ACOT9_HUMAN
ID ACOT9_HUMAN Reviewed; 439 AA.
AC Q9Y305; B3KNC9; B7ZM94;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 163.
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; ORFNames=CGI-16;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND IDENTIFICATION BY MASS
RP 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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-305.
RX PubMed=18772397; DOI=10.1126/science.1164368;
RA Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
RA Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T.,
RA Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y.,
RA Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M.,
RA Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E.,
RA Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B.,
RA Velculescu V.E., Kinzler K.W.;
RT "Core signaling pathways in human pancreatic cancers revealed by global
RT genomic analyses.";
RL Science 321:1801-1806(2008).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y305-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y305-2; Sequence=VSP_036419;
CC Name=3;
CC IsoId=Q9Y305-3; Sequence=VSP_036420;
CC Name=4;
CC IsoId=Q9Y305-4; Sequence=VSP_041093;
CC -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family.
CC {ECO:0000305}.
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DR EMBL; AF132950; AAD27725.1; -; mRNA.
DR EMBL; AK024337; BAG51291.1; -; mRNA.
DR EMBL; BX648512; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC093011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98998.1; -; Genomic_DNA.
DR EMBL; BC136671; AAI36672.1; -; mRNA.
DR EMBL; BC144360; AAI44361.1; -; mRNA.
DR CCDS; CCDS35216.1; -. [Q9Y305-1]
DR CCDS; CCDS43924.1; -. [Q9Y305-4]
DR CCDS; CCDS83460.1; -. [Q9Y305-3]
DR RefSeq; NP_001028755.2; NM_001033583.2. [Q9Y305-1]
DR RefSeq; NP_001032248.1; NM_001037171.1. [Q9Y305-4]
DR RefSeq; NP_001317188.1; NM_001330259.1. [Q9Y305-3]
DR AlphaFoldDB; Q9Y305; -.
DR SMR; Q9Y305; -.
DR BioGRID; 117132; 146.
DR IntAct; Q9Y305; 53.
DR MINT; Q9Y305; -.
DR STRING; 9606.ENSP00000368605; -.
DR ChEMBL; CHEMBL4295987; -.
DR GlyGen; Q9Y305; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y305; -.
DR PhosphoSitePlus; Q9Y305; -.
DR SwissPalm; Q9Y305; -.
DR BioMuta; ACOT9; -.
DR DMDM; 224471815; -.
DR EPD; Q9Y305; -.
DR jPOST; Q9Y305; -.
DR MassIVE; Q9Y305; -.
DR MaxQB; Q9Y305; -.
DR PaxDb; Q9Y305; -.
DR PeptideAtlas; Q9Y305; -.
DR PRIDE; Q9Y305; -.
DR ProteomicsDB; 85953; -. [Q9Y305-1]
DR ProteomicsDB; 85954; -. [Q9Y305-2]
DR ProteomicsDB; 85955; -. [Q9Y305-3]
DR ProteomicsDB; 85956; -. [Q9Y305-4]
DR Antibodypedia; 24512; 261 antibodies from 31 providers.
DR DNASU; 23597; -.
DR Ensembl; ENST00000336430.11; ENSP00000336580.7; ENSG00000123130.17. [Q9Y305-1]
DR Ensembl; ENST00000379295.5; ENSP00000368597.1; ENSG00000123130.17. [Q9Y305-3]
DR Ensembl; ENST00000379303.10; ENSP00000368605.5; ENSG00000123130.17. [Q9Y305-4]
DR GeneID; 23597; -.
DR KEGG; hsa:23597; -.
DR MANE-Select; ENST00000379303.10; ENSP00000368605.5; NM_001037171.2; NP_001032248.1. [Q9Y305-4]
DR UCSC; uc004dao.4; human. [Q9Y305-1]
DR CTD; 23597; -.
DR DisGeNET; 23597; -.
DR GeneCards; ACOT9; -.
DR HGNC; HGNC:17152; ACOT9.
DR HPA; ENSG00000123130; Low tissue specificity.
DR MIM; 300862; gene.
DR neXtProt; NX_Q9Y305; -.
DR OpenTargets; ENSG00000123130; -.
DR PharmGKB; PA142672656; -.
DR VEuPathDB; HostDB:ENSG00000123130; -.
DR eggNOG; KOG2763; Eukaryota.
DR GeneTree; ENSGT00390000005330; -.
DR InParanoid; Q9Y305; -.
DR OMA; PLAQDPW; -.
DR OrthoDB; 786592at2759; -.
DR PhylomeDB; Q9Y305; -.
DR TreeFam; TF313352; -.
DR BioCyc; MetaCyc:HS04631-MON; -.
DR PathwayCommons; Q9Y305; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SignaLink; Q9Y305; -.
DR BioGRID-ORCS; 23597; 10 hits in 705 CRISPR screens.
DR ChiTaRS; ACOT9; human.
DR GenomeRNAi; 23597; -.
DR Pharos; Q9Y305; Tbio.
DR PRO; PR:Q9Y305; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y305; protein.
DR Bgee; ENSG00000123130; Expressed in secondary oocyte and 191 other tissues.
DR ExpressionAtlas; Q9Y305; baseline and differential.
DR Genevisible; Q9Y305; HS.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:HGNC-UCL.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; ISS:HGNC-UCL.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; ISS:HGNC-UCL.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Hydrolase; Mitochondrion;
KW Reference proteome; Repeat; Serine esterase; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 22..439
FT /note="Acyl-coenzyme A thioesterase 9, mitochondrial"
FT /id="PRO_0000053812"
FT DOMAIN 84..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 MOD_RES 103
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036420"
FT VAR_SEQ 5..39
FT /note="ALRLCALGKGQLTPGRGLTQGPQNPKKQGIFHIHE -> PC (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10810093"
FT /id="VSP_036419"
FT VAR_SEQ 39
FT /note="E -> EACSSIHVNH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_041093"
FT VARIANT 305
FT /note="N -> H (in a pancreatic ductal adenocarcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:18772397"
FT /id="VAR_062668"
FT CONFLICT 188
FT /note="L -> S (in Ref. 2; BAG51291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 49902 MW; 1CE2158D4F83D4D6 CRC64;
MRRAALRLCA LGKGQLTPGR GLTQGPQNPK KQGIFHIHEV RDKLREIVGA STNWRDHVKA
MEERKLLHSF LAKSQDGLPP RRMKDSYIEV LLPLGSEPEL REKYLTVQNT VRFGRILEDL
DSLGVLICYM HNKIHSAKMS PLSIVTALVD KIDMCKKSLS PEQDIKFSGH VSWVGKTSME
VKMQMFQLHG DEFCPVLDAT FVMVARDSEN KGPAFVNPLI PESPEEEELF RQGELNKGRR
IAFSSTSLLK MAPSAEERTT IHEMFLSTLD PKTISFRSRV LPSNAVWMEN SKLKSLEICH
PQERNIFNRI FGGFLMRKAY ELAWATACSF GGSRPFVVAV DDIMFQKPVE VGSLLFLSSQ
VCFTQNNYIQ VRVHSEVASL QEKQHTTTNV FHFTFMSEKE VPLVFPKTYG ESMLYLDGQR
HFNSMSGPAT LRKDYLVEP
