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 02-MAR-2010, entry version 64. 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 MEDLINE=20272150; 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 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 [4] 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 [5] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103; LYS-157; LYS-250 AND RP LYS-407, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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 [7] 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 -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; 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 -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family. 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; CH471074; EAW98998.1; -; Genomic_DNA. DR EMBL; BC136671; AAI36672.1; -; mRNA. DR EMBL; BC144360; AAI44361.1; -; mRNA. DR IPI; IPI00220710; -. DR IPI; IPI00748985; -. DR IPI; IPI00921986; -. DR RefSeq; NP_001028755.2; -. DR UniGene; Hs.298885; -. DR PRIDE; Q9Y305; -. DR Ensembl; ENST00000336430; ENSP00000336580; ENSG00000123130; Homo sapiens. DR GeneID; 23597; -. DR KEGG; hsa:23597; -. DR UCSC; uc004dao.1; human. DR CTD; 23597; -. DR GeneCards; GC0XM023629; -. DR HGNC; HGNC:17152; ACOT9. DR PharmGKB; PA142672656; -. DR HOVERGEN; HBG004168; -. DR InParanoid; Q9Y305; -. DR ArrayExpress; Q9Y305; -. DR Bgee; Q9Y305; -. DR CleanEx; HS_ACOT9; -. DR Genevestigator; Q9Y305; -. DR GermOnline; ENSG00000123130; Homo sapiens. DR GO; GO:0005739; C:mitochondrion; ISS:HGNC. DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; ISS:HGNC. DR GO; GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW. DR GO; GO:0006637; P:acyl-CoA metabolic process; ISS:HGNC. DR InterPro; IPR006683; Thioestr_supf. DR Pfam; PF03061; 4HBT; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Hydrolase; KW Mitochondrion; Polymorphism; Serine esterase; Transit peptide. FT TRANSIT 1 21 Mitochondrion (By similarity). FT CHAIN 22 439 Acyl-coenzyme A thioesterase 9, FT mitochondrial. FT /FTId=PRO_0000053812. FT MOD_RES 103 103 N6-acetyllysine. FT MOD_RES 157 157 N6-acetyllysine. FT MOD_RES 250 250 N6-acetyllysine. FT MOD_RES 407 407 N6-acetyllysine. FT VAR_SEQ 1 60 Missing (in isoform 3). FT /FTId=VSP_036420. FT VAR_SEQ 5 39 ALRLCALGKGQLTPGRGLTQGPQNPKKQGIFHIHE -> PC FT (in isoform 2). FT /FTId=VSP_036419. FT VARIANT 305 305 N -> H (in a pancreatic ductal FT adenocarcinoma sample; somatic mutation). FT /FTId=VAR_062668. FT CONFLICT 188 188 L -> S (in Ref. 2; BAG51291). 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 //