LIPG_RAT
ID LIPG_RAT Reviewed; 395 AA.
AC P04634;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Gastric triacylglycerol lipase;
DE Short=GL;
DE Short=Gastric lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:3839077};
DE AltName: Full=Lingual lipase;
DE Flags: Precursor;
GN Name=Lipf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-50, FUNCTION, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=3839077; DOI=10.1093/nar/13.6.1891;
RA Docherty A.J.P., Bodmer M.W., Angal S., Verger R., Riviere C., Lowe P.A.,
RA Lyons A., Emtage J.S., Harris T.J.R.;
RT "Molecular cloning and nucleotide sequence of rat lingual lipase cDNA.";
RL Nucleic Acids Res. 13:1891-1903(1985).
CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free
CC fatty acids, diacylglycerol, monoacylglycerol, and glycerol
CC (PubMed:3839077). Shows a preferential hydrolysis at the sn-3 position
CC of triacylglycerol (By similarity). {ECO:0000250|UniProtKB:P07098,
CC ECO:0000269|PubMed:3839077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:3839077};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:39931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753;
CC Evidence={ECO:0000250|UniProtKB:P07098};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39932;
CC Evidence={ECO:0000250|UniProtKB:P07098};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-trioctanoylglycerol + H2O = 1,2-dioctanoyl-sn-glycerol +
CC H(+) + octanoate; Xref=Rhea:RHEA:40047, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978,
CC ChEBI:CHEBI:76979; Evidence={ECO:0000250|UniProtKB:P07098};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40048;
CC Evidence={ECO:0000250|UniProtKB:P07098};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P80035}.
CC -!- TISSUE SPECIFICITY: Secreted by the serous (von Ebner's) glands at the
CC back of the rat tongue. {ECO:0000269|PubMed:3839077}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; X02309; CAA26179.1; -; mRNA.
DR PIR; A23045; LIRTT.
DR RefSeq; NP_059037.1; NM_017341.2.
DR AlphaFoldDB; P04634; -.
DR SMR; P04634; -.
DR STRING; 10116.ENSRNOP00000027969; -.
DR ChEMBL; CHEMBL4802004; -.
DR ESTHER; ratno-1lipg; Acidic_Lipase.
DR GlyGen; P04634; 4 sites.
DR PaxDb; P04634; -.
DR Ensembl; ENSRNOT00000027969; ENSRNOP00000027969; ENSRNOG00000019448.
DR GeneID; 50682; -.
DR KEGG; rno:50682; -.
DR UCSC; RGD:708441; rat.
DR CTD; 8513; -.
DR RGD; 708441; Lipf.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000161066; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; P04634; -.
DR OMA; HKYWPTY; -.
DR OrthoDB; 651396at2759; -.
DR PhylomeDB; P04634; -.
DR TreeFam; TF315485; -.
DR Reactome; R-RNO-192456; Digestion of dietary lipid.
DR PRO; PR:P04634; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019448; Expressed in stomach and 1 other tissue.
DR Genevisible; P04634; RN.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0016298; F:lipase activity; TAS:RGD.
DR GO; GO:0016615; F:malate dehydrogenase activity; IDA:MGI.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0007586; P:digestion; TAS:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006108; P:malate metabolic process; IDA:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR039097; Gastric_lipase.
DR InterPro; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005:SF15; PTHR11005:SF15; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:3839077"
FT CHAIN 19..395
FT /note="Gastric triacylglycerol lipase"
FT /id="PRO_0000017768"
FT DOMAIN 77..376
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07098"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 371
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..254
FT /evidence="ECO:0000250|UniProtKB:P07098"
SQ SEQUENCE 395 AA; 44588 MW; E601854A923522EA CRC64;
MWLLLITSVI STFGGAHGLF GKLGPGNPEA NMNISQMITY WGYPCQEYEV VTEDGYILGV
YRIPHGKNNS ENIGKRPVVY LQHGLIASAT NWIANLPNNS LAFMLADAGY DVWLGNSRGN
TWSRKNVYYS PDSVEFWAFS FDEMAKYDLP ATINFIVQKT GQEKIHYVGH SQGTTIGFIA
FSTNPTLAKK IKTFYALAPV ATVKYTQSPL KKISFIPTFL FKLMFGKKMF LPHTYFDDFL
GTEVCSREVL DLLCSNTLFI FCGFDKKNLN VSRFDVYLGH NPAGTSVQDF LHWAQLVRSG
KFQAFNWGSP SQNMLHYNQK TPPEYDVSAM TVPVAVWNGG NDILADPQDV AMLLPKLSNL
LFHKEILAYN HLDFIWAMDA PQEVYNEMIS MMAED
