LIPG_MOUSE
ID LIPG_MOUSE Reviewed; 395 AA.
AC Q9CPP7; Q8BK78; Q9CPP8; Q9D6L1; Q9D6L9; Q9D6M9; Q9D6N8; Q9D6P3; Q9D6Q2;
AC Q9D6Q3; Q9D6Q6; Q9D6S5; Q9D6T5; Q9D6X0; Q9D760; Q9D766; Q9D767; Q9D796;
AC Q9D798; Q9D7C5;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Gastric triacylglycerol lipase;
DE Short=GL;
DE Short=Gastric lipase;
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:P07098};
DE Flags: Precursor;
GN Name=Lipf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:BAB26787.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free
CC fatty acids, diacylglycerol, monoacylglycerol, and glycerol (By
CC similarity). Shows a preferential hydrolysis at the sn-3 position of
CC triacylglycerol (By similarity). {ECO:0000250|UniProtKB:P07098}.
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:0000250|UniProtKB:P07098};
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AK009300; BAB26201.1; -; mRNA.
DR EMBL; AK009359; BAB26240.1; -; mRNA.
DR EMBL; AK009413; BAB26272.1; -; mRNA.
DR EMBL; AK009428; BAB26280.1; -; mRNA.
DR EMBL; AK009431; BAB26283.1; -; mRNA.
DR EMBL; AK009437; BAB26287.1; -; mRNA.
DR EMBL; AK009459; BAB26300.1; -; mRNA.
DR EMBL; AK009473; BAB26312.1; -; mRNA.
DR EMBL; AK009474; BAB26313.1; -; mRNA.
DR EMBL; AK009479; BAB26316.1; -; mRNA.
DR EMBL; AK009523; BAB26338.1; -; mRNA.
DR EMBL; AK009525; BAB26339.1; -; mRNA.
DR EMBL; AK009537; BAB26346.1; -; mRNA.
DR EMBL; AK009544; BAB26350.1; -; mRNA.
DR EMBL; AK009546; BAB26352.1; -; mRNA.
DR EMBL; AK009560; BAB26359.1; -; mRNA.
DR EMBL; AK009571; BAB26368.1; -; mRNA.
DR EMBL; AK009573; BAB26370.1; -; mRNA.
DR EMBL; AK009729; BAB26466.1; -; mRNA.
DR EMBL; AK009773; BAB26495.1; -; mRNA.
DR EMBL; AK009875; BAB26556.1; -; mRNA.
DR EMBL; AK009990; BAB26629.1; -; mRNA.
DR EMBL; AK010019; BAB26647.1; -; mRNA.
DR EMBL; AK010026; BAB26651.1; -; mRNA.
DR EMBL; AK010035; BAB26656.1; -; mRNA.
DR EMBL; AK010058; BAB26673.1; -; mRNA.
DR EMBL; AK010061; BAB26675.1; -; mRNA.
DR EMBL; AK010093; BAB26697.1; -; mRNA.
DR EMBL; AK010103; BAB26703.1; -; mRNA.
DR EMBL; AK010106; BAB26704.1; -; mRNA.
DR EMBL; AK010116; BAB26711.1; -; mRNA.
DR EMBL; AK010124; BAB26715.1; -; mRNA.
DR EMBL; AK010125; BAB26716.1; -; mRNA.
DR EMBL; AK010139; BAB26725.1; -; mRNA.
DR EMBL; AK010148; BAB26733.1; -; mRNA.
DR EMBL; AK010173; BAB26746.1; -; mRNA.
DR EMBL; AK010203; BAB26766.1; -; mRNA.
DR EMBL; AK010231; BAB26784.1; -; mRNA.
DR EMBL; AK010236; BAB26787.1; -; mRNA.
DR EMBL; AK075910; BAC36048.1; -; mRNA.
DR EMBL; BC061067; AAH61067.1; -; mRNA.
DR CCDS; CCDS29754.1; -.
DR RefSeq; NP_080610.1; NM_026334.3.
DR RefSeq; XP_017173769.1; XM_017318280.1.
DR AlphaFoldDB; Q9CPP7; -.
DR SMR; Q9CPP7; -.
DR STRING; 10090.ENSMUSP00000025680; -.
DR ESTHER; mouse-1lipg; Acidic_Lipase.
DR MEROPS; S33.A57; -.
DR GlyGen; Q9CPP7; 2 sites.
DR PhosphoSitePlus; Q9CPP7; -.
DR MaxQB; Q9CPP7; -.
DR PaxDb; Q9CPP7; -.
DR PRIDE; Q9CPP7; -.
DR ProteomicsDB; 292095; -.
DR Antibodypedia; 30193; 211 antibodies from 28 providers.
DR DNASU; 67717; -.
DR Ensembl; ENSMUST00000025680; ENSMUSP00000025680; ENSMUSG00000024768.
DR GeneID; 67717; -.
DR KEGG; mmu:67717; -.
DR UCSC; uc008hfw.1; mouse.
DR CTD; 8513; -.
DR MGI; MGI:1914967; Lipf.
DR VEuPathDB; HostDB:ENSMUSG00000024768; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000161066; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; Q9CPP7; -.
DR OMA; HKYWPTY; -.
DR OrthoDB; 651396at2759; -.
DR PhylomeDB; Q9CPP7; -.
DR TreeFam; TF315485; -.
DR Reactome; R-MMU-192456; Digestion of dietary lipid.
DR BioGRID-ORCS; 67717; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q9CPP7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CPP7; protein.
DR Bgee; ENSMUSG00000024768; Expressed in trachea and 12 other tissues.
DR Genevisible; Q9CPP7; MM.
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; IEA:Ensembl.
DR GO; GO:0016615; F:malate dehydrogenase activity; IEA:Ensembl.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006108; P:malate metabolic process; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250|UniProtKB:P07098"
FT CHAIN 19..395
FT /note="Gastric triacylglycerol lipase"
FT /id="PRO_0000017767"
FT DOMAIN 81..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 DISULFID 245..254
FT /evidence="ECO:0000250|UniProtKB:P07098"
FT CONFLICT 46
FT /note="E -> V (in Ref. 1; BAB26703)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="Q -> L (in Ref. 1; BAB26350)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="I -> V (in Ref. 1; BAB26697)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="T -> K (in Ref. 1; BAB26240)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="A -> T (in Ref. 1; BAB26746)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="T -> A (in Ref. 1; BAB26346)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> F (in Ref. 1; BAB26733/BAB26746)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..198
FT /note="LA -> FT (in Ref. 1; BAB26746)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="A -> T (in Ref. 1; BAB26733)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="V -> I (in Ref. 1; BAB26725)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..215
FT /note="SL -> HF (in Ref. 1; BAB26240)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="L -> F (in Ref. 1; BAB26733)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="P -> H (in Ref. 1; BAB26784)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="P -> L (in Ref. 1; BAB26704)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="L -> F (in Ref. 1; BAB26703/BAB26766)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="L -> F (in Ref. 1; BAB26287)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="H -> Y (in Ref. 1; BAB26350)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="F -> L (in Ref. 1; BAB26283)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="D -> G (in Ref. 1; BAB26201/BAB26711)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="G -> P (in Ref. 1; BAC36048)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="Q -> R (in Ref. 1; BAB26556)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="M -> L (in Ref. 1; BAB26784)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="T -> S (in Ref. 1; BAB26629)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="D -> Y (in Ref. 1; BAB26359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 44637 MW; D3F96B65EA671E34 CRC64;
MWLLLVTSVL SAFGGAHGLF GKLGPKNPEA NMNVSQMITY WGYPSEEYEV VTEDGYILGV
YRIPYGKKNS ENIGKRPVAY LQHGLIASAT NWITNLPNNS LAFILADAGY DVWLGNSRGN
TWSRKNVYYS PDSVEFWAFS FDEMAKYDLP ATIDFIVQKT GQEKIHYVGH SQGTTIGFIA
FSTNPALAKK IKRFYALAPV ATVKYTESPF KKISLIPKFL LKVIFGNKMF MPHNYLDQFL
GTEVCSRELL DLLCSNALFI FCGFDKKNLN VSRFDVYLGH NPAGTSTQDL FHWAQLAKSG
KLQAYNWGSP LQNMLHYNQK TPPYYDVSAM TVPIAVWNGG HDILADPQDV AMLLPKLPNL
LYHKEILPYN HLDFIWAMDA PQEVYNEIVT MMAED
