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Protein

Acyl-coenzyme A thioesterase 9, mitochondrial

Gene

Acot9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • acetyl-CoA hydrolase activity Source: HGNC
  • acyl-CoA hydrolase activity Source: MGI
  • carboxylic ester hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  • acyl-CoA metabolic process Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.2.2. 3474.
3.1.2.20. 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 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1928939. Acot9.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: HGNC
Complete GO annotation...

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.
ExpressionAtlasiQ9R0X4. baseline and differential.
GenevisibleiQ9R0X4. MM.

Interactioni

Subunit structurei

Interacts with NYAP1, NYAP2 and MYO16.1 Publication

Protein-protein interaction databases

IntActiQ9R0X4. 3 interactions.
MINTiMINT-4086590.
STRINGi10090.ENSMUSP00000026324.

Structurei

3D structure databases

ProteinModelPortaliQ9R0X4.
SMRiQ9R0X4. Positions 301-415.
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.
OMAiMFQLHGN.
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

« Hide

        10         20         30         40         50
MKRAAIRLWT LNKGLLTHGR GLSQGSQYKI SEPLHIHQVR DKLREIVGVS
60 70 80 90 100
TVWRDHVKAM EERKLLHSFL PKSQKVLPPR KMRDSYIEVL LPLGTDPELR
110 120 130 140 150
DKYVTVQNTV RFGRILEDLD SLGVLVCYMH NHNHSTKMSP LSIVTVLVDK
160 170 180 190 200
IDMCKHSLSP EQDIKFTGHV SWVGNTSMEV KMKMFQLHND EKYWPVLDAT
210 220 230 240 250
FVMVARDSEN KGPAFVNPLI PENKEEEELF KQGELNKSRR IAFSTSSLLK
260 270 280 290 300
VAPSSEERNI IHELFLTTLD PKTISFQSRI LPPKAVWMED TKLKSLDICH
310 320 330 340 350
PQERNVFNRI FGGFLMRKAY ELAWATACSF GGSRPYVVTV DDIMFQKPVE
360 370 380 390 400
VGSLLFLSSQ VCFTQDNYIQ VRVHSEVSSL DSREHMTTNV FHFTFMSEKE
410 420 430
VPLIFPKTYG ESMLYLDGQR HFKSMSTPVT LKKDYPVEP
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 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9R0X4.
SMRiQ9R0X4. Positions 301-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R0X4. 3 interactions.
MINTiMINT-4086590.
STRINGi10090.ENSMUSP00000026324.

PTM databases

PhosphoSiteiQ9R0X4.

Proteomic databases

MaxQBiQ9R0X4.
PaxDbiQ9R0X4.
PRIDEiQ9R0X4.

Protocols and materials databases

DNASUi56360.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23597.
MGIiMGI:1928939. Acot9.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi3.1.2.2. 3474.
3.1.2.20. 3474.

Miscellaneous databases

NextBioi312378.
PROiQ9R0X4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0X4.
CleanExiMM_ACOT9.
ExpressionAtlasiQ9R0X4. baseline and differential.
GenevisibleiQ9R0X4. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 115 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.