ACO10_MOUSE
ID ACO10_MOUSE Reviewed; 439 AA.
AC Q32MW3; A0FJF7; Q32MW2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Acyl-coenzyme A thioesterase 10, mitochondrial;
DE Short=Acyl-CoA thioesterase 10;
DE EC=3.1.2.-;
DE AltName: Full=Mitochondrial 48 kDa acyl-CoA thioester hydrolase 2;
DE Short=Mt-ACT48.2;
DE Flags: Precursor;
GN Name=Acot10 {ECO:0000312|MGI:MGI:1928940};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=10383425; DOI=10.1074/jbc.274.27.19188;
RA Poupon V., Begue B., Gagnon J., Dautry-Varsat A., Cerf-Bensussan N.,
RA Benmerah A.;
RT "Molecular cloning and characterization of MT-ACT48, a novel mitochondrial
RT acyl-CoA thioesterase.";
RL J. Biol. Chem. 274:19188-19194(1999).
RN [2] {ECO:0000312|EMBL:AAI08961.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3] {ECO:0000305, ECO:0000312|EMBL:ABK20321.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-426.
RX PubMed=17305828; DOI=10.1111/j.1420-9101.2006.01245.x;
RA Gayral P., Caminade P., Boursot P., Galtier N.;
RT "The evolutionary fate of recently duplicated retrogenes in mice.";
RL J. Evol. Biol. 20:617-626(2007).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels. Active on long chain acyl-CoAs. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10383425,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family.
CC {ECO:0000255}.
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DR EMBL; AJ238894; CAB45255.1; -; mRNA.
DR EMBL; BC108959; AAI08960.1; -; mRNA.
DR EMBL; BC108960; AAI08961.1; -; mRNA.
DR EMBL; EF014736; ABK20321.1; -; Genomic_DNA.
DR CCDS; CCDS27395.1; -.
DR RefSeq; NP_073727.2; NM_022816.2.
DR AlphaFoldDB; Q32MW3; -.
DR SMR; Q32MW3; -.
DR STRING; 10090.ENSMUSP00000051333; -.
DR iPTMnet; Q32MW3; -.
DR PhosphoSitePlus; Q32MW3; -.
DR SwissPalm; Q32MW3; -.
DR jPOST; Q32MW3; -.
DR MaxQB; Q32MW3; -.
DR PaxDb; Q32MW3; -.
DR PeptideAtlas; Q32MW3; -.
DR PRIDE; Q32MW3; -.
DR ProteomicsDB; 285591; -.
DR DNASU; 64833; -.
DR Ensembl; ENSMUST00000052910; ENSMUSP00000051333; ENSMUSG00000047565.
DR GeneID; 64833; -.
DR KEGG; mmu:64833; -.
DR UCSC; uc007vio.1; mouse.
DR CTD; 64833; -.
DR MGI; MGI:1928940; Acot10.
DR VEuPathDB; HostDB:ENSMUSG00000047565; -.
DR eggNOG; KOG2763; Eukaryota.
DR GeneTree; ENSGT00390000005330; -.
DR HOGENOM; CLU_032862_2_1_1; -.
DR InParanoid; Q32MW3; -.
DR OMA; REMLWYI; -.
DR OrthoDB; 786592at2759; -.
DR PhylomeDB; Q32MW3; -.
DR TreeFam; TF313352; -.
DR BioGRID-ORCS; 64833; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Acot10; mouse.
DR PRO; PR:Q32MW3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q32MW3; protein.
DR Bgee; ENSMUSG00000047565; Expressed in spermatid and 3 other tissues.
DR Genevisible; Q32MW3; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:MGI.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
PE 2: Evidence at transcript level;
KW Hydrolase; Mitochondrion; Reference proteome; Repeat; Serine esterase;
KW Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q9R0X4"
FT CHAIN 22..439
FT /note="Acyl-coenzyme A thioesterase 10, mitochondrial"
FT /id="PRO_0000306248"
FT DOMAIN 85..209
FT /note="HotDog ACOT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 289..401
FT /note="HotDog ACOT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT CONFLICT 119
FT /note="L -> F (in Ref. 1; CAB45255)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="L -> P (in Ref. 3; ABK20321)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="T -> K (in Ref. 3; ABK20321)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="P -> L (in Ref. 2; AAI08961)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="S -> G (in Ref. 3; ABK20321)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="K -> F (in Ref. 3; ABK20321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 50552 MW; A1BE1226F663250C CRC64;
MKRAAMRLWT LNKGLLTHGR GLSQGSQYKI SEPLHIHQVQ VKLREIVGIS TVWRDHVQAM
EERKLLHSFL PKSQKVLPPR KIRDSYIEVL LPLGTDPELR DKYVTVQNTV RFGRILEDLD
SLGVLVCYMH NHNHSTNMSL LSIVTVLVDK IDMCKHSLSP EQDIKFTGHV SWVGNTTMEV
KMKMFQLHDD ETYWPVLDAT FVMVAQDSEN KRPAFVNPLI PENKEEEELF TQGELNKSRR
IAFSTSSLLK VAPSSEERNI IHELFLSTLD PKTISFQSRI LPPKAVWMED TKLKSLDICH
PQERNVFNRI FGGFLMRKAY ELAWATACSF GGSRPYVVTV DDIMFQKPVE VGSLLFLSSQ
VCFTQGNYIQ VRVHSEVFSL DSREHMTTNV FHFTFMSEKE VPLIFPKTYG ESMLYLDGQR
HFKSMSTPVT LKKDYPVEP
