SNVHVIGHSL GSHAAGEAGR 

       190        200        210        220        230        240 
RTNGAIGRIT GLDPAEPCFE GTPELVRLDP SDAQFVDAIH TDGAPIVPNL GFGMSQTVGH 

       250        260        270        280        290        300 
LDFFPNGGIE MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFAAF 

       310        320        330        340        350        360 
SCASYSVFSA NKCFPCPSGG CPQMGHYADR YSGKTNGVGQ KFYLNTGDKS NFSRWRYKVS 

       370        380        390        400        410        420 
VTLSGQKVTG HILVSLFGNA GNSKQYEIYK GSLHPGYTHS NEFDSDVDVG DLQRVKFIWY 

       430        440        450        460 
NNVINPSLPR VGASSISVER NDGRVFKFCS AETVREDVLL TLNAC 

« Hide

References

[1]"Low-temperature carbon utilization is regulated by novel gene activity in the heart of a hibernating mammal."
Andrews M.T., Squire T.L., Bowen C.M., Rollins M.B.
Proc. Natl. Acad. Sci. U.S.A. 95:8392-8397(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION IN HIBERNATION.
Tissue: Heart.
[2]"Pancreatic triacylglycerol lipase in a hibernating mammal. I. Novel genomic organization."
Squire T.L., Andrews M.T.
Physiol. Genomics 16:119-130(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[3]Bauer V.W., Andrews M.T.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: White adipose tissue.
[4]"Pancreatic triacylglycerol lipase in a hibernating mammal. II. Cold-adapted function and differential expression."
Squire T.L., Lowe M.E., Bauer V.W., Andrews M.T.
Physiol. Genomics 16:131-140(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF027293 mRNA. Translation: AAC40162.2.
AF395870 mRNA. Translation: AAK72259.1.
AF177402 mRNA. Translation: AAD51123.2.
AF177403 mRNA. Translation: AAD51124.1.

3D structure databases

ProteinModelPortalO88354.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000038552.
HOVERGENHBG003243.

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...

Entry information

Entry nameLIPP_SPETR
AccessionPrimary (citable) accession number: O88354
Secondary accession number(s): Q9QWF3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 87 of the entry and version 2 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