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Reviewed, UniProtKB/Swiss-Prot Q9Y305 (ACOT9_HUMAN)

Last modified December 15, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete 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.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the acyl coenzyme A hydrolase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Molecular functionHydrolase
Serine esterase
   PTMAcetylation
   Technical termComplete 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

carboxylesterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 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.

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.6
Modified residue1571N6-acetyllysine Ref.6
Modified residue2501N6-acetyllysine Ref.6
Modified residue4071N6-acetyllysine Ref.6

Natural variations

Alternative sequence1 – 6060Missing in isoform 3.
VSP_036420
Alternative sequence5 – 3935ALRLC…FHIHE → PC in isoform 2.
VSP_036419

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.

Checksum: 99ADE404D472CEEB
Show »

FASTA40646,355
Isoform 3.

Checksum: AC76325AB9264911
Show »

FASTA37943,207

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: 10810093] [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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Placenta.
[3]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].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Testis.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103; LYS-157; LYS-250 AND LYS-407, MASS SPECTROMETRY.

Cross-references

Sequence databases

AF132950 mRNA. Translation: AAD27725.1.
AK024337 mRNA. Translation: BAG51291.1.
CH471074 Genomic DNA. Translation: EAW98998.1.
BC136671 mRNA. Translation: AAI36672.1.
BC144360 mRNA. Translation: AAI44361.1.
IPIIPI00220710.
IPI00748985.
IPI00921986.
RefSeqNP_001028755.2.
UniGeneHs.298885

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ9Y305.

Genome annotation databases

EnsemblENST00000336430; ENSP00000336580; ENSG00000123130; Homo sapiens. [Genome view]
GeneID23597.
KEGGhsa:23597.
UCSCuc004dao.1. human.

Organism-specific databases

CTD23597.
GeneCardsGC0XM023629.
HGNCHGNC:17152. ACOT9.
PharmGKBPA142672656.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9Y305.
InParanoidQ9Y305.

Gene expression databases

ArrayExpressQ9Y305.
BgeeQ9Y305.
CleanExHS_ACOT9.
GenevestigatorQ9Y305.
GermOnlineENSG00000123130. Homo sapiens.

Family and domain databases

ProtoNetSearch...

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: December 15, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents