Full text data of ACOT7
ACOT7
(BACH)
[Confidence: low (only semi-automatic identification from reviews)]
Cytosolic acyl coenzyme A thioester hydrolase; 3.1.2.2 (Acyl-CoA thioesterase 7; Brain acyl-CoA hydrolase; BACH; CTE-IIa; CTE-II; Long chain acyl-CoA thioester hydrolase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cytosolic acyl coenzyme A thioester hydrolase; 3.1.2.2 (Acyl-CoA thioesterase 7; Brain acyl-CoA hydrolase; BACH; CTE-IIa; CTE-II; Long chain acyl-CoA thioester hydrolase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O00154
ID BACH_HUMAN Reviewed; 380 AA.
AC O00154; A8K0K7; A8K232; A8K6B8; A8K837; B3KQ12; O43703; Q53Y78;
read moreAC Q5JYL2; Q5JYL3; Q5JYL4; Q5JYL5; Q5JYL6; Q5TGR4; Q9UJM9; Q9Y539;
AC Q9Y540;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 3.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=Cytosolic acyl coenzyme A thioester hydrolase;
DE EC=3.1.2.2;
DE AltName: Full=Acyl-CoA thioesterase 7;
DE AltName: Full=Brain acyl-CoA hydrolase;
DE Short=BACH;
DE AltName: Full=CTE-IIa;
DE Short=CTE-II;
DE AltName: Full=Long chain acyl-CoA thioester hydrolase;
GN Name=ACOT7; Synonyms=BACH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=10578051;
RA Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T.,
RA Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K.,
RA Endo T., Suga T.;
RT "Purification, molecular cloning, and genomic organization of human
RT brain long-chain acyl-CoA hydrolase.";
RL J. Biochem. 126:1013-1019(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 5 AND 6), SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12435388; DOI=10.1016/S0006-291X(02)02587-1;
RA Yamada J., Kuramochi Y., Takagi M., Watanabe T., Suga T.;
RT "Human brain acyl-CoA hydrolase isoforms encoded by a single gene.";
RL Biochem. Biophys. Res. Commun. 299:49-56(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Hippocampus;
RA Hajra A.K., Uhler M.D., Larkins L.K.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4; 5; 6 AND 7).
RC TISSUE=Cerebellum, Colon, Placenta, Stomach, and Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 79-90, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168; LYS-198 AND LYS-283,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 209-378.
RG Structural genomics consortium (SGC);
RT "Human acyl-CoA thioesterase 7.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that
CC catalyze the hydrolysis of acyl-CoAs to the free fatty acid and
CC coenzyme A (CoASH), providing the potential to regulate
CC intracellular levels of acyl-CoAs, free fatty acids and CoASH. May
CC play an important physiological function in brain. May play a
CC regulatory role by modulating the cellular levels of fatty acyl-
CC CoA ligands for certain transcription factors as well as the
CC substrates for fatty acid metabolizing enzymes, contributing to
CC lipid homeostasis. Has broad specificity, active towards fatty
CC acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity
CC toward palmitoyl-CoA.
CC -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + H(2)O = CoA + palmitate.
CC -!- SUBUNIT: Homohexamer (By similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: Isoform 6: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: Isoform 5: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=B, HBACHb;
CC IsoId=O00154-1; Sequence=Displayed;
CC Name=2; Synonyms=A-X, hBACHa-X;
CC IsoId=O00154-2; Sequence=VSP_000152, VSP_000155, VSP_000156;
CC Name=3; Synonyms=A-Xi, hBACHa-Xi;
CC IsoId=O00154-3; Sequence=VSP_000152, VSP_000154;
CC Name=4; Synonyms=A, hBACHa;
CC IsoId=O00154-4; Sequence=VSP_000152;
CC Note=Major isoform;
CC Name=5; Synonyms=C, hBACHc;
CC IsoId=O00154-5; Sequence=VSP_000151;
CC Name=6; Synonyms=D, hBACHd;
CC IsoId=O00154-6; Sequence=VSP_000153;
CC Name=7;
CC IsoId=O00154-7; Sequence=VSP_047094;
CC -!- TISSUE SPECIFICITY: Isoform 4 is expressed exclusively in brain.
CC -!- DOMAIN: Both hydrolase domains are required for efficient activity
CC (By similarity).
CC -!- SIMILARITY: Contains 2 acyl coenzyme A hydrolase domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61211.1; Type=Frameshift; Positions=371;
CC Sequence=AAH17365.2; Type=Erroneous initiation;
CC Sequence=CAI19435.1; Type=Erroneous initiation;
CC Sequence=CAI19774.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D88894; BAA24350.1; -; mRNA.
DR EMBL; AB074415; BAC20174.1; -; mRNA.
DR EMBL; AB074416; BAC20175.1; -; mRNA.
DR EMBL; AB074417; BAC20176.1; -; mRNA.
DR EMBL; AB074418; BAC20177.1; -; mRNA.
DR EMBL; AB074419; BAC20178.1; -; mRNA.
DR EMBL; U91316; AAB61211.1; ALT_FRAME; mRNA.
DR EMBL; BT006888; AAP35534.1; -; mRNA.
DR EMBL; AK289572; BAF82261.1; -; mRNA.
DR EMBL; AK290097; BAF82786.1; -; mRNA.
DR EMBL; AK291583; BAF84272.1; -; mRNA.
DR EMBL; AK292202; BAF84891.1; -; mRNA.
DR EMBL; AK057168; BAG51874.1; -; mRNA.
DR EMBL; AL031847; CAI19440.1; -; Genomic_DNA.
DR EMBL; AL031848; CAI19440.1; JOINED; Genomic_DNA.
DR EMBL; AL031847; CAI19435.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL031848; CAI19435.1; JOINED; Genomic_DNA.
DR EMBL; AL031847; CAI19442.1; -; Genomic_DNA.
DR EMBL; AL031848; CAI19442.1; JOINED; Genomic_DNA.
DR EMBL; AL031847; CAI19443.1; -; Genomic_DNA.
DR EMBL; AL031848; CAI19443.1; JOINED; Genomic_DNA.
DR EMBL; AL031848; CAI19774.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL031847; CAI19774.1; JOINED; Genomic_DNA.
DR EMBL; AL031848; CAI19777.1; -; Genomic_DNA.
DR EMBL; AL031847; CAI19777.1; JOINED; Genomic_DNA.
DR EMBL; AL031848; CAI19778.1; -; Genomic_DNA.
DR EMBL; AL031847; CAI19778.1; JOINED; Genomic_DNA.
DR EMBL; AL031848; CAI19779.1; -; Genomic_DNA.
DR EMBL; AL031847; CAI19779.1; JOINED; Genomic_DNA.
DR EMBL; CH471130; EAW71528.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71529.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71530.1; -; Genomic_DNA.
DR EMBL; BC017365; AAH17365.2; ALT_INIT; mRNA.
DR PIR; JC7161; JC7161.
DR RefSeq; NP_009205.3; NM_007274.3.
DR RefSeq; NP_863654.1; NM_181864.2.
DR RefSeq; NP_863655.1; NM_181865.2.
DR RefSeq; NP_863656.1; NM_181866.2.
DR UniGene; Hs.126137; -.
DR PDB; 2QQ2; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=209-378.
DR PDBsum; 2QQ2; -.
DR ProteinModelPortal; O00154; -.
DR SMR; O00154; 52-373.
DR IntAct; O00154; 2.
DR MINT; MINT-2869715; -.
DR PhosphoSite; O00154; -.
DR UCD-2DPAGE; O00154; -.
DR PaxDb; O00154; -.
DR PRIDE; O00154; -.
DR DNASU; 11332; -.
DR Ensembl; ENST00000361521; ENSP00000354615; ENSG00000097021.
DR Ensembl; ENST00000377842; ENSP00000367073; ENSG00000097021.
DR Ensembl; ENST00000377845; ENSP00000367076; ENSG00000097021.
DR Ensembl; ENST00000377855; ENSP00000367086; ENSG00000097021.
DR Ensembl; ENST00000377860; ENSP00000367091; ENSG00000097021.
DR Ensembl; ENST00000418124; ENSP00000402532; ENSG00000097021.
DR GeneID; 11332; -.
DR KEGG; hsa:11332; -.
DR UCSC; uc001amt.3; human.
DR CTD; 11332; -.
DR GeneCards; GC01M006324; -.
DR HGNC; HGNC:24157; ACOT7.
DR HPA; HPA025735; -.
DR HPA; HPA025762; -.
DR MIM; 602587; gene.
DR neXtProt; NX_O00154; -.
DR PharmGKB; PA142672655; -.
DR eggNOG; COG1607; -.
DR HOVERGEN; HBG036928; -.
DR InParanoid; O00154; -.
DR KO; K17360; -.
DR OMA; ANKAALW; -.
DR OrthoDB; EOG7QZGB2; -.
DR PhylomeDB; O00154; -.
DR BRENDA; 3.1.2.2; 2681.
DR SABIO-RK; O00154; -.
DR ChiTaRS; ACOT7; human.
DR EvolutionaryTrace; O00154; -.
DR GeneWiki; ACOT7; -.
DR GenomeRNAi; 11332; -.
DR NextBio; 35469290; -.
DR PRO; PR:O00154; -.
DR ArrayExpress; O00154; -.
DR Bgee; O00154; -.
DR Genevestigator; O00154; -.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; TAS:ProtInc.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0009062; P:fatty acid catabolic process; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR InterPro; IPR006683; Thioestr_supf.
DR Pfam; PF03061; 4HBT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Mitochondrion;
KW Reference proteome; Repeat; Serine esterase.
FT CHAIN 1 380 Cytosolic acyl coenzyme A thioester
FT hydrolase.
FT /FTId=PRO_0000053806.
FT DOMAIN 56 151 Acyl coenzyme A hydrolase 1.
FT DOMAIN 242 319 Acyl coenzyme A hydrolase 2.
FT ACT_SITE 66 66 By similarity.
FT ACT_SITE 255 255 By similarity.
FT MOD_RES 168 168 N6-acetyllysine.
FT MOD_RES 198 198 N6-acetyllysine.
FT MOD_RES 283 283 N6-acetyllysine.
FT VAR_SEQ 1 58 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
FT VGPRADLPPCGACITGR -> MLLLRRSLSLNVLRKEVDRA
FT CFGEKAKQ (in isoform 5).
FT /FTId=VSP_000151.
FT VAR_SEQ 1 57 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
FT VGPRADLPPCGACITG -> MSGPDVETPSAIQIC (in
FT isoform 2, isoform 3 and isoform 4).
FT /FTId=VSP_000152.
FT VAR_SEQ 1 57 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
FT VGPRADLPPCGACITG -> MAFQLS (in isoform
FT 6).
FT /FTId=VSP_000153.
FT VAR_SEQ 1 57 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
FT VGPRADLPPCGACITG -> MARPGLIHSAPGLPDTCALLQ
FT PPAASAAAAPSMSGPDVETPSAIQIC (in isoform
FT 7).
FT /FTId=VSP_047094.
FT VAR_SEQ 287 380 GCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAAS
FT AFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQM
FT KAKRQGHAEPQP -> AHVMPAGADHTAPSSSPSTGTKCSL
FT LRHHHLGTHDLHEQ (in isoform 3).
FT /FTId=VSP_000154.
FT VAR_SEQ 287 288 GC -> AP (in isoform 2).
FT /FTId=VSP_000155.
FT VAR_SEQ 289 380 Missing (in isoform 2).
FT /FTId=VSP_000156.
FT CONFLICT 82 82 E -> G (in Ref. 5; BAG51874).
FT CONFLICT 371 372 KR -> DD (in Ref. 3; AAB61211).
FT CONFLICT 377 378 EP -> DA (in Ref. 3; AAB61211).
FT HELIX 223 226
FT STRAND 228 233
FT HELIX 236 238
FT STRAND 241 245
FT HELIX 247 266
FT STRAND 267 280
FT STRAND 288 299
FT STRAND 301 314
FT STRAND 323 335
FT HELIX 352 371
SQ SEQUENCE 380 AA; 41796 MW; BDD75D62A60095BC CRC64;
MKLLARALRL CEFGRQASSR RLVAGQGCVG PRRGCCAPVQ VVGPRADLPP CGACITGRIM
RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC VAALARVERT DFLSPMCIGE
VAHVSAEITY TSKHSVEVQV NVMSENILTG AKKLTNKATL WYVPLSLKNV DKVLEVPPVV
YSRQEQEEEG RKRYEAQKLE RMETKWRNGD IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT
LHGFVHGGVT MKLMDEVAGI VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS
NKSMEIEVLV DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE
GKGRYLQMKA KRQGHAEPQP
//
ID BACH_HUMAN Reviewed; 380 AA.
AC O00154; A8K0K7; A8K232; A8K6B8; A8K837; B3KQ12; O43703; Q53Y78;
read moreAC Q5JYL2; Q5JYL3; Q5JYL4; Q5JYL5; Q5JYL6; Q5TGR4; Q9UJM9; Q9Y539;
AC Q9Y540;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 3.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=Cytosolic acyl coenzyme A thioester hydrolase;
DE EC=3.1.2.2;
DE AltName: Full=Acyl-CoA thioesterase 7;
DE AltName: Full=Brain acyl-CoA hydrolase;
DE Short=BACH;
DE AltName: Full=CTE-IIa;
DE Short=CTE-II;
DE AltName: Full=Long chain acyl-CoA thioester hydrolase;
GN Name=ACOT7; Synonyms=BACH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=10578051;
RA Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T.,
RA Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K.,
RA Endo T., Suga T.;
RT "Purification, molecular cloning, and genomic organization of human
RT brain long-chain acyl-CoA hydrolase.";
RL J. Biochem. 126:1013-1019(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 5 AND 6), SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12435388; DOI=10.1016/S0006-291X(02)02587-1;
RA Yamada J., Kuramochi Y., Takagi M., Watanabe T., Suga T.;
RT "Human brain acyl-CoA hydrolase isoforms encoded by a single gene.";
RL Biochem. Biophys. Res. Commun. 299:49-56(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Hippocampus;
RA Hajra A.K., Uhler M.D., Larkins L.K.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4; 5; 6 AND 7).
RC TISSUE=Cerebellum, Colon, Placenta, Stomach, and Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 79-90, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168; LYS-198 AND LYS-283,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 209-378.
RG Structural genomics consortium (SGC);
RT "Human acyl-CoA thioesterase 7.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that
CC catalyze the hydrolysis of acyl-CoAs to the free fatty acid and
CC coenzyme A (CoASH), providing the potential to regulate
CC intracellular levels of acyl-CoAs, free fatty acids and CoASH. May
CC play an important physiological function in brain. May play a
CC regulatory role by modulating the cellular levels of fatty acyl-
CC CoA ligands for certain transcription factors as well as the
CC substrates for fatty acid metabolizing enzymes, contributing to
CC lipid homeostasis. Has broad specificity, active towards fatty
CC acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity
CC toward palmitoyl-CoA.
CC -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + H(2)O = CoA + palmitate.
CC -!- SUBUNIT: Homohexamer (By similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: Isoform 6: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: Isoform 5: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=B, HBACHb;
CC IsoId=O00154-1; Sequence=Displayed;
CC Name=2; Synonyms=A-X, hBACHa-X;
CC IsoId=O00154-2; Sequence=VSP_000152, VSP_000155, VSP_000156;
CC Name=3; Synonyms=A-Xi, hBACHa-Xi;
CC IsoId=O00154-3; Sequence=VSP_000152, VSP_000154;
CC Name=4; Synonyms=A, hBACHa;
CC IsoId=O00154-4; Sequence=VSP_000152;
CC Note=Major isoform;
CC Name=5; Synonyms=C, hBACHc;
CC IsoId=O00154-5; Sequence=VSP_000151;
CC Name=6; Synonyms=D, hBACHd;
CC IsoId=O00154-6; Sequence=VSP_000153;
CC Name=7;
CC IsoId=O00154-7; Sequence=VSP_047094;
CC -!- TISSUE SPECIFICITY: Isoform 4 is expressed exclusively in brain.
CC -!- DOMAIN: Both hydrolase domains are required for efficient activity
CC (By similarity).
CC -!- SIMILARITY: Contains 2 acyl coenzyme A hydrolase domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61211.1; Type=Frameshift; Positions=371;
CC Sequence=AAH17365.2; Type=Erroneous initiation;
CC Sequence=CAI19435.1; Type=Erroneous initiation;
CC Sequence=CAI19774.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D88894; BAA24350.1; -; mRNA.
DR EMBL; AB074415; BAC20174.1; -; mRNA.
DR EMBL; AB074416; BAC20175.1; -; mRNA.
DR EMBL; AB074417; BAC20176.1; -; mRNA.
DR EMBL; AB074418; BAC20177.1; -; mRNA.
DR EMBL; AB074419; BAC20178.1; -; mRNA.
DR EMBL; U91316; AAB61211.1; ALT_FRAME; mRNA.
DR EMBL; BT006888; AAP35534.1; -; mRNA.
DR EMBL; AK289572; BAF82261.1; -; mRNA.
DR EMBL; AK290097; BAF82786.1; -; mRNA.
DR EMBL; AK291583; BAF84272.1; -; mRNA.
DR EMBL; AK292202; BAF84891.1; -; mRNA.
DR EMBL; AK057168; BAG51874.1; -; mRNA.
DR EMBL; AL031847; CAI19440.1; -; Genomic_DNA.
DR EMBL; AL031848; CAI19440.1; JOINED; Genomic_DNA.
DR EMBL; AL031847; CAI19435.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL031848; CAI19435.1; JOINED; Genomic_DNA.
DR EMBL; AL031847; CAI19442.1; -; Genomic_DNA.
DR EMBL; AL031848; CAI19442.1; JOINED; Genomic_DNA.
DR EMBL; AL031847; CAI19443.1; -; Genomic_DNA.
DR EMBL; AL031848; CAI19443.1; JOINED; Genomic_DNA.
DR EMBL; AL031848; CAI19774.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL031847; CAI19774.1; JOINED; Genomic_DNA.
DR EMBL; AL031848; CAI19777.1; -; Genomic_DNA.
DR EMBL; AL031847; CAI19777.1; JOINED; Genomic_DNA.
DR EMBL; AL031848; CAI19778.1; -; Genomic_DNA.
DR EMBL; AL031847; CAI19778.1; JOINED; Genomic_DNA.
DR EMBL; AL031848; CAI19779.1; -; Genomic_DNA.
DR EMBL; AL031847; CAI19779.1; JOINED; Genomic_DNA.
DR EMBL; CH471130; EAW71528.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71529.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71530.1; -; Genomic_DNA.
DR EMBL; BC017365; AAH17365.2; ALT_INIT; mRNA.
DR PIR; JC7161; JC7161.
DR RefSeq; NP_009205.3; NM_007274.3.
DR RefSeq; NP_863654.1; NM_181864.2.
DR RefSeq; NP_863655.1; NM_181865.2.
DR RefSeq; NP_863656.1; NM_181866.2.
DR UniGene; Hs.126137; -.
DR PDB; 2QQ2; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=209-378.
DR PDBsum; 2QQ2; -.
DR ProteinModelPortal; O00154; -.
DR SMR; O00154; 52-373.
DR IntAct; O00154; 2.
DR MINT; MINT-2869715; -.
DR PhosphoSite; O00154; -.
DR UCD-2DPAGE; O00154; -.
DR PaxDb; O00154; -.
DR PRIDE; O00154; -.
DR DNASU; 11332; -.
DR Ensembl; ENST00000361521; ENSP00000354615; ENSG00000097021.
DR Ensembl; ENST00000377842; ENSP00000367073; ENSG00000097021.
DR Ensembl; ENST00000377845; ENSP00000367076; ENSG00000097021.
DR Ensembl; ENST00000377855; ENSP00000367086; ENSG00000097021.
DR Ensembl; ENST00000377860; ENSP00000367091; ENSG00000097021.
DR Ensembl; ENST00000418124; ENSP00000402532; ENSG00000097021.
DR GeneID; 11332; -.
DR KEGG; hsa:11332; -.
DR UCSC; uc001amt.3; human.
DR CTD; 11332; -.
DR GeneCards; GC01M006324; -.
DR HGNC; HGNC:24157; ACOT7.
DR HPA; HPA025735; -.
DR HPA; HPA025762; -.
DR MIM; 602587; gene.
DR neXtProt; NX_O00154; -.
DR PharmGKB; PA142672655; -.
DR eggNOG; COG1607; -.
DR HOVERGEN; HBG036928; -.
DR InParanoid; O00154; -.
DR KO; K17360; -.
DR OMA; ANKAALW; -.
DR OrthoDB; EOG7QZGB2; -.
DR PhylomeDB; O00154; -.
DR BRENDA; 3.1.2.2; 2681.
DR SABIO-RK; O00154; -.
DR ChiTaRS; ACOT7; human.
DR EvolutionaryTrace; O00154; -.
DR GeneWiki; ACOT7; -.
DR GenomeRNAi; 11332; -.
DR NextBio; 35469290; -.
DR PRO; PR:O00154; -.
DR ArrayExpress; O00154; -.
DR Bgee; O00154; -.
DR Genevestigator; O00154; -.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; TAS:ProtInc.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0009062; P:fatty acid catabolic process; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR InterPro; IPR006683; Thioestr_supf.
DR Pfam; PF03061; 4HBT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Mitochondrion;
KW Reference proteome; Repeat; Serine esterase.
FT CHAIN 1 380 Cytosolic acyl coenzyme A thioester
FT hydrolase.
FT /FTId=PRO_0000053806.
FT DOMAIN 56 151 Acyl coenzyme A hydrolase 1.
FT DOMAIN 242 319 Acyl coenzyme A hydrolase 2.
FT ACT_SITE 66 66 By similarity.
FT ACT_SITE 255 255 By similarity.
FT MOD_RES 168 168 N6-acetyllysine.
FT MOD_RES 198 198 N6-acetyllysine.
FT MOD_RES 283 283 N6-acetyllysine.
FT VAR_SEQ 1 58 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
FT VGPRADLPPCGACITGR -> MLLLRRSLSLNVLRKEVDRA
FT CFGEKAKQ (in isoform 5).
FT /FTId=VSP_000151.
FT VAR_SEQ 1 57 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
FT VGPRADLPPCGACITG -> MSGPDVETPSAIQIC (in
FT isoform 2, isoform 3 and isoform 4).
FT /FTId=VSP_000152.
FT VAR_SEQ 1 57 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
FT VGPRADLPPCGACITG -> MAFQLS (in isoform
FT 6).
FT /FTId=VSP_000153.
FT VAR_SEQ 1 57 MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQV
FT VGPRADLPPCGACITG -> MARPGLIHSAPGLPDTCALLQ
FT PPAASAAAAPSMSGPDVETPSAIQIC (in isoform
FT 7).
FT /FTId=VSP_047094.
FT VAR_SEQ 287 380 GCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAAS
FT AFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQM
FT KAKRQGHAEPQP -> AHVMPAGADHTAPSSSPSTGTKCSL
FT LRHHHLGTHDLHEQ (in isoform 3).
FT /FTId=VSP_000154.
FT VAR_SEQ 287 288 GC -> AP (in isoform 2).
FT /FTId=VSP_000155.
FT VAR_SEQ 289 380 Missing (in isoform 2).
FT /FTId=VSP_000156.
FT CONFLICT 82 82 E -> G (in Ref. 5; BAG51874).
FT CONFLICT 371 372 KR -> DD (in Ref. 3; AAB61211).
FT CONFLICT 377 378 EP -> DA (in Ref. 3; AAB61211).
FT HELIX 223 226
FT STRAND 228 233
FT HELIX 236 238
FT STRAND 241 245
FT HELIX 247 266
FT STRAND 267 280
FT STRAND 288 299
FT STRAND 301 314
FT STRAND 323 335
FT HELIX 352 371
SQ SEQUENCE 380 AA; 41796 MW; BDD75D62A60095BC CRC64;
MKLLARALRL CEFGRQASSR RLVAGQGCVG PRRGCCAPVQ VVGPRADLPP CGACITGRIM
RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC VAALARVERT DFLSPMCIGE
VAHVSAEITY TSKHSVEVQV NVMSENILTG AKKLTNKATL WYVPLSLKNV DKVLEVPPVV
YSRQEQEEEG RKRYEAQKLE RMETKWRNGD IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT
LHGFVHGGVT MKLMDEVAGI VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS
NKSMEIEVLV DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE
GKGRYLQMKA KRQGHAEPQP
//
MIM
602587
*RECORD*
*FIELD* NO
602587
*FIELD* TI
*602587 ACYL-CoA THIOESTERASE 7; ACOT7
;;ACYL-CoA THIOESTERASE, LONG-CHAIN, CYTOSOLIC;;
read moreCTE-II;;
ACYL-CoA THIOESTER HYDROLASE, LONG-CHAIN, 2;;
ACYL-CoA HYDROLASE, LONG-CHAIN, BRAIN; BACH;;
ACYL-CoA HYDROLASE, LONG-CHAIN, LIVER; LACH;;
ACYL-CoA THIOESTERASE 2, FORMERLY
*FIELD* TX
DESCRIPTION
Long-chain acyl-CoA thioesterases (EC 3.1.2.2), such as ACOT7, are found
in all organisms and cleave fatty acyl-CoAs into free fatty acids and
CoA.
CLONING
Engberg et al. (1997) purified a liver cytosolic isoform of long-chain
acyl-CoA thioesterase from peroxisome proliferator-treated rats and
named it CTE-II for 'cytosolic long-chain acyl-CoA thioesterase.'
Antibodies against CTE-II were used to screen an expression library of
peroxisome proliferator-induced rat liver cDNA. The predicted 338-amino
acid protein migrated at 40 kD on SDS-PAGE. Engberg et al. (1997)
observed many evenly distributed nucleotide differences and pronounced
differences in the C-terminal regions between CTE-II and the closely
related ACT (602586) and suggested that the 2 enzymes are encoded by
different genes. Engberg et al. (1997) noted that there are human ESTs
homologous to CTE-II.
Yamada et al. (1997) isolated cDNAs encoding long-chain acyl-CoA
hydrolases from rat brain and liver cDNA libraries and designated the
clones Bach and Lach, respectively. Since the nucleotide sequences of
the N-terminal regions were entirely different but the downstream
sequences were virtually identical, Yamada et al. (1997) suggested that
Bach and Lach are derived from the same gene by alternative splicing.
Using a rat Bach cDNA to screen a human brain cDNA library, Yamada et
al. (1999) cloned BACH. The deduced protein contains 338 amino acids and
shares 95% identity with rat Bach. Northern blot analysis detected a
1.9-kb BACH transcript in human brain RNA. Biochemical analysis of human
brain homogenates showed that BACH is a cytosolic enzyme. SDS-PAGE
detected BACH at 43 kD, but gel filtration detected BACH at about 100
kD, indicating that the protein forms multimers.
By 5-prime RACE and RT-PCR of human brain total RNA, Yamada et al.
(2002) identified 6 BACH splice variants. Four variants, designated
BACHa to BACHd, differ in their use of 1 of 4 alternate first exons
(exons 1a through 1d, respectively) and encode proteins of 329 to 380
amino acids. All 4 of these proteins contain the hydrolase domain and a
bipartite nuclear localization signal (NLS) in their C-terminal halves,
and BACHb and BACHc have N-terminal mitochondrial localization signals.
The 2 remaining variants contain exon X, an alternatively spliced exon
between exons 7 and 8 that causes a frameshift and introduces a
premature stop codon. These C-terminally truncated proteins of 246 and
283 amino acids lack the hydrolase domain and NLS. The BACH proteins
containing the mitochondrial localization signal were detected in
mitochondria of transfected mouse neuroblastoma cells, but those
containing only the NLS did not localize to nuclei, even though the
isolated NLS was functional when fused to a test protein.
Immunohistochemical analysis of human brain detected BACHa in the
cytosol of neurons such as pyramidal cells in the cerebral cortex and
Purkinje cells in the cerebellum. In mouse brain, Bacha was also
detected in nuclei as well as cytosol of certain large neurons in the
cerebellum, medulla oblongata, and spinal cord. Yamada et al. (2002)
suggested that the NLS of BACH may be masked by the full-length protein
as a regulatory mechanism.
GENE FUNCTION
Yamada et al. (1997) found that bacterial extracts of E. coli expressing
either rat Bach or Lach cDNAs had 100-fold higher acyl-CoA hydrolase
activity, demonstrating that both cDNAs encode long-chain acyl-CoA
hydrolases.
By analyzing the activity of purified BACH against several fatty
acyl-CoAs, Yamada et al. (1999) found that BACH showed a relatively
broad specificity, with acyl-CoAs with carbon chains of C8 to C18 being
good substrates. BACH activity was inhibited by a sulfhydryl blocking
agent. Recombinant BACH was also active against palmitoyl-CoA.
Yang et al. (2004) found significantly decreased levels of acyl-CoA
hydrolase in hippocampal tissue from 5 patients with mesial temporal
lobe epilepsy (608096) compared to controls.
GENE STRUCTURE
Yamada et al. (2002) determined that the ACOT7 gene contains 13 exons,
including 4 alternative first exons (exons 1a through 1d) and exon X, an
alternatively spliced exon between exons 7 and 8. The gene spans 129 kb.
MAPPING
By radiation hybrid analysis, Yamada et al. (1999) mapped the ACOT7 gene
to chromosome 1p36.2. Hunt et al. (2005) stated that the human ACOT7
gene maps to chromosome 1p36.31-p36.11 and the mouse Acot7 gene maps to
chromosome 4E2.
NOMENCLATURE
Hunt et al. (2005) noted that acyl-CoA thioesterases are referred to in
the literature as acyl-CoA hydrolases, but the reaction catalyzed is the
cleavage of a thioester bond. They presented a revised nomenclature for
these enzymes using the name acyl-CoA thioesterase and the root gene
symbol ACOT.
*FIELD* RF
1. Engberg, S. T.; Aoyama, T.; Alexson, S. E. H.; Hashimoto, T.; Svensson,
L. T.: Peroxisome proliferator-induced acyl-CoA thioesterase from
rat liver cytosol: molecular cloning and functional expression in
Chinese hamster ovary cells. Biochem. J. 323: 525-531, 1997.
2. Hunt, M. C.; Yamada, J.; Maltais, L. J.; Wright, M. W.; Podesta,
E. J.; Alexson, S. E. H.: A revised nomenclature for mammalian acyl-CoA
thioesterases/hydrolases. J. Lipid Res. 46: 2029-2032, 2005.
3. Yamada, J.; Furihata, T.; Iida, N.; Watanabe, T.; Hosokawa, M.;
Satoh, T.; Someya, A.; Nagaoka, I.; Suga, T.: Molecular cloning and
expression of cDNAs encoding rat brain and liver cytosolic long-chain
acyl-CoA hydrolases. Biochem. Biophys. Res. Commun. 232: 198-203,
1997.
4. Yamada, J.; Kuramochi, Y.; Takagi, M.; Watanabe, T.; Suga, T.:
Human brain acyl-CoA hydrolase isoforms encoded by a single gene. Biochem.
Biophys. Res. Commun. 299: 49-56, 2002.
5. Yamada, J.; Kurata, A.; Hirata, M.; Taniguchi, T.; Takama, H.;
Furihata, T.; Shiratori, K.; Iida, N.; Takagi-Sakuma, M.; Watanabe,
T.; Kurosaki, K.; Endo, T.; Suga, T.: Purification, molecular cloning,
and genomic organization of human brain long-chain acyl-CoA hydrolase. J.
Biochem. 126: 1013-1019, 1999.
6. Yang, J. W.; Czech, T.; Yamada, J.; Csaszar, E.; Baumgartner, C.;
Slavc, I.; Lubec, G.: Aberrant cytosolic acyl-CoA thioester hydrolase
in hippocampus of patients with mesial temporal lobe epilepsy. Amino
Acids 27: 269-275, 2004.
*FIELD* CN
Cassandra L. Kniffin - updated: 6/6/2006
Patricia A. Hartz - updated: 4/21/2006
*FIELD* CD
Rebekah S. Rasooly: 5/1/1998
*FIELD* ED
wwang: 06/23/2006
ckniffin: 6/6/2006
mgross: 6/6/2006
terry: 4/21/2006
carol: 3/17/2006
alopez: 5/1/1998
*RECORD*
*FIELD* NO
602587
*FIELD* TI
*602587 ACYL-CoA THIOESTERASE 7; ACOT7
;;ACYL-CoA THIOESTERASE, LONG-CHAIN, CYTOSOLIC;;
read moreCTE-II;;
ACYL-CoA THIOESTER HYDROLASE, LONG-CHAIN, 2;;
ACYL-CoA HYDROLASE, LONG-CHAIN, BRAIN; BACH;;
ACYL-CoA HYDROLASE, LONG-CHAIN, LIVER; LACH;;
ACYL-CoA THIOESTERASE 2, FORMERLY
*FIELD* TX
DESCRIPTION
Long-chain acyl-CoA thioesterases (EC 3.1.2.2), such as ACOT7, are found
in all organisms and cleave fatty acyl-CoAs into free fatty acids and
CoA.
CLONING
Engberg et al. (1997) purified a liver cytosolic isoform of long-chain
acyl-CoA thioesterase from peroxisome proliferator-treated rats and
named it CTE-II for 'cytosolic long-chain acyl-CoA thioesterase.'
Antibodies against CTE-II were used to screen an expression library of
peroxisome proliferator-induced rat liver cDNA. The predicted 338-amino
acid protein migrated at 40 kD on SDS-PAGE. Engberg et al. (1997)
observed many evenly distributed nucleotide differences and pronounced
differences in the C-terminal regions between CTE-II and the closely
related ACT (602586) and suggested that the 2 enzymes are encoded by
different genes. Engberg et al. (1997) noted that there are human ESTs
homologous to CTE-II.
Yamada et al. (1997) isolated cDNAs encoding long-chain acyl-CoA
hydrolases from rat brain and liver cDNA libraries and designated the
clones Bach and Lach, respectively. Since the nucleotide sequences of
the N-terminal regions were entirely different but the downstream
sequences were virtually identical, Yamada et al. (1997) suggested that
Bach and Lach are derived from the same gene by alternative splicing.
Using a rat Bach cDNA to screen a human brain cDNA library, Yamada et
al. (1999) cloned BACH. The deduced protein contains 338 amino acids and
shares 95% identity with rat Bach. Northern blot analysis detected a
1.9-kb BACH transcript in human brain RNA. Biochemical analysis of human
brain homogenates showed that BACH is a cytosolic enzyme. SDS-PAGE
detected BACH at 43 kD, but gel filtration detected BACH at about 100
kD, indicating that the protein forms multimers.
By 5-prime RACE and RT-PCR of human brain total RNA, Yamada et al.
(2002) identified 6 BACH splice variants. Four variants, designated
BACHa to BACHd, differ in their use of 1 of 4 alternate first exons
(exons 1a through 1d, respectively) and encode proteins of 329 to 380
amino acids. All 4 of these proteins contain the hydrolase domain and a
bipartite nuclear localization signal (NLS) in their C-terminal halves,
and BACHb and BACHc have N-terminal mitochondrial localization signals.
The 2 remaining variants contain exon X, an alternatively spliced exon
between exons 7 and 8 that causes a frameshift and introduces a
premature stop codon. These C-terminally truncated proteins of 246 and
283 amino acids lack the hydrolase domain and NLS. The BACH proteins
containing the mitochondrial localization signal were detected in
mitochondria of transfected mouse neuroblastoma cells, but those
containing only the NLS did not localize to nuclei, even though the
isolated NLS was functional when fused to a test protein.
Immunohistochemical analysis of human brain detected BACHa in the
cytosol of neurons such as pyramidal cells in the cerebral cortex and
Purkinje cells in the cerebellum. In mouse brain, Bacha was also
detected in nuclei as well as cytosol of certain large neurons in the
cerebellum, medulla oblongata, and spinal cord. Yamada et al. (2002)
suggested that the NLS of BACH may be masked by the full-length protein
as a regulatory mechanism.
GENE FUNCTION
Yamada et al. (1997) found that bacterial extracts of E. coli expressing
either rat Bach or Lach cDNAs had 100-fold higher acyl-CoA hydrolase
activity, demonstrating that both cDNAs encode long-chain acyl-CoA
hydrolases.
By analyzing the activity of purified BACH against several fatty
acyl-CoAs, Yamada et al. (1999) found that BACH showed a relatively
broad specificity, with acyl-CoAs with carbon chains of C8 to C18 being
good substrates. BACH activity was inhibited by a sulfhydryl blocking
agent. Recombinant BACH was also active against palmitoyl-CoA.
Yang et al. (2004) found significantly decreased levels of acyl-CoA
hydrolase in hippocampal tissue from 5 patients with mesial temporal
lobe epilepsy (608096) compared to controls.
GENE STRUCTURE
Yamada et al. (2002) determined that the ACOT7 gene contains 13 exons,
including 4 alternative first exons (exons 1a through 1d) and exon X, an
alternatively spliced exon between exons 7 and 8. The gene spans 129 kb.
MAPPING
By radiation hybrid analysis, Yamada et al. (1999) mapped the ACOT7 gene
to chromosome 1p36.2. Hunt et al. (2005) stated that the human ACOT7
gene maps to chromosome 1p36.31-p36.11 and the mouse Acot7 gene maps to
chromosome 4E2.
NOMENCLATURE
Hunt et al. (2005) noted that acyl-CoA thioesterases are referred to in
the literature as acyl-CoA hydrolases, but the reaction catalyzed is the
cleavage of a thioester bond. They presented a revised nomenclature for
these enzymes using the name acyl-CoA thioesterase and the root gene
symbol ACOT.
*FIELD* RF
1. Engberg, S. T.; Aoyama, T.; Alexson, S. E. H.; Hashimoto, T.; Svensson,
L. T.: Peroxisome proliferator-induced acyl-CoA thioesterase from
rat liver cytosol: molecular cloning and functional expression in
Chinese hamster ovary cells. Biochem. J. 323: 525-531, 1997.
2. Hunt, M. C.; Yamada, J.; Maltais, L. J.; Wright, M. W.; Podesta,
E. J.; Alexson, S. E. H.: A revised nomenclature for mammalian acyl-CoA
thioesterases/hydrolases. J. Lipid Res. 46: 2029-2032, 2005.
3. Yamada, J.; Furihata, T.; Iida, N.; Watanabe, T.; Hosokawa, M.;
Satoh, T.; Someya, A.; Nagaoka, I.; Suga, T.: Molecular cloning and
expression of cDNAs encoding rat brain and liver cytosolic long-chain
acyl-CoA hydrolases. Biochem. Biophys. Res. Commun. 232: 198-203,
1997.
4. Yamada, J.; Kuramochi, Y.; Takagi, M.; Watanabe, T.; Suga, T.:
Human brain acyl-CoA hydrolase isoforms encoded by a single gene. Biochem.
Biophys. Res. Commun. 299: 49-56, 2002.
5. Yamada, J.; Kurata, A.; Hirata, M.; Taniguchi, T.; Takama, H.;
Furihata, T.; Shiratori, K.; Iida, N.; Takagi-Sakuma, M.; Watanabe,
T.; Kurosaki, K.; Endo, T.; Suga, T.: Purification, molecular cloning,
and genomic organization of human brain long-chain acyl-CoA hydrolase. J.
Biochem. 126: 1013-1019, 1999.
6. Yang, J. W.; Czech, T.; Yamada, J.; Csaszar, E.; Baumgartner, C.;
Slavc, I.; Lubec, G.: Aberrant cytosolic acyl-CoA thioester hydrolase
in hippocampus of patients with mesial temporal lobe epilepsy. Amino
Acids 27: 269-275, 2004.
*FIELD* CN
Cassandra L. Kniffin - updated: 6/6/2006
Patricia A. Hartz - updated: 4/21/2006
*FIELD* CD
Rebekah S. Rasooly: 5/1/1998
*FIELD* ED
wwang: 06/23/2006
ckniffin: 6/6/2006
mgross: 6/6/2006
terry: 4/21/2006
carol: 3/17/2006
alopez: 5/1/1998