BACH_HUMAN
ID BACH_HUMAN Reviewed; 380 AA.
AC O00154; A8K0K7; A8K232; A8K6B8; A8K837; B3KQ12; O43703; Q53Y78; Q5JYL2;
AC Q5JYL3; Q5JYL4; Q5JYL5; Q5JYL6; Q5TGR4; Q9UJM9; Q9Y539; Q9Y540;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Cytosolic acyl coenzyme A thioester hydrolase;
DE EC=3.1.2.2 {ECO:0000305|PubMed:10578051};
DE AltName: Full=Acyl-CoA thioesterase 7;
DE AltName: Full=Brain acyl-CoA hydrolase;
DE Short=BACH;
DE Short=hBACH {ECO:0000303|PubMed:10578051};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10578051; DOI=10.1093/oxfordjournals.jbchem.a022544;
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., Endo T.,
RA Suga T.;
RT "Purification, molecular cloning, and genomic organization of human brain
RT 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 79-90, AND IDENTIFICATION BY 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, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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., Buerckstuemmer T.,
RA 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: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (PubMed:10578051). Preferentially hydrolyzes palmitoyl-CoA, but
CC has a broad specificity acting on other fatty acyl-CoAs with chain-
CC lengths of C8-C18 (PubMed:10578051). May play an important
CC physiological function in brain (PubMed:10578051).
CC {ECO:0000269|PubMed:10578051}.
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:0000269|PubMed:10578051};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:10578051};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate;
CC Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386;
CC Evidence={ECO:0000305|PubMed:10578051};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC Evidence={ECO:0000305|PubMed:10578051};
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:0000305|PubMed:10578051};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:10578051};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000305|PubMed:10578051};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000305|PubMed:10578051};
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:Q64559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000250|UniProtKB:Q64559};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+);
CC Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000250|UniProtKB:Q64559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000250|UniProtKB:Q64559};
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:Q64559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000250|UniProtKB:Q64559};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:10578051}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q91V12}.
CC -!- INTERACTION:
CC O00154; Q01484: ANK2; NbExp=2; IntAct=EBI-948905, EBI-941975;
CC O00154; Q13554: CAMK2B; NbExp=3; IntAct=EBI-948905, EBI-1058722;
CC O00154; Q9HCK8: CHD8; NbExp=2; IntAct=EBI-948905, EBI-1169146;
CC O00154; Q13618: CUL3; NbExp=2; IntAct=EBI-948905, EBI-456129;
CC O00154; Q06787: FMR1; NbExp=2; IntAct=EBI-948905, EBI-366305;
CC O00154; V9HW27: HEL-S-101; NbExp=3; IntAct=EBI-948905, EBI-10178933;
CC O00154; P43360: MAGEA6; NbExp=3; IntAct=EBI-948905, EBI-1045155;
CC O00154; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-948905, EBI-741515;
CC O00154; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-948905, EBI-741480;
CC O00154; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-948905, EBI-10173939;
CC O00154-4; Q8WYK0: ACOT12; NbExp=3; IntAct=EBI-12007918, EBI-11954993;
CC O00154-4; O95429: BAG4; NbExp=3; IntAct=EBI-12007918, EBI-2949658;
CC O00154-4; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-12007918, EBI-11523526;
CC O00154-4; Q15038: DAZAP2; NbExp=3; IntAct=EBI-12007918, EBI-724310;
CC O00154-4; P32321: DCTD; NbExp=3; IntAct=EBI-12007918, EBI-739870;
CC O00154-4; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-12007918, EBI-744099;
CC O00154-4; P43357: MAGEA3; NbExp=3; IntAct=EBI-12007918, EBI-5651459;
CC O00154-4; P43360: MAGEA6; NbExp=3; IntAct=EBI-12007918, EBI-1045155;
CC O00154-4; Q14863: POU6F1; NbExp=3; IntAct=EBI-12007918, EBI-18138148;
CC O00154-4; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-12007918, EBI-11995806;
CC O00154-4; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-12007918, EBI-741515;
CC O00154-4; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12007918, EBI-741480;
CC O00154-4; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12007918, EBI-947187;
CC O00154-4; Q04323-2: UBXN1; NbExp=3; IntAct=EBI-12007918, EBI-11530712;
CC O00154-4; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-12007918, EBI-11962468;
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytosol
CC {ECO:0000305|PubMed:12435388}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytosol
CC {ECO:0000305|PubMed:12435388}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:12435388}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion
CC {ECO:0000269|PubMed:12435388}.
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 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 {ECO:0000269|PubMed:12435388}.
CC -!- DOMAIN: Both HotDog ACOT-type hydrolase domains are required for
CC efficient activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 4]: Major isoform. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61211.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH17365.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031848; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS30573.1; -. [O00154-7]
DR CCDS; CCDS65.1; -. [O00154-1]
DR CCDS; CCDS66.1; -. [O00154-5]
DR CCDS; CCDS67.1; -. [O00154-6]
DR PIR; JC7161; JC7161.
DR RefSeq; NP_009205.3; NM_007274.3. [O00154-7]
DR RefSeq; NP_863654.1; NM_181864.2. [O00154-1]
DR RefSeq; NP_863655.1; NM_181865.2. [O00154-5]
DR RefSeq; NP_863656.1; NM_181866.2. [O00154-6]
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 AlphaFoldDB; O00154; -.
DR SMR; O00154; -.
DR BioGRID; 116460; 87.
DR IntAct; O00154; 55.
DR MINT; O00154; -.
DR STRING; 9606.ENSP00000367086; -.
DR GlyGen; O00154; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00154; -.
DR MetOSite; O00154; -.
DR PhosphoSitePlus; O00154; -.
DR SwissPalm; O00154; -.
DR BioMuta; ACOT7; -.
DR UCD-2DPAGE; O00154; -.
DR CPTAC; CPTAC-303; -.
DR CPTAC; CPTAC-304; -.
DR EPD; O00154; -.
DR jPOST; O00154; -.
DR MassIVE; O00154; -.
DR MaxQB; O00154; -.
DR PaxDb; O00154; -.
DR PeptideAtlas; O00154; -.
DR PRIDE; O00154; -.
DR ProteomicsDB; 47737; -. [O00154-1]
DR ProteomicsDB; 47738; -. [O00154-2]
DR ProteomicsDB; 47739; -. [O00154-3]
DR ProteomicsDB; 47740; -. [O00154-4]
DR ProteomicsDB; 47741; -. [O00154-5]
DR ProteomicsDB; 47742; -. [O00154-6]
DR TopDownProteomics; O00154-1; -. [O00154-1]
DR Antibodypedia; 12967; 159 antibodies from 22 providers.
DR DNASU; 11332; -.
DR Ensembl; ENST00000361521.9; ENSP00000354615.4; ENSG00000097021.20. [O00154-7]
DR Ensembl; ENST00000377842.7; ENSP00000367073.3; ENSG00000097021.20. [O00154-6]
DR Ensembl; ENST00000377845.7; ENSP00000367076.3; ENSG00000097021.20. [O00154-5]
DR Ensembl; ENST00000377855.6; ENSP00000367086.2; ENSG00000097021.20. [O00154-1]
DR Ensembl; ENST00000377860.8; ENSP00000367091.4; ENSG00000097021.20. [O00154-3]
DR Ensembl; ENST00000418124.5; ENSP00000402532.1; ENSG00000097021.20. [O00154-2]
DR Ensembl; ENST00000545482.5; ENSP00000439218.2; ENSG00000097021.20. [O00154-7]
DR Ensembl; ENST00000608083.5; ENSP00000476610.1; ENSG00000097021.20. [O00154-4]
DR GeneID; 11332; -.
DR KEGG; hsa:11332; -.
DR MANE-Select; ENST00000361521.9; ENSP00000354615.4; NM_007274.4; NP_009205.3. [O00154-7]
DR UCSC; uc001amq.4; human. [O00154-1]
DR CTD; 11332; -.
DR DisGeNET; 11332; -.
DR GeneCards; ACOT7; -.
DR HGNC; HGNC:24157; ACOT7.
DR HPA; ENSG00000097021; Tissue enhanced (brain).
DR MIM; 602587; gene.
DR neXtProt; NX_O00154; -.
DR OpenTargets; ENSG00000097021; -.
DR PharmGKB; PA142672655; -.
DR VEuPathDB; HostDB:ENSG00000097021; -.
DR eggNOG; KOG2763; Eukaryota.
DR GeneTree; ENSGT00940000155229; -.
DR HOGENOM; CLU_050164_0_0_1; -.
DR InParanoid; O00154; -.
DR OMA; PTDVNWG; -.
DR OrthoDB; 1069806at2759; -.
DR PhylomeDB; O00154; -.
DR TreeFam; TF329579; -.
DR BioCyc; MetaCyc:HS01875-MON; -.
DR BRENDA; 3.1.2.2; 2681.
DR BRENDA; 3.1.2.20; 2681.
DR PathwayCommons; O00154; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SABIO-RK; O00154; -.
DR SignaLink; O00154; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 11332; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; ACOT7; human.
DR EvolutionaryTrace; O00154; -.
DR GeneWiki; ACOT7; -.
DR GenomeRNAi; 11332; -.
DR Pharos; O00154; Tbio.
DR PRO; PR:O00154; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00154; protein.
DR Bgee; ENSG00000097021; Expressed in lateral nuclear group of thalamus and 181 other tissues.
DR ExpressionAtlas; O00154; baseline and differential.
DR Genevisible; O00154; HS.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0000062; F:fatty-acyl-CoA binding; IDA:BHF-UCL.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IDA:BHF-UCL.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0036116; P:long-chain fatty-acyl-CoA catabolic process; IDA:BHF-UCL.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0036114; P:medium-chain fatty-acyl-CoA catabolic process; IDA:BHF-UCL.
DR GO; GO:1900535; P:palmitic acid biosynthetic process; IDA:BHF-UCL.
DR InterPro; IPR040170; Cytosol_ACT.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006683; Thioestr_dom.
DR PANTHER; PTHR11049; PTHR11049; 2.
DR Pfam; PF03061; 4HBT; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Fatty acid metabolism; Hydrolase;
KW Lipid metabolism; Mitochondrion; Reference proteome; Repeat;
KW Serine esterase.
FT CHAIN 1..380
FT /note="Cytosolic acyl coenzyme A thioester hydrolase"
FT /id="PRO_0000053806"
FT DOMAIN 50..168
FT /note="HotDog ACOT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 224..338
FT /note="HotDog ACOT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT REGION 350..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /evidence="ECO:0000250"
FT MOD_RES 168
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 283
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..58
FT /note="MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCG
FT ACITGR -> MLLLRRSLSLNVLRKEVDRACFGEKAKQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12435388,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_000151"
FT VAR_SEQ 1..57
FT /note="MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCG
FT ACITG -> MSGPDVETPSAIQIC (in isoform 2, isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:10578051,
FT ECO:0000303|PubMed:12435388, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.4"
FT /id="VSP_000152"
FT VAR_SEQ 1..57
FT /note="MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCG
FT ACITG -> MAFQLS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12435388,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_000153"
FT VAR_SEQ 1..57
FT /note="MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCG
FT ACITG -> MARPGLIHSAPGLPDTCALLQPPAASAAAAPSMSGPDVETPSAIQIC
FT (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047094"
FT VAR_SEQ 287..380
FT /note="GCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQE
FT GRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHAEPQP -> AHVMPAGADHTAP
FT SSSPSTGTKCSLLRHHHLGTHDLHEQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12435388"
FT /id="VSP_000154"
FT VAR_SEQ 287..288
FT /note="GC -> AP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12435388"
FT /id="VSP_000155"
FT VAR_SEQ 289..380
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12435388"
FT /id="VSP_000156"
FT CONFLICT 82
FT /note="E -> G (in Ref. 5; BAG51874)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..372
FT /note="KR -> DD (in Ref. 3; AAB61211)"
FT /evidence="ECO:0000305"
FT CONFLICT 377..378
FT /note="EP -> DA (in Ref. 3; AAB61211)"
FT /evidence="ECO:0000305"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:2QQ2"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:2QQ2"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:2QQ2"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2QQ2"
FT HELIX 247..266
FT /evidence="ECO:0007829|PDB:2QQ2"
FT STRAND 267..280
FT /evidence="ECO:0007829|PDB:2QQ2"
FT STRAND 288..299
FT /evidence="ECO:0007829|PDB:2QQ2"
FT STRAND 301..314
FT /evidence="ECO:0007829|PDB:2QQ2"
FT STRAND 323..335
FT /evidence="ECO:0007829|PDB:2QQ2"
FT HELIX 352..371
FT /evidence="ECO:0007829|PDB:2QQ2"
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
