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Reviewed, UniProtKB/Swiss-Prot P80035 (LIPG_CANFA)

Last modified January 19, 2010. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Gastric triacylglycerol lipase
      Short name=Gastric lipase
      Short name=GL
    EC=3.1.1.3
Gene names
Name: LIPF
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

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Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subcellular location

Secreted.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

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Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2
Chain20 – 398379Gastric triacylglycerol lipase
PRO_0000017765

Sites

Active site1721Nucleophile
Active site3431Charge relay system
Active site3721Charge relay system

Amino acid modifications

Glycosylation341N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation3271N-linked (GlcNAc...) Potential
Disulfide bond246 ↔ 255

Experimental info

Sequence conflict391I → T AA sequence Ref.2

Secondary structure

1 .............................................................................. 398
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P80035-1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: E04D62F7518E386C

FASTA39845,131
        10         20         30         40         50         60 
MWLLLTAASV ISTLGTTHGL FGKLHPTNPE VTMNISQMIT YWGYPAEEYE VVTEDGYILG 

        70         80         90        100        110        120 
IDRIPYGRKN SENIGRRPVA FLQHGLLASA TNWISNLPNN SLAFILADAG YDVWLGNSRG 

       130        140        150        160        170        180 
NTWARRNLYY SPDSVEFWAF SFDEMAKYDL PATIDFILKK TGQDKLHYVG HSQGTTIGFI 

       190        200        210        220        230        240 
AFSTNPKLAK RIKTFYALAP VATVKYTETL LNKLMLVPSF LFKLIFGNKI FYPHHFFDQF 

       250        260        270        280        290        300 
LATEVCSRET VDLLCSNALF IICGFDTMNL NMSRLDVYLS HNPAGTSVQN VLHWSQAVKS 

       310        320        330        340        350        360 
GKFQAFDWGS PVQNMMHYHQ SMPPYYNLTD MHVPIAVWNG GNDLLADPHD VDLLLSKLPN 

       370        380        390 
LIYHRKIPPY NHLDFIWAMD APQAVYNEIV SMMGTDNK

« Hide

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References

[1]"The complete cDNA sequence encoding dog gastric lipase."
Vaganay S., Joliff G., Bertaux O., Toselli E., Devignes M.D., Benicourt C.
DNA Seq. 8:257-262(1998) [PubMed: 10520456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Stomach.
[2]"Purification and biochemical characterization of dog gastric lipase."
Carriere F., Moreau H., Raphel V., Laugier R., Benicourt C., Junien J.-L., Verger R.
Eur. J. Biochem. 202:75-83(1991) [PubMed: 1935982] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-59.
[3]"Crystal structure of the open form of dog gastric lipase in complex with a phosphonate inhibitor."
Roussel A., Miled N., Berti-Dupuis L., Riviere M., Spinelli S., Berna P., Gruber V., Verger R., Cambillau C.
J. Biol. Chem. 277:2266-2274(2002) [PubMed: 11689574] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-396.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y13899 mRNA. Translation: CAA74198.1.
PIRS19539.
RefSeqNP_001003209.1.
UniGeneCfa.3733

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8QX-ray2.70A/B21-396[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSCAFT00000024834; ENSCAFP00000023039; ENSCAFG00000015682; Canis familiaris. [Genome view]
GeneID403867.
KEGGcfa:403867.

Organism-specific databases

CTD403867.

Phylogenomic databases

eggNOGmaNOG18630.
HOVERGENP80035.
InParanoidP80035.

Enzyme and pathway databases

BRENDA3.1.1.3. 463.

Family and domain databases

InterProIPR006693. AB_hydro-assoc_lipase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamPF04083. Abhydro_lipase. 1 hit.
PF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PROSITEPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLIPG_CANFA
AccessionPrimary (citable) accession number: P80035
Secondary accession number(s): O02857
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 15, 1998
Last modified: January 19, 2010
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents