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[1]
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NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=9215542 [NCBI, ExPASy, EBI, Israel, Japan]
Falany C.N.,
Fortinberry H.,
Leiter E.H.,
Barnes S.;
"Cloning, expression, and chromosomal localization of mouse liver bile acid CoA:amino acid N-acyltransferase.";
J. Lipid Res. 38:1139-1148(1997).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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TISSUE SPECIFICITY.
DOI=10.1074/jbc.M300987200; PubMed=12810727 [NCBI, ExPASy, EBI, Israel, Japan]
O'Byrne J.,
Hunt M.C.,
Rai D.K.,
Saeki M.,
Alexson S.E.;
"The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine.";
J. Biol. Chem. 278:34237-34244(2003).
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- 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.
- CATALYTIC ACTIVITY: Palmitoyl-CoA + H2O = CoA + palmitate.
- BIOPHYSICOCHEMICAL PROPERTIES:
- SUBUNIT: 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.
- MISCELLANEOUS: Mouse BAAT seems to be selective for taurine conjugation of cholyl CoA. In mouse only taurine-conjugated bile acids are found in bile.
- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
- SEQUENCE CAUTION:
- Sequence=AAB58325.1; Type=Frameshift; Positions=40, 44;
- Sequence=BAC25534.1; Type=Frameshift; Positions=63;
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Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 420 AA [This is the length of the unprocessed precursor] |
Molecular weight: 46482 Da [This is the MW of the unprocessed precursor] |
CRC64: AABC6DB573C5EF50 [This is a checksum on the sequence] |
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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
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Q91X34 in FASTA format |
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