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Protein

Gastric triacylglycerol lipase

Gene

LIPF

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei172Nucleophile1 Publication1
Active sitei343Charge relay system1 Publication1
Active sitei372Charge relay system1 Publication1

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 databases

ChEMBLiCHEMBL2169727.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000001776520 – 398Gastric triacylglycerol lipaseAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi34N-linked (GlcNAc...)Sequence analysis1
Glycosylationi99N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi246 ↔ 2551 Publication
Glycosylationi271N-linked (GlcNAc...)Sequence analysis1
Glycosylationi327N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP80035.

Interactioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000023039.

Structurei

Secondary structure

1398
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 25Combined sources3
Helixi29 – 32Combined sources4
Helixi35 – 41Combined sources7
Beta strandi47 – 52Combined sources6
Beta strandi56 – 64Combined sources9
Turni72 – 76Combined sources5
Beta strandi79 – 83Combined sources5
Helixi90 – 93Combined sources4
Beta strandi94 – 96Combined sources3
Turni98 – 100Combined sources3
Helixi102 – 108Combined sources7
Beta strandi112 – 115Combined sources4
Beta strandi126 – 130Combined sources5
Turni135 – 138Combined sources4
Helixi142 – 147Combined sources6
Helixi149 – 161Combined sources13
Beta strandi166 – 171Combined sources6
Helixi173 – 184Combined sources12
Helixi186 – 189Combined sources4
Beta strandi192 – 199Combined sources8
Helixi210 – 215Combined sources6
Helixi219 – 225Combined sources7
Beta strandi228 – 232Combined sources5
Helixi236 – 244Combined sources9
Turni245 – 247Combined sources3
Turni249 – 251Combined sources3
Helixi252 – 263Combined sources12
Helixi267 – 269Combined sources3
Helixi272 – 274Combined sources3
Helixi275 – 279Combined sources5
Helixi288 – 300Combined sources13
Helixi311 – 318Combined sources8
Beta strandi319 – 322Combined sources4
Helixi328 – 330Combined sources3
Beta strandi335 – 340Combined sources6
Beta strandi344 – 346Combined sources3
Helixi348 – 355Combined sources8
Beta strandi361 – 367Combined sources7
Helixi374 – 377Combined sources4
Helixi381 – 384Combined sources4
Helixi386 – 394Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP80035.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 377AB hydrolase-1Sequence analysisAdd BLAST296

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)DescriptionActionsGraphical viewLength
Sequence conflicti39I → T AA sequence (PubMed:1935982).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K8QX-ray2.70A/B21-396[»]
ProteinModelPortaliP80035.
SMRiP80035.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000023039.

Chemistry databases

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...

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: November 2, 2016
This is version 117 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.