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P80035 (LIPG_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

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

Protein attributes

Sequence length398 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.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Ontologies

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

Sequences

Sequence LengthMass (Da)Tools
P80035 [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

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y13899 mRNA. Translation: CAA74198.1.
PIRS19539.
RefSeqNP_001003209.1. NM_001003209.1.
UniGeneCfa.3733.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8QX-ray2.70A/B21-396[»]
ProteinModelPortalP80035.
SMRP80035. Positions 21-396.
ModBaseSearch...

Protein-protein interaction databases

STRINGP80035.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403867.
KEGGcfa:403867.

Organism-specific databases

CTD8513.

Phylogenomic databases

eggNOGmaNOG18630.
GeneTreeENSGT00550000074328.
HOVERGENHBG006265.
InParanoidP80035.
OrthoDBEOG43TZVJ.

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_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: November 16, 2011
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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