BAAT_MOUSE
ID BAAT_MOUSE Reviewed; 420 AA.
AC Q91X34; A2AKK7; O08833; Q8C1I3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Bile acid-CoA:amino acid N-acyltransferase;
DE Short=BACAT;
DE Short=BAT;
DE EC=2.3.1.65 {ECO:0000269|PubMed:9215542};
DE AltName: Full=Bile acid-CoA thioesterase {ECO:0000250|UniProtKB:Q14032};
DE AltName: Full=Choloyl-CoA hydrolase;
DE EC=3.1.2.27 {ECO:0000250|UniProtKB:Q14032};
DE AltName: Full=Glycine N-choloyltransferase;
DE AltName: Full=Long-chain fatty-acyl-CoA hydrolase;
DE EC=3.1.2.2 {ECO:0000250|UniProtKB:Q14032};
GN Name=Baat;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9215542;
RA Falany C.N., Fortinberry H., Leiter E.H., Barnes S.;
RT "Cloning, expression, and chromosomal localization of mouse liver bile acid
RT CoA:amino acid N-acyltransferase.";
RL J. Lipid Res. 38:1139-1148(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12810727; DOI=10.1074/jbc.m300987200;
RA O'Byrne J., Hunt M.C., Rai D.K., Saeki M., Alexson S.E.;
RT "The human bile acid-CoA:amino acid N-acyltransferase functions in the
RT conjugation of fatty acids to glycine.";
RL J. Biol. Chem. 278:34237-34244(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-346; LYS-350 AND
RP LYS-409, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the amidation of bile acids (BAs) with the amino
CC acid taurine (PubMed:9215542). Selective for taurine conjugation of
CC cholyl CoA and only taurine-conjugated BAs are found in bile
CC (PubMed:9215542). Amidation of BAs in the liver with taurine prior to
CC their excretion into bile is an important biochemical event in bile
CC acid metabolism (By similarity). This conjugation (or amidation) plays
CC several important biological roles in that it promotes the secretion of
CC BAs and cholesterol into bile and increases the detergent properties of
CC BAs in the intestine, which facilitates lipid and vitamin absorption
CC (By similarity). May also act as an acyl-CoA thioesterase that
CC regulates intracellular levels of free fatty acids (By similarity). In
CC vitro, catalyzes the hydrolysis of long- and very long-chain saturated
CC acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates
CC glycine to these acyl-CoAs (By similarity).
CC {ECO:0000250|UniProtKB:Q14032, ECO:0000269|PubMed:9215542}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + glycine = CoA + glycocholate + H(+);
CC Xref=Rhea:RHEA:14001, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57373; EC=2.3.1.65;
CC Evidence={ECO:0000269|PubMed:9215542};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14002;
CC Evidence={ECO:0000305|PubMed:9215542};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + H2O = cholate + CoA + H(+);
CC Xref=Rhea:RHEA:14541, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373; EC=3.1.2.27;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14542;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA + H(+);
CC Xref=Rhea:RHEA:31511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:36234, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989; EC=3.1.2.27;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31512;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+);
CC Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H2O = CoA + docosanoate + H(+);
CC Xref=Rhea:RHEA:40783, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:23858, ChEBI:CHEBI:57287, ChEBI:CHEBI:65059;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetracosanoyl-CoA = CoA + H(+) + tetracosanoate;
CC Xref=Rhea:RHEA:40787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexacosanoyl-CoA = CoA + H(+) + hexacosanoate;
CC Xref=Rhea:RHEA:40791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31013, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + taurine = CoA + H(+) + taurocholate;
CC Xref=Rhea:RHEA:47100, ChEBI:CHEBI:15378, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47101;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + glycine = CoA + glycochenodeoxycholate
CC + H(+); Xref=Rhea:RHEA:49788, ChEBI:CHEBI:15378, ChEBI:CHEBI:36252,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:62989;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49789;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + taurine = CoA + H(+) +
CC taurochenodeoxycholate; Xref=Rhea:RHEA:49784, ChEBI:CHEBI:9407,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989,
CC ChEBI:CHEBI:507393; Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49785;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + glycine = CoA + H(+) + N-eicosanoylglycinate;
CC Xref=Rhea:RHEA:49792, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57380, ChEBI:CHEBI:87391;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49793;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + hexacosanoyl-CoA = CoA + H(+) + N-
CC hexacosanoylglycine; Xref=Rhea:RHEA:49772, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:64868,
CC ChEBI:CHEBI:87414; Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49773;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + glycine = CoA + H(+) + N-docosanoylglycine;
CC Xref=Rhea:RHEA:49780, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:65059, ChEBI:CHEBI:87410;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49781;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 mM for taurine toward choloyl-CoA
CC {ECO:0000269|PubMed:9215542};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q14032}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q14032}. Peroxisome
CC {ECO:0000250|UniProtKB:Q63276}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, kidney, gallbladder,
CC proximal intestine and distal intestine. Weakly expressed in adrenal
CC gland, lung, brain and muscle. {ECO:0000269|PubMed:12810727,
CC ECO:0000269|PubMed:9215542}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB58325.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC25534.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U95215; AAB58325.1; ALT_FRAME; mRNA.
DR EMBL; AK017923; BAC25534.1; ALT_FRAME; mRNA.
DR EMBL; AL772310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466565; EDL02319.1; -; Genomic_DNA.
DR EMBL; BC012683; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS18173.1; -.
DR RefSeq; NP_031545.2; NM_007519.3.
DR AlphaFoldDB; Q91X34; -.
DR SMR; Q91X34; -.
DR STRING; 10090.ENSMUSP00000041983; -.
DR ESTHER; mouse-BAAT; Acyl-CoA_Thioesterase.
DR MEROPS; S09.A50; -.
DR iPTMnet; Q91X34; -.
DR PhosphoSitePlus; Q91X34; -.
DR SwissPalm; Q91X34; -.
DR jPOST; Q91X34; -.
DR MaxQB; Q91X34; -.
DR PaxDb; Q91X34; -.
DR PeptideAtlas; Q91X34; -.
DR PRIDE; Q91X34; -.
DR ProteomicsDB; 277102; -.
DR Antibodypedia; 14641; 215 antibodies from 29 providers.
DR DNASU; 12012; -.
DR Ensembl; ENSMUST00000043056; ENSMUSP00000041983; ENSMUSG00000039653.
DR Ensembl; ENSMUST00000166036; ENSMUSP00000129603; ENSMUSG00000039653.
DR GeneID; 12012; -.
DR KEGG; mmu:12012; -.
DR UCSC; uc008svt.2; mouse.
DR CTD; 570; -.
DR MGI; MGI:106642; Baat.
DR VEuPathDB; HostDB:ENSMUSG00000039653; -.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR GeneTree; ENSGT01010000222336; -.
DR HOGENOM; CLU_029849_4_0_1; -.
DR InParanoid; Q91X34; -.
DR OMA; LTPFQVV; -.
DR OrthoDB; 1260385at2759; -.
DR PhylomeDB; Q91X34; -.
DR TreeFam; TF314911; -.
DR Reactome; R-MMU-159418; Recycling of bile acids and salts.
DR Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR SABIO-RK; Q91X34; -.
DR BioGRID-ORCS; 12012; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q91X34; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91X34; protein.
DR Bgee; ENSMUSG00000039653; Expressed in left lobe of liver and 19 other tissues.
DR Genevisible; Q91X34; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0033882; F:choloyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047963; F:glycine N-choloyltransferase activity; ISO:MGI.
DR GO; GO:0052816; F:long-chain acyl-CoA hydrolase activity; ISO:MGI.
DR GO; GO:0052815; F:medium-chain acyl-CoA hydrolase activity; ISO:MGI.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016410; F:N-acyltransferase activity; IDA:MGI.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052817; F:very long chain acyl-CoA hydrolase activity; ISO:MGI.
DR GO; GO:0006637; P:acyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISO:MGI.
DR GO; GO:0002152; P:bile acid conjugation; ISO:MGI.
DR GO; GO:0008206; P:bile acid metabolic process; IDA:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006544; P:glycine metabolic process; ISO:MGI.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0019530; P:taurine metabolic process; ISO:MGI.
DR Gene3D; 2.60.40.2240; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR InterPro; IPR014940; BAAT_C.
DR InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Fatty acid metabolism; Hydrolase;
KW Lipid metabolism; Peroxisome; Phosphoprotein; Reference proteome;
KW Serine esterase; Transferase.
FT CHAIN 1..420
FT /note="Bile acid-CoA:amino acid N-acyltransferase"
FT /id="PRO_0000202160"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 362
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63276"
FT MOD_RES 346
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 350
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 409
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63276"
FT CONFLICT 97
FT /note="M -> I (in Ref. 1; AAB58325)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="I -> L (in Ref. 1; AAB58325)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="H -> Q (in Ref. 2; BAC25534)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="S -> R (in Ref. 2; BAC25534)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="A -> SQ (in Ref. 1; AAB58325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46482 MW; AABC6DB573C5EF50 CRC64;
MAKLTAVPLS ALVDEPVHIQ VTGLAPFQVV CLQASLKDEK GNLFSSQAFY RASEVGEVDL
EHDPSLGGDY MGVHPMGLFW SLKPEKLLGR LIKRDVMNSP YQIHIKACHP YFPLQDIVVS
PPLDSLTLER WYVAPGVKRI QVKESRIRGA LFLPPGEGPF PGVIDLFGGA GGLMEFRASL
LASRGFATLA LAYWNYDDLP SRLEKVDLEY FEEGVEFLLR HPKVLGPGVG ILSVCIGAEI
GLSMAINLKQ IRATVLINGP NFVSQSPHVY HGQVYPPVPS NEEFVVTNAL GLVEFYRTFQ
ETADKDSKYC FPIEKAHGHF LFVVGEDDKN LNSKVHANQA IAQLMKNGKK NWTLLSYPGA
GHLIEPPYTP LCQASRMPIL IPSLSWGGEV IPHAAAQEHS WKEIQKFLKQ HLLPDLSSQL
