Q9Y305 (ACOT9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-coenzyme A thioesterase 9, mitochondrial
Short name=Acyl-CoA thioesterase 9
EC=3.1.2.-

Alternative name(s):
Acyl-CoA thioester hydrolase 9

Gene names

Name:	ACOT9
ORF Names:	CGI-16

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs.
Subunit structure	Interacts with NYAP1, NYAP2 and MYO16 By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the acyl coenzyme A hydrolase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Molecular function	Hydrolase Serine esterase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acyl-CoA metabolic process Inferred from sequence or structural similarity. Source: HGNC
Cellular_component	mitochondrion Inferred from sequence or structural similarity. Source: HGNC
Molecular_function	acetyl-CoA hydrolase activity Inferred from sequence or structural similarity. Source: HGNC carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y305-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform 2 (identifier: Q9Y305-2)

The sequence of this isoform differs from the canonical sequence as follows:
     5-39: ALRLCALGKGQLTPGRGLTQGPQNPKKQGIFHIHE → PC

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9Y305-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9Y305-4)

The sequence of this isoform differs from the canonical sequence as follows:
     39-39: E → EACSSIHVNH

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 21	21	Mitochondrion By similarity
	Chain	22 – 439	418	Acyl-coenzyme A thioesterase 9, mitochondrial		PRO_0000053812
Amino acid modifications
	Modified residue	103	1	N6-acetyllysine Ref.7
Natural variations
	Alternative sequence	1 – 60	60	Missing in isoform 3.		VSP_036420
	Alternative sequence	5 – 39	35	ALRLC…FHIHE → PC in isoform 2.		VSP_036419
	Alternative sequence	39	1	E → EACSSIHVNH in isoform 4.		VSP_041093
	Natural variant	305	1	N → H in a pancreatic ductal adenocarcinoma sample; somatic mutation. Ref.9		VAR_062668
Experimental info
	Sequence conflict	188	1	L → S in BAG51291. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 3, 2009. Version 2. Checksum: 1CE2158D4F83D4D6	FASTA	439	49,902
	10 20 30 40 50 60 MRRAALRLCA LGKGQLTPGR GLTQGPQNPK KQGIFHIHEV RDKLREIVGA STNWRDHVKA 70 80 90 100 110 120 MEERKLLHSF LAKSQDGLPP RRMKDSYIEV LLPLGSEPEL REKYLTVQNT VRFGRILEDL 130 140 150 160 170 180 DSLGVLICYM HNKIHSAKMS PLSIVTALVD KIDMCKKSLS PEQDIKFSGH VSWVGKTSME 190 200 210 220 230 240 VKMQMFQLHG DEFCPVLDAT FVMVARDSEN KGPAFVNPLI PESPEEEELF RQGELNKGRR 250 260 270 280 290 300 IAFSSTSLLK MAPSAEERTT IHEMFLSTLD PKTISFRSRV LPSNAVWMEN SKLKSLEICH 310 320 330 340 350 360 PQERNIFNRI FGGFLMRKAY ELAWATACSF GGSRPFVVAV DDIMFQKPVE VGSLLFLSSQ 370 380 390 400 410 420 VCFTQNNYIQ VRVHSEVASL QEKQHTTTNV FHFTFMSEKE VPLVFPKTYG ESMLYLDGQR 430 HFNSMSGPAT LRKDYLVEP
	Isoform 2 [UniParc]. Checksum: 99ADE404D472CEEB	FASTA	406	46,355
	10 20 30 40 50 60 MRRAPCVRDK LREIVGASTN WRDHVKAMEE RKLLHSFLAK SQDGLPPRRM KDSYIEVLLP 70 80 90 100 110 120 LGSEPELREK YLTVQNTVRF GRILEDLDSL GVLICYMHNK IHSAKMSPLS IVTALVDKID 130 140 150 160 170 180 MCKKSLSPEQ DIKFSGHVSW VGKTSMEVKM QMFQLHGDEF CPVLDATFVM VARDSENKGP 190 200 210 220 230 240 AFVNPLIPES PEEEELFRQG ELNKGRRIAF SSTSLLKMAP SAEERTTIHE MFLSTLDPKT 250 260 270 280 290 300 ISFRSRVLPS NAVWMENSKL KSLEICHPQE RNIFNRIFGG FLMRKAYELA WATACSFGGS 310 320 330 340 350 360 RPFVVAVDDI MFQKPVEVGS LLFLSSQVCF TQNNYIQVRV HSEVASLQEK QHTTTNVFHF 370 380 390 400 TFMSEKEVPL VFPKTYGESM LYLDGQRHFN SMSGPATLRK DYLVEP
	Isoform 3 [UniParc]. Checksum: AC76325AB9264911	FASTA	379	43,207
	10 20 30 40 50 60 MEERKLLHSF LAKSQDGLPP RRMKDSYIEV LLPLGSEPEL REKYLTVQNT VRFGRILEDL 70 80 90 100 110 120 DSLGVLICYM HNKIHSAKMS PLSIVTALVD KIDMCKKSLS PEQDIKFSGH VSWVGKTSME 130 140 150 160 170 180 VKMQMFQLHG DEFCPVLDAT FVMVARDSEN KGPAFVNPLI PESPEEEELF RQGELNKGRR 190 200 210 220 230 240 IAFSSTSLLK MAPSAEERTT IHEMFLSTLD PKTISFRSRV LPSNAVWMEN SKLKSLEICH 250 260 270 280 290 300 PQERNIFNRI FGGFLMRKAY ELAWATACSF GGSRPFVVAV DDIMFQKPVE VGSLLFLSSQ 310 320 330 340 350 360 VCFTQNNYIQ VRVHSEVASL QEKQHTTTNV FHFTFMSEKE VPLVFPKTYG ESMLYLDGQR 370 HFNSMSGPAT LRKDYLVEP
	Isoform 4 [UniParc]. Checksum: AA20C18EF239983D	FASTA	448	50,851
	10 20 30 40 50 60 MRRAALRLCA LGKGQLTPGR GLTQGPQNPK KQGIFHIHEA CSSIHVNHVR DKLREIVGAS 70 80 90 100 110 120 TNWRDHVKAM EERKLLHSFL AKSQDGLPPR RMKDSYIEVL LPLGSEPELR EKYLTVQNTV 130 140 150 160 170 180 RFGRILEDLD SLGVLICYMH NKIHSAKMSP LSIVTALVDK IDMCKKSLSP EQDIKFSGHV 190 200 210 220 230 240 SWVGKTSMEV KMQMFQLHGD EFCPVLDATF VMVARDSENK GPAFVNPLIP ESPEEEELFR 250 260 270 280 290 300 QGELNKGRRI AFSSTSLLKM APSAEERTTI HEMFLSTLDP KTISFRSRVL PSNAVWMENS 310 320 330 340 350 360 KLKSLEICHP QERNIFNRIF GGFLMRKAYE LAWATACSFG GSRPFVVAVD DIMFQKPVEV 370 380 390 400 410 420 GSLLFLSSQV CFTQNNYIQV RVHSEVASLQ EKQHTTTNVF HFTFMSEKEV PLVFPKTYGE 430 440 SMLYLDGQRH FNSMSGPATL RKDYLVEP

References

[1]	"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics." Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C. Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Placenta.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain and Testis.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, MASS SPECTROMETRY.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Core signaling pathways in human pancreatic cancers revealed by global genomic analyses." Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P., Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y. , Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W. Science 321:1801-1806(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-305.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF132950 mRNA. Translation: AAD27725.1. AK024337 mRNA. Translation: BAG51291.1. BX648512 mRNA. No translation available. AC093011 Genomic DNA. No translation available. AC131011 Genomic DNA. No translation available. CH471074 Genomic DNA. Translation: EAW98998.1. BC136671 mRNA. Translation: AAI36672.1. BC144360 mRNA. Translation: AAI44361.1.
IPI	IPI00220710. IPI00646015. IPI00748985. IPI00921986.
RefSeq	NP_001028755.2. NM_001033583.2. NP_001032248.1. NM_001037171.1.
UniGene	Hs.298885.
3D structure databases
ProteinModelPortal	Q9Y305.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y305. 3 interactions.
STRING	9606.ENSP00000368605.
PTM databases
PhosphoSite	Q9Y305.
Polymorphism databases
DMDM	224471815.
Proteomic databases
PaxDb	Q9Y305.
PRIDE	Q9Y305.
Protocols and materials databases
DNASU	23597.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000336430; ENSP00000336580; ENSG00000123130. ENST00000379295; ENSP00000368597; ENSG00000123130. ENST00000379303; ENSP00000368605; ENSG00000123130.
GeneID	23597.
KEGG	hsa:23597.
UCSC	uc004dao.3. human. uc004dap.3. human.
Organism-specific databases
CTD	23597.
GeneCards	GC0XM023629.
HGNC	HGNC:17152. ACOT9.
HPA	HPA035533.
MIM	300862. gene.
neXtProt	NX_Q9Y305.
PharmGKB	PA142672656.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG269414.
HOGENOM	HOG000188398.
HOVERGEN	HBG004168.
InParanoid	Q9Y305.
OMA	TACSFGG.
Gene expression databases
ArrayExpress	Q9Y305.
Bgee	Q9Y305.
CleanEx	HS_ACOT9.
Genevestigator	Q9Y305.
GermOnline	ENSG00000123130. Homo sapiens.
Family and domain databases
InterPro	IPR006683. Thioestr_supf. [Graphical view]
Pfam	PF03061. 4HBT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	23597.
NextBio	46262.
SOURCE	Search...

Entry information

Entry name

ACOT9_HUMAN

Accession

Primary (citable) accession number: Q9Y305
Secondary accession number(s): B3KNC9, B7ZM94

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	March 3, 2009
Last modified:	May 1, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.