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Q9Y305 (ACOT9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   Molecular functionHydrolase
Serine esterase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacyl-CoA metabolic process

Inferred from sequence or structural similarity. Source: HGNC

   Cellular_componentmitochondrion

Inferred from sequence or structural similarity. Source: HGNC

   Molecular_functionacetyl-CoA hydrolase activity

Inferred from sequence or structural similarity. Source: HGNC

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion By similarity
Chain22 – 439418Acyl-coenzyme A thioesterase 9, mitochondrial
PRO_0000053812

Amino acid modifications

Modified residue1031N6-acetyllysine Ref.7

Natural variations

Alternative sequence1 – 6060Missing in isoform 3.
VSP_036420
Alternative sequence5 – 3935ALRLC…FHIHE → PC in isoform 2.
VSP_036419
Alternative sequence391E → EACSSIHVNH in isoform 4.
VSP_041093
Natural variant3051N → H in a pancreatic ductal adenocarcinoma sample; somatic mutation. Ref.9
VAR_062668

Experimental info

Sequence conflict1881L → S in BAG51291. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: 1CE2158D4F83D4D6

FASTA43949,902
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 99ADE404D472CEEB
Show »

FASTA40646,355
Isoform 3 [UniParc].

Checksum: AC76325AB9264911
Show »

FASTA37943,207
Isoform 4 [UniParc].

Checksum: AA20C18EF239983D
Show »

FASTA44850,851

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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. expand/collapse author list , 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.
RefSeqNP_001028755.2. NM_001033583.2.
NP_001032248.1. NM_001037171.1.
XP_005274528.1. XM_005274471.1.
XP_005274529.1. XM_005274472.1.
UniGeneHs.298885.

3D structure databases

ProteinModelPortalQ9Y305.
SMRQ9Y305. Positions 104-237, 286-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117132. 8 interactions.
IntActQ9Y305. 7 interactions.
MINTMINT-3085225.
STRING9606.ENSP00000368605.

PTM databases

PhosphoSiteQ9Y305.

Polymorphism databases

DMDM224471815.

Proteomic databases

PaxDbQ9Y305.
PRIDEQ9Y305.

Protocols and materials databases

DNASU23597.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336430; ENSP00000336580; ENSG00000123130. [Q9Y305-1]
ENST00000379295; ENSP00000368597; ENSG00000123130. [Q9Y305-3]
ENST00000379303; ENSP00000368605; ENSG00000123130. [Q9Y305-4]
GeneID23597.
KEGGhsa:23597.
UCSCuc004dao.3. human. [Q9Y305-4]
uc004dap.3. human. [Q9Y305-1]

Organism-specific databases

CTD23597.
GeneCardsGC0XM023629.
HGNCHGNC:17152. ACOT9.
HPAHPA035533.
MIM300862. gene.
neXtProtNX_Q9Y305.
PharmGKBPA142672656.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269414.
HOGENOMHOG000188398.
HOVERGENHBG004168.
InParanoidQ9Y305.
KOK17361.
OMAPWIEALT.
OrthoDBEOG7GQXVJ.
PhylomeDBQ9Y305.
TreeFamTF313352.

Gene expression databases

ArrayExpressQ9Y305.
BgeeQ9Y305.
CleanExHS_ACOT9.
GenevestigatorQ9Y305.

Family and domain databases

InterProIPR006683. Thioestr_supf.
[Graphical view]
PfamPF03061. 4HBT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi23597.
NextBio46262.
PROQ9Y305.
SOURCESearch...

Entry information

Entry nameACOT9_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM