ID   ACOT9_BOVIN             Reviewed;         437 AA.
AC   Q3SWX2;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Acyl-coenzyme A thioesterase 9, mitochondrial;
DE            Short=Acyl-CoA thioesterase 9;
DE            EC=3.1.2.-;
DE   AltName: Full=Acyl-CoA thioester hydrolase 9;
DE   Flags: Precursor;
GN   Name=ACOT9;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze
CC       the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A
CC       (CoASH), providing the potential to regulate intracellular levels of
CC       acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs.
CC   -!- SUBUNIT: Interacts with NYAP1, NYAP2 and MYO16. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT030514; ABQ12954.1; -; mRNA.
DR   EMBL; BC104625; AAI04626.1; -; mRNA.
DR   RefSeq; NP_001029732.1; NM_001034560.1.
DR   AlphaFoldDB; Q3SWX2; -.
DR   SMR; Q3SWX2; -.
DR   STRING; 9913.ENSBTAP00000014953; -.
DR   PaxDb; Q3SWX2; -.
DR   PRIDE; Q3SWX2; -.
DR   Ensembl; ENSBTAT00000014953; ENSBTAP00000014953; ENSBTAG00000011258.
DR   GeneID; 527845; -.
DR   KEGG; bta:527845; -.
DR   CTD; 23597; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011258; -.
DR   VGNC; VGNC:25551; ACOT9.
DR   eggNOG; KOG2763; Eukaryota.
DR   GeneTree; ENSGT00390000005330; -.
DR   HOGENOM; CLU_032862_2_1_1; -.
DR   InParanoid; Q3SWX2; -.
DR   OMA; PLAQDPW; -.
DR   OrthoDB; 786592at2759; -.
DR   TreeFam; TF313352; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000011258; Expressed in oocyte and 104 other tissues.
DR   ExpressionAtlas; Q3SWX2; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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: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   Acetylation; Hydrolase; Mitochondrion; Reference proteome; Repeat;
KW   Serine esterase; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..437
FT                   /note="Acyl-coenzyme A thioesterase 9, mitochondrial"
FT                   /id="PRO_0000364186"
FT   DOMAIN          84..207
FT                   /note="HotDog ACOT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   DOMAIN          287..399
FT                   /note="HotDog ACOT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   MOD_RES         101
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y305"
SQ   SEQUENCE   437 AA;  49853 MW;  945F868C0005FBAD CRC64;
     MRRAALRLCT LSKGLLAPSR GLTQESQNPE NVFHIREVRD KLREIVGAST NWRDHVKAME
     ERKLLHSFLA KSQKGLPPRT MKDSYIEVFL PLGSQPELRE KYLTVQNTVR FGRILEDLDS
     LGVLICYMHN KIHSAKMSPL SIVTALVDKI DMCKKNLSPE QDIKFSGHVS WVGKTSMEVK
     MHMFQLHGND FSPVLDATFV MVARDSENKG PAFVNPLILE SPEEEELFQQ GELNKGRRVA
     FSSTSLLKMA PTAEERTTIH EMFLNTLDPK TISFRSRVLP ANSVWMENSK LKSLDICHPQ
     ERNIFNRIFG GFLMRKAYEL GWATACNFGG SRPFIVAVDD IMFQKPVEVG SLLFLSAQVC
     FTQGNYIQVR VHSEVASLQD KEHMTTNVFH FTFMSEKEVP LVFPRTYGES MLYLDGQRHF
     KSMSAPVTLK RNYVVEP