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Protein

Acyl-coenzyme A thioesterase 9, mitochondrial

Gene

Acot9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionHydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.2.2 3474
3.1.2.20 3474
ReactomeiR-MMU-77289 Mitochondrial Fatty Acid Beta-Oxidation

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1928939 Acot9

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 21Mitochondrion1 PublicationAdd BLAST21
ChainiPRO_000000087022 – 439Acyl-coenzyme A thioesterase 9, mitochondrialAdd BLAST418

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei102N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9R0X4
MaxQBiQ9R0X4
PaxDbiQ9R0X4
PeptideAtlasiQ9R0X4
PRIDEiQ9R0X4

PTM databases

iPTMnetiQ9R0X4
PhosphoSitePlusiQ9R0X4
SwissPalmiQ9R0X4

Expressioni

Gene expression databases

BgeeiENSMUSG00000025287
CleanExiMM_ACOT9
ExpressionAtlasiQ9R0X4 baseline and differential
GenevisibleiQ9R0X4 MM

Interactioni

Subunit structurei

Interacts with NYAP1, NYAP2 and MYO16.1 Publication

Protein-protein interaction databases

BioGridi207923, 1 interactor
IntActiQ9R0X4, 4 interactors
MINTiQ9R0X4
STRINGi10090.ENSMUSP00000026324

Structurei

3D structure databases

ProteinModelPortaliQ9R0X4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini85 – 209HotDog ACOT-type 1PROSITE-ProRule annotationAdd BLAST125
Domaini289 – 401HotDog ACOT-type 2PROSITE-ProRule annotationAdd BLAST113

Sequence similaritiesi

Belongs to the acyl coenzyme A hydrolase family.Curated

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG2763 Eukaryota
ENOG410XSYM LUCA
GeneTreeiENSGT00390000005330
HOGENOMiHOG000188398
HOVERGENiHBG004168
InParanoidiQ9R0X4
KOiK17361
OMAiNSCLFTF
OrthoDBiEOG091G06UC
PhylomeDBiQ9R0X4
TreeFamiTF313352

Family and domain databases

InterProiView protein in InterPro
IPR033120 HOTDOG_ACOT
IPR029069 HotDog_dom_sf
SUPFAMiSSF54637 SSF54637, 2 hits
PROSITEiView protein in PROSITE
PS51770 HOTDOG_ACOT, 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)DescriptionActionsGraphical viewLength
Sequence conflicti219 – 222LIPE → THSG in BAA79193 (Ref. 2) Curated4

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_019736.4
UniGeneiMm.268710

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiACOT9_MOUSE
AccessioniPrimary (citable) accession number: Q9R0X4
Secondary accession number(s): Q545G7, Q9WTJ0, Q9WUZ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 2000
Last modified: April 25, 2018
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health