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 14-OCT-2015, entry version 113. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., 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., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA 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., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA 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., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA 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., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA 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., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RP 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., RA Walther T.C., 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., RA Buerckstuemmer T., 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., RA Ayoub D., 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., RA Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., RA Nikolsky Y., Hartigan J., Smith D.R., Hidalgo M., Leach S.D., RA Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C., RA Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N., RA Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.; RT "Core signaling pathways in human pancreatic cancers revealed by RT global genomic analyses."; RL Science 321:1801-1806(2008). CC -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that CC catalyze the hydrolysis of acyl-CoAs to the free fatty acid and CC coenzyme A (CoASH), providing the potential to regulate CC intracellular levels of acyl-CoAs, free fatty acids and CoASH. CC 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 Note=No experimental confirmation available.; CC Name=2; CC IsoId=Q9Y305-2; Sequence=VSP_036419; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=Q9Y305-3; Sequence=VSP_036420; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=Q9Y305-4; Sequence=VSP_041093; CC -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 HotDog ACOT-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU01106}. 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; 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 RefSeq; NP_001028755.2; NM_001033583.2. [Q9Y305-1] DR RefSeq; NP_001032248.1; NM_001037171.1. [Q9Y305-4] DR RefSeq; XP_005274529.1; XM_005274472.1. [Q9Y305-3] DR UniGene; Hs.298885; -. DR ProteinModelPortal; Q9Y305; -. DR SMR; Q9Y305; 288-415. DR BioGrid; 117132; 25. DR IntAct; Q9Y305; 8. DR MINT; MINT-3085225; -. DR STRING; 9606.ENSP00000368605; -. DR PhosphoSite; Q9Y305; -. DR BioMuta; ACOT9; -. DR DMDM; 224471815; -. DR MaxQB; Q9Y305; -. DR PaxDb; Q9Y305; -. DR PRIDE; Q9Y305; -. DR DNASU; 23597; -. DR Ensembl; ENST00000336430; ENSP00000336580; ENSG00000123130. [Q9Y305-1] DR Ensembl; ENST00000379295; ENSP00000368597; ENSG00000123130. [Q9Y305-3] DR Ensembl; ENST00000379303; ENSP00000368605; ENSG00000123130. [Q9Y305-4] DR GeneID; 23597; -. DR KEGG; hsa:23597; -. DR UCSC; uc004dao.3; human. [Q9Y305-4] DR UCSC; uc004dap.3; human. [Q9Y305-1] DR CTD; 23597; -. DR GeneCards; ACOT9; -. DR HGNC; HGNC:17152; ACOT9. DR HPA; HPA035533; -. DR MIM; 300862; gene. DR neXtProt; NX_Q9Y305; -. DR PharmGKB; PA142672656; -. DR eggNOG; NOG269414; -. DR GeneTree; ENSGT00390000005330; -. DR HOGENOM; HOG000188398; -. DR HOVERGEN; HBG004168; -. DR InParanoid; Q9Y305; -. DR KO; K17361; -. DR OMA; MFQLHGN; -. DR OrthoDB; EOG7GQXVJ; -. DR PhylomeDB; Q9Y305; -. DR TreeFam; TF313352; -. DR GenomeRNAi; 23597; -. DR NextBio; 46262; -. DR PRO; PR:Q9Y305; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; Q9Y305; -. DR CleanEx; HS_ACOT9; -. DR ExpressionAtlas; Q9Y305; baseline and differential. DR Genevisible; Q9Y305; HS. DR GO; GO:0005739; C:mitochondrion; ISS:HGNC. DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; ISS:HGNC. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0006637; P:acyl-CoA metabolic process; ISS:HGNC. DR Gene3D; 3.10.129.10; -; 2. DR InterPro; IPR029069; HotDog_dom. DR InterPro; IPR006683; Thioestr_supf. DR Pfam; PF03061; 4HBT; 1. DR SUPFAM; SSF54637; SSF54637; 2. DR PROSITE; PS51770; HOTDOG_ACOT; 2. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Hydrolase; KW Mitochondrion; Polymorphism; Reference proteome; Repeat; KW Serine esterase; Transit peptide. FT TRANSIT 1 21 Mitochondrion. {ECO:0000250}. FT CHAIN 22 439 Acyl-coenzyme A thioesterase 9, FT mitochondrial. FT /FTId=PRO_0000053812. FT DOMAIN 84 209 HotDog ACOT-type 1. {ECO:0000255|PROSITE- FT ProRule:PRU01106}. FT DOMAIN 289 401 HotDog ACOT-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU01106}. FT MOD_RES 103 103 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT VAR_SEQ 1 60 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_036420. FT VAR_SEQ 5 39 ALRLCALGKGQLTPGRGLTQGPQNPKKQGIFHIHE -> PC FT (in isoform 2). FT {ECO:0000303|PubMed:10810093}. FT /FTId=VSP_036419. FT VAR_SEQ 39 39 E -> EACSSIHVNH (in isoform 4). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_041093. FT VARIANT 305 305 N -> H (in a pancreatic ductal FT adenocarcinoma sample; somatic mutation). FT {ECO:0000269|PubMed:18772397}. FT /FTId=VAR_062668. FT CONFLICT 188 188 L -> S (in Ref. 2; BAG51291). FT {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 //