Q91X34 (BAAT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bile acid-CoA:amino acid N-acyltransferase
Short name=BACAT
Short name=BAT
EC=2.3.1.65

Alternative name(s):
Glycine N-choloyltransferase
Long-chain fatty-acyl-CoA hydrolase
EC=3.1.2.2

Gene names

Name:

Baat

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs By similarity.
Catalytic activity	Choloyl-CoA + glycine = CoA + glycocholate. Ref.1 Palmitoyl-CoA + H2O = CoA + palmitate. Ref.1
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity. Peroxisome By similarity. Note: Cytoplasmic or/and peroxisomal By similarity.
Tissue specificity	Highly expressed in liver, kidney, gallbladder, proximal intestine and distal intestine. Weakly expressed in adrenal gland, lung, brain and muscle. Ref.1 Ref.6
Miscellaneous	Mouse BAAT seems to be selective for taurine conjugation of cholyl CoA. In mouse only taurine-conjugated bile acids are found in bile.
Sequence similarities	Belongs to the C/M/P thioester hydrolase family.
Biophysicochemical properties	Kinetic parameters: KM=1.9 mM for taurine
Sequence caution	The sequence AAB58325.1 differs from that shown. Reason: Frameshift at positions 40 and 44. The sequence BAC25534.1 differs from that shown. Reason: Frameshift at position 63.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cytoplasm Peroxisome
Molecular function	Acyltransferase Hydrolase Serine esterase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro bile acid metabolic process Inferred from direct assay Ref.1. Source: MGI fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay Ref.6. Source: UniProtKB peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acyltransferase activity Inferred from direct assay Ref.1. Source: MGI carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW glycine N-choloyltransferase activity Inferred from electronic annotation. Source: EC palmitoyl-CoA hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 420	420	Bile acid-CoA:amino acid N-acyltransferase		PRO_0000202160
Sites
	Active site	235	1	Charge relay system By similarity
	Active site	328	1	Charge relay system By similarity
	Active site	362	1	Charge relay system By similarity
Experimental info
	Sequence conflict	97	1	M → I in AAB58325. Ref.1
	Sequence conflict	117	1	I → L in AAB58325. Ref.1
	Sequence conflict	268	1	H → Q in BAC25534. Ref.2
	Sequence conflict	385	1	S → R in BAC25534. Ref.2
	Sequence conflict	394	1	A → SQ in AAB58325. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q91X34 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: AABC6DB573C5EF50	FASTA	420	46,482
	10 20 30 40 50 60 MAKLTAVPLS ALVDEPVHIQ VTGLAPFQVV CLQASLKDEK GNLFSSQAFY RASEVGEVDL 70 80 90 100 110 120 EHDPSLGGDY MGVHPMGLFW SLKPEKLLGR LIKRDVMNSP YQIHIKACHP YFPLQDIVVS 130 140 150 160 170 180 PPLDSLTLER WYVAPGVKRI QVKESRIRGA LFLPPGEGPF PGVIDLFGGA GGLMEFRASL 190 200 210 220 230 240 LASRGFATLA LAYWNYDDLP SRLEKVDLEY FEEGVEFLLR HPKVLGPGVG ILSVCIGAEI 250 260 270 280 290 300 GLSMAINLKQ IRATVLINGP NFVSQSPHVY HGQVYPPVPS NEEFVVTNAL GLVEFYRTFQ 310 320 330 340 350 360 ETADKDSKYC FPIEKAHGHF LFVVGEDDKN LNSKVHANQA IAQLMKNGKK NWTLLSYPGA 370 380 390 400 410 420 GHLIEPPYTP LCQASRMPIL IPSLSWGGEV IPHAAAQEHS WKEIQKFLKQ HLLPDLSSQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression, and chromosomal localization of mouse liver bile acid CoA:amino acid N-acyltransferase." Falany C.N., Fortinberry H., Leiter E.H., Barnes S. J. Lipid Res. 38:1139-1148(1997) [PubMed: 9215542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Thymus.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Liver.
[6]	"The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine." O'Byrne J., Hunt M.C., Rai D.K., Saeki M., Alexson S.E. J. Biol. Chem. 278:34237-34244(2003) [PubMed: 12810727] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U95215 mRNA. Translation: AAB58325.1. Frameshift. AK017923 mRNA. Translation: BAC25534.1. Frameshift. AL772310 Genomic DNA. Translation: CAM21769.1. CH466565 Genomic DNA. Translation: EDL02319.1. BC012683 mRNA. No translation available.
IPI	IPI00314202.
RefSeq	NP_031545.2. NM_007519.3.
UniGene	Mm.2859.
3D structure databases
ProteinModelPortal	Q91X34.
ModBase	Search...
Protein-protein interaction databases
STRING	Q91X34.
PTM databases
PhosphoSite	Q91X34.
Proteomic databases
PRIDE	Q91X34.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000043056; ENSMUSP00000041983; ENSMUSG00000039653. ENSMUST00000166036; ENSMUSP00000129603; ENSMUSG00000039653.
GeneID	12012.
KEGG	mmu:12012.
UCSC	uc008svt.2. mouse.
Organism-specific databases
CTD	570.
MGI	MGI:106642. Baat.
Phylogenomic databases
GeneTree	ENSGT00390000001046.
HOGENOM	HBG713807.
HOVERGEN	HBG000331.
InParanoid	Q91X34.
OMA	TDLEYFE.
OrthoDB	EOG4B8JD9.
PhylomeDB	Q91X34.
Gene expression databases
ArrayExpress	Q91X34.
Bgee	Q91X34.
Genevestigator	Q91X34.
GermOnline	ENSMUSG00000039653. Mus musculus.
Family and domain databases
InterPro	IPR016662. Acyl-CoA_thioEstase_long-chain. IPR014940. BAAT_C. IPR006862. Thio_Ohase/aa_AcTrfase. [Graphical view]
KO	K00659.
Pfam	PF08840. BAAT_C. 1 hit. PF04775. Bile_Hydr_Trans. 1 hit. [Graphical view]
PIRSF	PIRSF016521. Acyl-CoA_hydro. 1 hit.
ProtoNet	Search...
Other
NextBio	280217.
SOURCE	Search...

Entry information

Entry name

BAAT_MOUSE

Accession

Primary (citable) accession number: Q91X34
Secondary accession number(s): A2AKK7, O08833, Q8C1I3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program