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Q29458 (LIPG_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 77. 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:
Gastric triacylglycerol lipase

Short name=GL
Short name=Gastric lipase
EC=3.1.1.3
Alternative name(s):
Pregastric esterase
Short name=PGE
Gene names
Name:LIPF
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subcellular location

Secreted.

Miscellaneous

Not inhibited by the thiol reagents 5,5'-dithiobis(2-nitrobenzoic acid) or 4,4'-dithiopyridine.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontriglyceride lipase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 397378Gastric triacylglycerol lipase
PRO_0000017764

Sites

Active site1711Nucleophile By similarity
Active site3421Charge relay system By similarity
Active site3711Charge relay system By similarity

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation3261N-linked (GlcNAc...) Potential
Disulfide bond245 ↔ 254 Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q29458 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F68977DED585EE36

FASTA39745,231
        10         20         30         40         50         60 
MWWLLVTVCF IHMSGNAFCF LGKIAKNPEA SMNVSQMISY WGYPSEMHKV ITADGYILQV 

        70         80         90        100        110        120 
YRIPHGKNNA NHLGQRPVVF LQHGLLGSAT NWISNLPKNS LGFLLADAGY DVWLGNSRGN 

       130        140        150        160        170        180 
TWAQEHLYYS PDSPEFWAFS FDEMAEYDLP STIDFILRRT GQKKLHYVGH SQGTTIGFIA 

       190        200        210        220        230        240 
FSTSPTLAEK IKVFYALAPV ATVKYTKSLF NKLALIPHFL FKIIFGDKMF YPHTFLEQFL 

       250        260        270        280        290        300 
GVEMCSRETL DVLCKNALFA ITGVDNKNFN MSRLDVYIAH NPAGTSVQNT LHWRQAVKSG 

       310        320        330        340        350        360 
KFQAFDWGAP YQNLMHYHQP TPPIYNLTAM NVPIAVWSAD NDLLADPQDV DFLLSKLSNL 

       370        380        390 
IYHKEIPNYN HLDFIWAMDA PQEVYNEIVS LMAEDKK 

« Hide

References

[1]"The cDNA sequence encoding bovine pregastric esterase."
Timmermans M.Y.J., Kupers L.P.M., Teuchy H.
Gene 147:259-262(1994) [PubMed: 7926811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Tongue serous gland.
[2]"Inhibition studies on calf pregastric esterase: the enzyme has no functional thiol group."
Timmermans M.Y.J., Reekmans G., Teuchy H.J.H., Kupers L.P.M.
Biochem. J. 314:931-936(1996) [PubMed: 8615791] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L26319 mRNA. Translation: AAA57037.1.
IPIIPI00706693.
PIRJC4017.
RefSeqNP_776528.1. NM_174103.2.
UniGeneBt.503.

3D structure databases

ProteinModelPortalQ29458.
SMRQ29458. Positions 27-395.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ29458.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281283.
KEGGbta:281283.

Organism-specific databases

CTD8513.

Phylogenomic databases

eggNOGmaNOG18630.
GeneTreeENSGT00550000074328.
HOVERGENHBG006265.
InParanoidQ29458.
OrthoDBEOG43TZVJ.
PhylomeDBQ29458.

Family and domain databases

InterProIPR000073. AB_hydrolase_1.
IPR006693. AB_hydrolase_lipase.
[Graphical view]
KOK14452.
PfamPF04083. Abhydro_lipase. 1 hit.
PF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PROSITEPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLIPG_BOVIN
AccessionPrimary (citable) accession number: Q29458
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 16, 2011
This is version 77 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