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Protein

Gastric triacylglycerol lipase

Gene

LIPF

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei172 – 1721Nucleophile1 Publication
Active sitei343 – 3431Charge relay system1 Publication
Active sitei372 – 3721Charge relay system1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Protein family/group databases

ESTHERicanfa-1lipg. Acidic_Lipase.
MEROPSiS33.A57.

Names & Taxonomyi

Protein namesi
Recommended name:
Gastric triacylglycerol lipase (EC:3.1.1.3)
Short name:
GL
Short name:
Gastric lipase
Gene namesi
Name:LIPF
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2169727.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 398379Gastric triacylglycerol lipasePRO_0000017765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...)Sequence analysis
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence analysis
Disulfide bondi246 ↔ 2551 Publication
Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence analysis
Glycosylationi327 – 3271N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP80035.

Interactioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000023039.

Structurei

Secondary structure

1
398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 253Combined sources
Helixi29 – 324Combined sources
Helixi35 – 417Combined sources
Beta strandi47 – 526Combined sources
Beta strandi56 – 649Combined sources
Turni72 – 765Combined sources
Beta strandi79 – 835Combined sources
Helixi90 – 934Combined sources
Beta strandi94 – 963Combined sources
Turni98 – 1003Combined sources
Helixi102 – 1087Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi126 – 1305Combined sources
Turni135 – 1384Combined sources
Helixi142 – 1476Combined sources
Helixi149 – 16113Combined sources
Beta strandi166 – 1716Combined sources
Helixi173 – 18412Combined sources
Helixi186 – 1894Combined sources
Beta strandi192 – 1998Combined sources
Helixi210 – 2156Combined sources
Helixi219 – 2257Combined sources
Beta strandi228 – 2325Combined sources
Helixi236 – 2449Combined sources
Turni245 – 2473Combined sources
Turni249 – 2513Combined sources
Helixi252 – 26312Combined sources
Helixi267 – 2693Combined sources
Helixi272 – 2743Combined sources
Helixi275 – 2795Combined sources
Helixi288 – 30013Combined sources
Helixi311 – 3188Combined sources
Beta strandi319 – 3224Combined sources
Helixi328 – 3303Combined sources
Beta strandi335 – 3406Combined sources
Beta strandi344 – 3463Combined sources
Helixi348 – 3558Combined sources
Beta strandi361 – 3677Combined sources
Helixi374 – 3774Combined sources
Helixi381 – 3844Combined sources
Helixi386 – 3949Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8QX-ray2.70A/B21-396[»]
ProteinModelPortaliP80035.
SMRiP80035. Positions 21-396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80035.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2624. Eukaryota.
COG0596. LUCA.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiP80035.
KOiK14452.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR025483. Lipase_euk.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000862. Steryl_ester_lip. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80035-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLLLTAASV ISTLGTTHGL FGKLHPTNPE VTMNISQMIT YWGYPAEEYE
60 70 80 90 100
VVTEDGYILG IDRIPYGRKN SENIGRRPVA FLQHGLLASA TNWISNLPNN
110 120 130 140 150
SLAFILADAG YDVWLGNSRG NTWARRNLYY SPDSVEFWAF SFDEMAKYDL
160 170 180 190 200
PATIDFILKK TGQDKLHYVG HSQGTTIGFI AFSTNPKLAK RIKTFYALAP
210 220 230 240 250
VATVKYTETL LNKLMLVPSF LFKLIFGNKI FYPHHFFDQF LATEVCSRET
260 270 280 290 300
VDLLCSNALF IICGFDTMNL NMSRLDVYLS HNPAGTSVQN VLHWSQAVKS
310 320 330 340 350
GKFQAFDWGS PVQNMMHYHQ SMPPYYNLTD MHVPIAVWNG GNDLLADPHD
360 370 380 390
VDLLLSKLPN LIYHRKIPPY NHLDFIWAMD APQAVYNEIV SMMGTDNK
Length:398
Mass (Da):45,131
Last modified:July 15, 1998 - v2
Checksum:iE04D62F7518E386C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391I → T AA sequence (PubMed:1935982).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13899 mRNA. Translation: CAA74198.1.
PIRiS19539.
RefSeqiNP_001003209.1. NM_001003209.1.
UniGeneiCfa.3733.

Genome annotation databases

GeneIDi403867.
KEGGicfa:403867.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13899 mRNA. Translation: CAA74198.1.
PIRiS19539.
RefSeqiNP_001003209.1. NM_001003209.1.
UniGeneiCfa.3733.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8QX-ray2.70A/B21-396[»]
ProteinModelPortaliP80035.
SMRiP80035. Positions 21-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000023039.

Chemistry

ChEMBLiCHEMBL2169727.

Protein family/group databases

ESTHERicanfa-1lipg. Acidic_Lipase.
MEROPSiS33.A57.

Proteomic databases

PaxDbiP80035.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403867.
KEGGicfa:403867.

Organism-specific databases

CTDi8513.

Phylogenomic databases

eggNOGiKOG2624. Eukaryota.
COG0596. LUCA.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiP80035.
KOiK14452.

Miscellaneous databases

EvolutionaryTraceiP80035.
PROiP80035.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR025483. Lipase_euk.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000862. Steryl_ester_lip. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-396, ACTIVE SITES, DISULFIDE BOND.

Entry informationi

Entry nameiLIPG_CANLF
AccessioniPrimary (citable) accession number: P80035
Secondary accession number(s): O02857
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 15, 1998
Last modified: June 8, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.