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Q9R0X4

- ACOT9_MOUSE

UniProt

Q9R0X4 - ACOT9_MOUSE

Protein

Acyl-coenzyme A thioesterase 9, mitochondrial

Gene

Acot9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. acetyl-CoA hydrolase activity Source: HGNC
    2. acyl-CoA hydrolase activity Source: MGI
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. acyl-CoA metabolic process Source: HGNC

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Enzyme and pathway databases

    BRENDAi3.1.2.2. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 9, mitochondrial (EC:3.1.2.-)
    Short name:
    Acyl-CoA thioesterase 9
    Alternative name(s):
    Acyl coenzyme A thioester hydrolase 2
    Short name:
    MTE-2
    Acyl-CoA thioester hydrolase 9
    Mitochondrial 48 kDa acyl-CoA thioester hydrolase 1
    Short name:
    Mt-ACT48.1
    Protein U8
    p48
    Gene namesi
    Name:Acot9
    Synonyms:Acate2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1928939. Acot9.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: HGNC

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2121Mitochondrion1 PublicationAdd
    BLAST
    Chaini22 – 439418Acyl-coenzyme A thioesterase 9, mitochondrialPRO_0000000870Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei102 – 1021N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9R0X4.
    PaxDbiQ9R0X4.
    PRIDEiQ9R0X4.

    PTM databases

    PhosphoSiteiQ9R0X4.

    Expressioni

    Gene expression databases

    BgeeiQ9R0X4.
    CleanExiMM_ACOT9.
    GenevestigatoriQ9R0X4.

    Interactioni

    Subunit structurei

    Interacts with NYAP1, NYAP2 and MYO16.1 Publication

    Protein-protein interaction databases

    IntActiQ9R0X4. 3 interactions.
    MINTiMINT-4086590.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R0X4.
    SMRiQ9R0X4. Positions 297-400.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acyl coenzyme A hydrolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG269414.
    GeneTreeiENSGT00390000005330.
    HOGENOMiHOG000188398.
    HOVERGENiHBG004168.
    InParanoidiQ9R0X4.
    KOiK17361.
    OMAiYTKVQVR.
    OrthoDBiEOG7GQXVJ.
    PhylomeDBiQ9R0X4.
    TreeFamiTF313352.

    Family and domain databases

    Gene3Di3.10.129.10. 2 hits.
    InterProiIPR029069. HotDog_dom.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9R0X4-1 [UniParc]FASTAAdd to Basket

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    MKRAAIRLWT LNKGLLTHGR GLSQGSQYKI SEPLHIHQVR DKLREIVGVS    50
    TVWRDHVKAM EERKLLHSFL PKSQKVLPPR KMRDSYIEVL LPLGTDPELR 100
    DKYVTVQNTV RFGRILEDLD SLGVLVCYMH NHNHSTKMSP LSIVTVLVDK 150
    IDMCKHSLSP EQDIKFTGHV SWVGNTSMEV KMKMFQLHND EKYWPVLDAT 200
    FVMVARDSEN KGPAFVNPLI PENKEEEELF KQGELNKSRR IAFSTSSLLK 250
    VAPSSEERNI IHELFLTTLD PKTISFQSRI LPPKAVWMED TKLKSLDICH 300
    PQERNVFNRI FGGFLMRKAY ELAWATACSF GGSRPYVVTV DDIMFQKPVE 350
    VGSLLFLSSQ VCFTQDNYIQ VRVHSEVSSL DSREHMTTNV FHFTFMSEKE 400
    VPLIFPKTYG ESMLYLDGQR HFKSMSTPVT LKKDYPVEP 439
    Length:439
    Mass (Da):50,560
    Last modified:May 1, 2000 - v1
    Checksum:i309CD950D85ACBD0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti219 – 2224LIPE → THSG in BAA79193. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ238893 mRNA. Translation: CAB45192.1.
    AB028898 mRNA. Translation: BAA79193.1.
    AK002892 mRNA. Translation: BAB22437.1.
    AK009717 mRNA. Translation: BAB26460.1.
    AK168713 mRNA. Translation: BAE40555.1.
    AK170876 mRNA. Translation: BAE42086.1.
    BX005263, BX119978 Genomic DNA. Translation: CAM23138.1.
    BX119978, BX005263 Genomic DNA. Translation: CAM21953.1.
    BC021763 mRNA. Translation: AAH21763.1.
    CCDSiCCDS41187.1.
    RefSeqiNP_062710.2. NM_019736.3.
    UniGeneiMm.268710.

    Genome annotation databases

    EnsembliENSMUST00000026324; ENSMUSP00000026324; ENSMUSG00000025287.
    GeneIDi56360.
    KEGGimmu:56360.
    UCSCiuc009urs.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ238893 mRNA. Translation: CAB45192.1 .
    AB028898 mRNA. Translation: BAA79193.1 .
    AK002892 mRNA. Translation: BAB22437.1 .
    AK009717 mRNA. Translation: BAB26460.1 .
    AK168713 mRNA. Translation: BAE40555.1 .
    AK170876 mRNA. Translation: BAE42086.1 .
    BX005263 , BX119978 Genomic DNA. Translation: CAM23138.1 .
    BX119978 , BX005263 Genomic DNA. Translation: CAM21953.1 .
    BC021763 mRNA. Translation: AAH21763.1 .
    CCDSi CCDS41187.1.
    RefSeqi NP_062710.2. NM_019736.3.
    UniGenei Mm.268710.

    3D structure databases

    ProteinModelPortali Q9R0X4.
    SMRi Q9R0X4. Positions 297-400.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9R0X4. 3 interactions.
    MINTi MINT-4086590.

    PTM databases

    PhosphoSitei Q9R0X4.

    Proteomic databases

    MaxQBi Q9R0X4.
    PaxDbi Q9R0X4.
    PRIDEi Q9R0X4.

    Protocols and materials databases

    DNASUi 56360.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026324 ; ENSMUSP00000026324 ; ENSMUSG00000025287 .
    GeneIDi 56360.
    KEGGi mmu:56360.
    UCSCi uc009urs.1. mouse.

    Organism-specific databases

    CTDi 23597.
    MGIi MGI:1928939. Acot9.

    Phylogenomic databases

    eggNOGi NOG269414.
    GeneTreei ENSGT00390000005330.
    HOGENOMi HOG000188398.
    HOVERGENi HBG004168.
    InParanoidi Q9R0X4.
    KOi K17361.
    OMAi YTKVQVR.
    OrthoDBi EOG7GQXVJ.
    PhylomeDBi Q9R0X4.
    TreeFami TF313352.

    Enzyme and pathway databases

    BRENDAi 3.1.2.2. 3474.

    Miscellaneous databases

    NextBioi 312378.
    PROi Q9R0X4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9R0X4.
    CleanExi MM_ACOT9.
    Genevestigatori Q9R0X4.

    Family and domain databases

    Gene3Di 3.10.129.10. 2 hits.
    InterProi IPR029069. HotDog_dom.
    [Graphical view ]
    SUPFAMi SSF54637. SSF54637. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesterase."
      Poupon V., Begue B., Gagnon J., Dautry-Varsat A., Cerf-Bensussan N., Benmerah A.
      J. Biol. Chem. 274:19188-19194(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-41, SUBCELLULAR LOCATION.
    2. Ishizuka Y., Mochizuki R., Tohdoh N.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: AKR.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Dendritic cell, Embryonic kidney, Kidney and Tongue.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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].
      Strain: FVB/N.
      Tissue: Mammary gland.
    6. "NYAP: a phosphoprotein family that links PI3K to WAVE1 signalling in neurons."
      Yokoyama K., Tezuka T., Kotani M., Nakazawa T., Hoshina N., Shimoda Y., Kakuta S., Sudo K., Watanabe K., Iwakura Y., Yamamoto T.
      EMBO J. 30:4739-4754(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NYAP1; NYAP2 AND MYO16.

    Entry informationi

    Entry nameiACOT9_MOUSE
    AccessioniPrimary (citable) accession number: Q9R0X4
    Secondary accession number(s): Q545G7, Q9WTJ0, Q9WUZ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3