ACOT9_MOUSE
ID ACOT9_MOUSE Reviewed; 439 AA.
AC Q9R0X4; Q545G7; Q9WTJ0; Q9WUZ8;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Acyl-coenzyme A thioesterase 9, mitochondrial;
DE Short=Acyl-CoA thioesterase 9;
DE EC=3.1.2.-;
DE AltName: Full=Acyl coenzyme A thioester hydrolase 2;
DE Short=MTE-2;
DE AltName: Full=Acyl-CoA thioester hydrolase 9;
DE AltName: Full=Mitochondrial 48 kDa acyl-CoA thioester hydrolase 1;
DE Short=Mt-ACT48.1;
DE AltName: Full=Protein U8;
DE AltName: Full=p48;
DE Flags: Precursor;
GN Name=Acot9; Synonyms=Acate2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-41, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10383425; DOI=10.1074/jbc.274.27.19188;
RA Poupon V., Begue B., Gagnon J., Dautry-Varsat A., Cerf-Bensussan N.,
RA Benmerah A.;
RT "Molecular cloning and characterization of MT-ACT48, a novel mitochondrial
RT acyl-CoA thioesterase.";
RL J. Biol. Chem. 274:19188-19194(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AKR/J;
RA Ishizuka Y., Mochizuki R., Tohdoh N.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Embryonic kidney, Kidney, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH NYAP1; NYAP2 AND MYO16.
RX PubMed=21946561; DOI=10.1038/emboj.2011.348;
RA Yokoyama K., Tezuka T., Kotani M., Nakazawa T., Hoshina N., Shimoda Y.,
RA Kakuta S., Sudo K., Watanabe K., Iwakura Y., Yamamoto T.;
RT "NYAP: a phosphoprotein family that links PI3K to WAVE1 signalling in
RT neurons.";
RL EMBO J. 30:4739-4754(2011).
CC -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze
CC the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A
CC (CoASH), providing the potential to regulate intracellular levels of
CC acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs.
CC -!- SUBUNIT: Interacts with NYAP1, NYAP2 and MYO16.
CC {ECO:0000269|PubMed:21946561}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:10383425}.
CC -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family.
CC {ECO:0000305}.
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DR EMBL; AJ238893; CAB45192.1; -; mRNA.
DR EMBL; AB028898; BAA79193.1; -; mRNA.
DR EMBL; AK002892; BAB22437.1; -; mRNA.
DR EMBL; AK009717; BAB26460.1; -; mRNA.
DR EMBL; AK168713; BAE40555.1; -; mRNA.
DR EMBL; AK170876; BAE42086.1; -; mRNA.
DR EMBL; BX005263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX119978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021763; AAH21763.1; -; mRNA.
DR CCDS; CCDS41187.1; -.
DR RefSeq; NP_062710.2; NM_019736.4.
DR AlphaFoldDB; Q9R0X4; -.
DR SMR; Q9R0X4; -.
DR BioGRID; 207923; 7.
DR IntAct; Q9R0X4; 2.
DR MINT; Q9R0X4; -.
DR STRING; 10090.ENSMUSP00000026324; -.
DR iPTMnet; Q9R0X4; -.
DR PhosphoSitePlus; Q9R0X4; -.
DR SwissPalm; Q9R0X4; -.
DR EPD; Q9R0X4; -.
DR jPOST; Q9R0X4; -.
DR MaxQB; Q9R0X4; -.
DR PaxDb; Q9R0X4; -.
DR PeptideAtlas; Q9R0X4; -.
DR PRIDE; Q9R0X4; -.
DR ProteomicsDB; 285655; -.
DR DNASU; 56360; -.
DR Ensembl; ENSMUST00000026324; ENSMUSP00000026324; ENSMUSG00000025287.
DR GeneID; 56360; -.
DR KEGG; mmu:56360; -.
DR UCSC; uc009urs.1; mouse.
DR CTD; 23597; -.
DR MGI; MGI:1928939; Acot9.
DR VEuPathDB; HostDB:ENSMUSG00000025287; -.
DR eggNOG; KOG2763; Eukaryota.
DR GeneTree; ENSGT00390000005330; -.
DR HOGENOM; CLU_032862_2_1_1; -.
DR InParanoid; Q9R0X4; -.
DR OMA; PLAQDPW; -.
DR OrthoDB; 786592at2759; -.
DR PhylomeDB; Q9R0X4; -.
DR TreeFam; TF313352; -.
DR BRENDA; 3.1.2.2; 3474.
DR BRENDA; 3.1.2.20; 3474.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR BioGRID-ORCS; 56360; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Acot9; mouse.
DR PRO; PR:Q9R0X4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9R0X4; protein.
DR Bgee; ENSMUSG00000025287; Expressed in endothelial cell of lymphatic vessel and 246 other tissues.
DR ExpressionAtlas; Q9R0X4; baseline and differential.
DR Genevisible; Q9R0X4; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IDA:HGNC-UCL.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:HGNC-UCL.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0046459; P:short-chain fatty acid metabolic process; IDA:UniProtKB.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Hydrolase; Mitochondrion;
KW Reference proteome; Repeat; Serine esterase; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:10383425"
FT CHAIN 22..439
FT /note="Acyl-coenzyme A thioesterase 9, mitochondrial"
FT /id="PRO_0000000870"
FT DOMAIN 85..209
FT /note="HotDog ACOT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 289..401
FT /note="HotDog ACOT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y305"
FT CONFLICT 219..222
FT /note="LIPE -> THSG (in Ref. 2; BAA79193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 50560 MW; 309CD950D85ACBD0 CRC64;
MKRAAIRLWT LNKGLLTHGR GLSQGSQYKI SEPLHIHQVR DKLREIVGVS TVWRDHVKAM
EERKLLHSFL PKSQKVLPPR KMRDSYIEVL LPLGTDPELR DKYVTVQNTV RFGRILEDLD
SLGVLVCYMH NHNHSTKMSP LSIVTVLVDK IDMCKHSLSP EQDIKFTGHV SWVGNTSMEV
KMKMFQLHND EKYWPVLDAT FVMVARDSEN KGPAFVNPLI PENKEEEELF KQGELNKSRR
IAFSTSSLLK VAPSSEERNI IHELFLTTLD PKTISFQSRI LPPKAVWMED TKLKSLDICH
PQERNVFNRI FGGFLMRKAY ELAWATACSF GGSRPYVVTV DDIMFQKPVE VGSLLFLSSQ
VCFTQDNYIQ VRVHSEVSSL DSREHMTTNV FHFTFMSEKE VPLIFPKTYG ESMLYLDGQR
HFKSMSTPVT LKKDYPVEP
