BACH_RAT
ID BACH_RAT Reviewed; 381 AA.
AC Q64559; O08652; O09041;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cytosolic acyl coenzyme A thioester hydrolase;
DE EC=3.1.2.2 {ECO:0000269|PubMed:7906114};
DE AltName: Full=ACH1;
DE AltName: Full=ACT;
DE AltName: Full=Acyl-CoA thioesterase 7;
DE AltName: Full=Brain acyl-CoA hydrolase;
DE Short=BACH;
DE AltName: Full=CTE-IIa;
DE AltName: Full=CTE-IIb;
DE Short=CTE-II;
DE AltName: Full=LACH1;
DE AltName: Full=Long chain acyl-CoA thioester hydrolase;
DE AltName: Full=MTE-II;
GN Name=Acot7; Synonyms=Bach;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 306-343.
RC TISSUE=Brain;
RX PubMed=8631842; DOI=10.1074/jbc.271.18.10470;
RA Broustas C.G., Larkins L.K., Uhler M.D., Hajra A.K.;
RT "Molecular cloning and expression of cDNA encoding rat brain cytosolic
RT acyl-coenzyme A thioester hydrolase.";
RL J. Biol. Chem. 271:10470-10476(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND PROTEIN SEQUENCE OF
RP 60-72; 256-264; 315-343 AND 370-380.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Liver;
RX PubMed=9125130; DOI=10.1006/bbrc.1997.6246;
RA Yamada J., Furihata T., Iida N., Watanabe T., Hosokawa M., Satoh T.,
RA Someya A., Nagaoka I., Suga T.;
RT "Molecular cloning and expression of cDNAs encoding rat brain and liver
RT cytosolic long-chain acyl-CoA hydrolases.";
RL Biochem. Biophys. Res. Commun. 232:198-203(1997).
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS (ISOFORM 2).
RA Yamada J., Furihata T., Iida N., Watanabe T., Hosokawa M., Satoh T.,
RA Someya A., Nagaoka I., Suga T.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9163348; DOI=10.1042/bj3230525;
RA Engberg S.T., Aoyama T., Alexson S.E.H., Hashimoto T., Svensson L.T.;
RT "Peroxisome proliferator-induced acyl-CoA thioesterase from rat liver
RT cytosol: molecular cloning and functional expression in Chinese hamster
RT ovary cells.";
RL Biochem. J. 323:525-531(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP PROTEIN SEQUENCE OF 135-153 AND 173-184 (ISOFORMS 1/2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Diao W., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7906114; DOI=10.1006/abbi.1994.1017;
RA Yamada J., Matsumoto I., Furihata T., Sakuma M., Suga T.;
RT "Purification and properties of long-chain acyl-CoA hydrolases from the
RT liver cytosol of rats treated with peroxisome proliferator.";
RL Arch. Biochem. Biophys. 308:118-125(1994).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [9]
RP REVIEW.
RX PubMed=11755680; DOI=10.1016/s0163-7827(01)00017-0;
RA Hunt M.C., Alexson S.E.H.;
RT "The role Acyl-CoA thioesterases play in mediating intracellular lipid
RT metabolism.";
RL Prog. Lipid Res. 41:99-130(2002).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (PubMed:7906114). Preferentially hydrolyzes palmitoyl-CoA, but
CC has a broad specificity acting on other fatty acyl-CoAs with chain-
CC lengths of C8-C18 (PubMed:7906114). May play an important physiological
CC function in brain (PubMed:7906114). {ECO:0000269|PubMed:7906114}.
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:7906114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:7906114};
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:0000269|PubMed:7906114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:7906114};
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:0000269|PubMed:7906114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:7906114};
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:0000269|PubMed:7906114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000305|PubMed:7906114};
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:0000269|PubMed:7906114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC Evidence={ECO:0000305|PubMed:7906114};
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:0000269|PubMed:7906114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000305|PubMed:7906114};
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:0000269|PubMed:7906114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000305|PubMed:7906114};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.9 uM for palmitoyl-CoA {ECO:0000269|PubMed:7906114};
CC Vmax=553 umol/min/mg enzyme with palmitoyl-CoA as substrate
CC {ECO:0000269|PubMed:7906114};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:7906114}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q91V12}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7906114}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=LACH1, MTE-II;
CC IsoId=Q64559-2; Sequence=Displayed;
CC Name=1; Synonyms=BACH, CTE-IIa, CTE-II;
CC IsoId=Q64559-1; Sequence=VSP_016956;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed constitutively in brain and
CC testis. Isoform 2 is induced in liver by treatment with the peroxisome
CC proliferator.
CC -!- DOMAIN: Both HotDog ACOT-type hydrolase domains are required for
CC efficient activity. {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- CAUTION: These proteins have been named according to their molecular
CC weight (see PubMed:11755680): BACH (also called CTE-IIa and CTE-II),
CC LACH1 (also called MTE-II) and ACT (also called CTE-IIb). It is unknown
CC whether ACT corresponds to another isoform. {ECO:0000305}.
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DR EMBL; U49694; AAC53202.1; -; mRNA.
DR EMBL; D88890; BAA19626.1; -; mRNA.
DR EMBL; D88891; BAA19627.2; -; mRNA.
DR EMBL; Y09332; CAA70512.1; -; mRNA.
DR EMBL; BC087716; AAH87716.1; -; mRNA.
DR PIR; JC5415; JC5415.
DR PIR; JC5416; JC5416.
DR RefSeq; NP_001139533.1; NM_001146061.1. [Q64559-2]
DR RefSeq; NP_037346.2; NM_013214.4.
DR AlphaFoldDB; Q64559; -.
DR SMR; Q64559; -.
DR STRING; 10116.ENSRNOP00000014213; -.
DR SwissLipids; SLP:000000586; -.
DR SwissLipids; SLP:000000614; -. [Q64559-1]
DR iPTMnet; Q64559; -.
DR PhosphoSitePlus; Q64559; -.
DR jPOST; Q64559; -.
DR PaxDb; Q64559; -.
DR PRIDE; Q64559; -.
DR GeneID; 26759; -.
DR KEGG; rno:26759; -.
DR UCSC; RGD:628856; rat. [Q64559-2]
DR CTD; 11332; -.
DR RGD; 628856; Acot7.
DR VEuPathDB; HostDB:ENSRNOG00000010580; -.
DR eggNOG; KOG2763; Eukaryota.
DR InParanoid; Q64559; -.
DR OrthoDB; 1069806at2759; -.
DR PhylomeDB; Q64559; -.
DR TreeFam; TF329579; -.
DR BRENDA; 3.1.2.2; 5301.
DR BRENDA; 3.1.2.20; 5301.
DR Reactome; R-RNO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SABIO-RK; Q64559; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q64559; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000010580; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q64559; baseline and differential.
DR Genevisible; Q64559; RN.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:RGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; ISO:RGD.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; ISO:RGD.
DR GO; GO:0009062; P:fatty acid catabolic process; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0036116; P:long-chain fatty-acyl-CoA catabolic process; ISO:RGD.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0036114; P:medium-chain fatty-acyl-CoA catabolic process; ISO:RGD.
DR GO; GO:1900535; P:palmitic acid biosynthetic process; ISO:RGD.
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 Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Fatty acid metabolism; Hydrolase; Lipid metabolism; Reference proteome;
KW Repeat; Serine esterase.
FT CHAIN 1..381
FT /note="Cytosolic acyl coenzyme A thioester hydrolase"
FT /id="PRO_0000053808"
FT DOMAIN 51..169
FT /note="HotDog ACOT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 225..339
FT /note="HotDog ACOT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT REGION 343..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 67
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /evidence="ECO:0000250"
FT MOD_RES 169
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00154"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00154"
FT MOD_RES 284
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00154"
FT VAR_SEQ 1..58
FT /note="MKLLARTLYLWEVGRQVASWSLTSGQECLVLRETWWASMRAVRTRAVHHKPG
FT HCIAMG -> MSGPTTDTPAAIQIC (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8631842, ECO:0000303|PubMed:9125130,
FT ECO:0000303|PubMed:9163348"
FT /id="VSP_016956"
FT CONFLICT 86
FT /note="V -> A (in Ref. 1; AAC53202)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="S -> R (in Ref. 1; AAC53202)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="L -> M (in Ref. 1; AAC53202)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="V -> A (in Ref. 2; BAA19627)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="I -> V (in Ref. 1; AAC53202)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="I -> V (in Ref. 2; BAA19627)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="L -> M (in Ref. 1; AAC53202)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="K -> N (in Ref. 1; AAC53202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42735 MW; F19CB7B34A4BE5D7 CRC64;
MKLLARTLYL WEVGRQVASW SLTSGQECLV LRETWWASMR AVRTRAVHHK PGHCIAMGRI
MRPDDANVAG NVHGGTILKM IEEAGVIIST RHCNSQNGER CVAALARVER TDFLSPMCIG
EVAHVSAEIT YTSKHSVEVQ VHVLSENILT GTKKLTNKAT LWYVPLSLKN VDKVLEVPPI
VYLRQEQEEE GRKRYEAQKL ERMETKWRNG DIVQPILNPE PNTVSYSQSS LIHLVGPSDC
TLHGFVHGGV TMKLMDEVAG IVAARHCKTN IVTASVDAIN FHDKIRKGCV ITISGRMTFT
SNKSMEIEVL VDADPVVDNS QKRYRAASAF FTYVSLNQEG KPLPVPQLVP ETEDEKKRFE
EGKGRYLQMK AKRQGHTEPQ P
