LIPG_BOVIN
ID LIPG_BOVIN Reviewed; 397 AA.
AC Q29458;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Gastric triacylglycerol lipase;
DE Short=GL;
DE Short=Gastric lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:8615791};
DE AltName: Full=Pregastric esterase;
DE Short=PGE;
DE Flags: Precursor;
GN Name=LIPF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tongue serous gland;
RX PubMed=7926811; DOI=10.1016/0378-1119(94)90077-9;
RA Timmermans M.Y.J., Kupers L.P.M., Teuchy H.;
RT "The cDNA sequence encoding bovine pregastric esterase.";
RL Gene 147:259-262(1994).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BOND, FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=8615791; DOI=10.1042/bj3140931;
RA Timmermans M.Y.J., Reekmans G., Teuchy H.J.H., Kupers L.P.M.;
RT "Inhibition studies on calf pregastric esterase: the enzyme has no
RT functional thiol group.";
RL Biochem. J. 314:931-936(1996).
CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free
CC fatty acids, diacylglycerol, monoacylglycerol, and glycerol
CC (PubMed:8615791). Shows a preferential hydrolysis at the sn-3 position
CC of triacylglycerol (By similarity). {ECO:0000250|UniProtKB:P07098,
CC ECO:0000269|PubMed:8615791}.
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:8615791};
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 -!- ACTIVITY REGULATION: Inhibited by diethylp-nitrophenyl phosphate but
CC not inhibited by thiol reagents 5,5'-dithiobis(2-nitrobenzoic acid) or
CC 4,4'-dithiopyridine. {ECO:0000269|PubMed:8615791}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P80035}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; L26319; AAA57037.1; -; mRNA.
DR PIR; JC4017; JC4017.
DR RefSeq; NP_776528.1; NM_174103.2.
DR AlphaFoldDB; Q29458; -.
DR SMR; Q29458; -.
DR STRING; 9913.ENSBTAP00000008453; -.
DR ESTHER; bovin-1lipg; Acidic_Lipase.
DR PaxDb; Q29458; -.
DR GeneID; 281283; -.
DR KEGG; bta:281283; -.
DR CTD; 8513; -.
DR eggNOG; KOG2624; Eukaryota.
DR InParanoid; Q29458; -.
DR OrthoDB; 651396at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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..19
FT /evidence="ECO:0000250|UniProtKB:P07098"
FT CHAIN 20..397
FT /note="Gastric triacylglycerol lipase"
FT /id="PRO_0000017764"
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 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..254
FT /evidence="ECO:0000269|PubMed:8615791"
SQ SEQUENCE 397 AA; 45231 MW; F68977DED585EE36 CRC64;
MWWLLVTVCF IHMSGNAFCF LGKIAKNPEA SMNVSQMISY WGYPSEMHKV ITADGYILQV
YRIPHGKNNA NHLGQRPVVF LQHGLLGSAT NWISNLPKNS LGFLLADAGY DVWLGNSRGN
TWAQEHLYYS PDSPEFWAFS FDEMAEYDLP STIDFILRRT GQKKLHYVGH SQGTTIGFIA
FSTSPTLAEK IKVFYALAPV ATVKYTKSLF NKLALIPHFL FKIIFGDKMF YPHTFLEQFL
GVEMCSRETL DVLCKNALFA ITGVDNKNFN MSRLDVYIAH NPAGTSVQNT LHWRQAVKSG
KFQAFDWGAP YQNLMHYHQP TPPIYNLTAM NVPIAVWSAD NDLLADPQDV DFLLSKLSNL
IYHKEIPNYN HLDFIWAMDA PQEVYNEIVS LMAEDKK
