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Acyl-coenzyme A thioesterase 8 (Acyl-CoA thioesterase 8) (EC 3.1.2.27) (Choloyl-coenzyme A thioesterase) (HIV-Nef-associated acyl-CoA thioesterase) (PTE-2) (Peroxisomal acyl-coenzyme A thioester hydrolase 1) (PTE-1) (Peroxisomal long-chain acyl-CoA thioesterase 1) (Thioesterase II) (hACTE-III) (hACTEIII) (hTE)

 ACOT8_HUMAN             Reviewed;         319 AA.
O14734; O15261; Q17RX4;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 165.
RecName: Full=Acyl-coenzyme A thioesterase 8;
Short=Acyl-CoA thioesterase 8;
EC=3.1.2.27 {ECO:0000269|PubMed:15194431, ECO:0000269|PubMed:9299485};
AltName: Full=Choloyl-coenzyme A thioesterase;
AltName: Full=HIV-Nef-associated acyl-CoA thioesterase;
AltName: Full=PTE-2;
AltName: Full=Peroxisomal acyl-coenzyme A thioester hydrolase 1;
Short=PTE-1;
AltName: Full=Peroxisomal long-chain acyl-CoA thioesterase 1;
AltName: Full=Thioesterase II;
Short=hACTE-III;
Short=hACTEIII;
Short=hTE;
Name=ACOT8; Synonyms=ACTEIII, PTE1, PTE2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INTERACTION
WITH HIV-1 NEF (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
PubMed=9299485; DOI=10.1006/bbrc.1997.7217;
Watanabe H., Shiratori T., Shoji H., Miyatake S., Okazaki Y.,
Ikuta K., Sato T., Saito T.;
"A novel acyl-CoA thioesterase enhances its enzymatic activity by
direct binding with HIV Nef.";
Biochem. Biophys. Res. Commun. 238:234-239(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH HIV-1 NEF (MICROBIAL
INFECTION), AND TISSUE SPECIFICITY.
TISSUE=Lymphoid tissue;
PubMed=9153233; DOI=10.1074/jbc.272.21.13779;
Liu L.X., Margottin F., Le Gall S., Schwartz O., Selig L.,
Benarous R., Benichou S.;
"Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with
Nef-mediated CD4 down-regulation.";
J. Biol. Chem. 272:13779-13785(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Muscle;
PubMed=10092594; DOI=10.1074/jbc.274.14.9216;
Jones J.M., Nau K., Geraghty M.T., Erdmann R., Gould S.J.;
"Identification of peroxisomal acyl-CoA thioesterases in yeast and
humans.";
J. Biol. Chem. 274:9216-9223(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
HIS-78.
PubMed=15194431; DOI=10.1016/j.yexcr.2004.02.029;
Ishizuka M., Toyama Y., Watanabe H., Fujiki Y., Takeuchi A.,
Yamasaki S., Yuasa S., Miyazaki M., Nakajima N., Taki S., Saito T.;
"Overexpression of human acyl-CoA thioesterase upregulates peroxisome
biogenesis.";
Exp. Cell Res. 297:127-141(2004).
[7]
REVIEW.
PubMed=11755680; DOI=10.1016/S0163-7827(01)00017-0;
Hunt M.C., Alexson S.E.H.;
"The role Acyl-CoA thioesterases play in mediating intracellular lipid
metabolism.";
Prog. Lipid Res. 41:99-130(2002).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Acyl-coenzyme A (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 (PubMed:9299485, PubMed:9153233, PubMed:15194431). Competes
with bile acid CoA:amino acid N-acyltransferase (BAAT) for bile
acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a
preference for medium-length fatty acyl-CoAs (C2 to C20)
(PubMed:9299485, PubMed:9153233). Inactive towards substrates with
more than C20 aliphatic chains (PubMed:9153233). Involved in the
metabolic regulation of peroxisome proliferation
(PubMed:15194431). {ECO:0000269|PubMed:15194431,
ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}.
-!- FUNCTION: (Microbial infection) May mediate Nef-induced down-
regulation of CD4 cell-surface expression (PubMed:9153233).
{ECO:0000269|PubMed:9153233}.
-!- CATALYTIC ACTIVITY: Choloyl-CoA + H(2)O = cholate + CoA.
{ECO:0000269|PubMed:15194431, ECO:0000269|PubMed:9299485}.
-!- ENZYME REGULATION: Inhibited by CoASH (IC(50)=10-15 uM). Also
inhibited by cysteine-reactive agents.
{ECO:0000250|UniProtKB:P58137}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10.1 uM for decanoyl-CoA {ECO:0000269|PubMed:9153233};
Vmax=7.1 umol/min/mg enzyme {ECO:0000269|PubMed:9153233};
-!- SUBUNIT: Homodimer (By similarity).
{ECO:0000250|UniProtKB:P58137}.
-!- SUBUNIT: (Microbial infection) Interacts with human
immunodeficiency virus (HIV-1) Nef (via middle region); this
interaction enhances ACOT8 Acyl-CoA thioesterase activity and
occurs in a Nef myristoylation-independent manner
(PubMed:9299485). According to a second report, the interaction
with HIV-1 Nef occurs in a Nef myristoylation-independent manner
but does not enhance ACOT8 Acyl-CoA thioesterase activity
(PubMed:9153233). {ECO:0000269|PubMed:9153233,
ECO:0000269|PubMed:9299485}.
-!- INTERACTION:
P04601:nef (xeno); NbExp=7; IntAct=EBI-1237371, EBI-6164028;
P50542:PEX5; NbExp=3; IntAct=EBI-1237371, EBI-597835;
Q04864:REL; NbExp=3; IntAct=EBI-1237371, EBI-307352;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10092594}.
Peroxisome matrix {ECO:0000269|PubMed:10092594,
ECO:0000269|PubMed:15194431}. Note=Predominantly localized in the
peroxisome (PubMed:10092594, PubMed:15194431).
{ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:15194431}.
-!- TISSUE SPECIFICITY: Detected in a T-cell line (at protein level).
Ubiquitous (PubMed:9153233, PubMed:9299485).
{ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}.
-!- INDUCTION: Regulated by peroxisome proliferator (such as
Clofibrate), via the peroxisome proliferator-activated receptors
(PPARs). {ECO:0000250}.
-!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF014404; AAB71665.1; -; mRNA.
EMBL; X86032; CAA60024.1; -; mRNA.
EMBL; AF124264; AAD27616.1; -; mRNA.
EMBL; AL008726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC117155; AAI17156.1; -; mRNA.
EMBL; BC117157; AAI17158.1; -; mRNA.
CCDS; CCDS13378.1; -.
PIR; JC5644; JC5644.
RefSeq; NP_005460.2; NM_005469.3.
UniGene; Hs.444776; -.
ProteinModelPortal; O14734; -.
SMR; O14734; -.
BioGrid; 115323; 17.
DIP; DIP-38179N; -.
IntAct; O14734; 10.
MINT; MINT-2998229; -.
STRING; 9606.ENSP00000217455; -.
SwissLipids; SLP:000000591; -.
iPTMnet; O14734; -.
PhosphoSitePlus; O14734; -.
SwissPalm; O14734; -.
BioMuta; ACOT8; -.
EPD; O14734; -.
MaxQB; O14734; -.
PaxDb; O14734; -.
PeptideAtlas; O14734; -.
PRIDE; O14734; -.
DNASU; 10005; -.
Ensembl; ENST00000217455; ENSP00000217455; ENSG00000101473.
GeneID; 10005; -.
KEGG; hsa:10005; -.
UCSC; uc002xqa.3; human.
CTD; 10005; -.
DisGeNET; 10005; -.
EuPathDB; HostDB:ENSG00000101473.16; -.
GeneCards; ACOT8; -.
HGNC; HGNC:15919; ACOT8.
HPA; CAB010261; -.
MIM; 608123; gene.
neXtProt; NX_O14734; -.
OpenTargets; ENSG00000101473; -.
PharmGKB; PA33941; -.
eggNOG; KOG3016; Eukaryota.
eggNOG; COG1946; LUCA.
GeneTree; ENSGT00390000004207; -.
HOGENOM; HOG000246495; -.
HOVERGEN; HBG019167; -.
InParanoid; O14734; -.
KO; K11992; -.
OMA; RHYWVPT; -.
OrthoDB; EOG091G0BLB; -.
PhylomeDB; O14734; -.
TreeFam; TF315124; -.
BRENDA; 3.1.2.2; 2681.
BRENDA; 3.1.2.20; 2681.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA.
Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
GeneWiki; ACOT8; -.
GenomeRNAi; 10005; -.
PRO; PR:O14734; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101473; -.
CleanEx; HS_ACOT8; -.
ExpressionAtlas; O14734; baseline and differential.
Genevisible; O14734; HS.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
GO; GO:0003986; F:acetyl-CoA hydrolase activity; TAS:Reactome.
GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0033882; F:choloyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016289; F:CoA hydrolase activity; TAS:Reactome.
GO; GO:0052815; F:medium-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
GO; GO:0043649; P:dicarboxylic acid catabolic process; IDA:UniProtKB.
GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
GO; GO:0045225; P:negative regulation of CD4 biosynthetic process; IDA:UniProtKB.
GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR003703; Acyl_CoA_thio.
InterPro; IPR029069; HotDog_dom.
PANTHER; PTHR11066; PTHR11066; 1.
SUPFAM; SSF54637; SSF54637; 2.
TIGRFAMs; TIGR00189; tesB; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Host-virus interaction; Hydrolase;
Peroxisome; Peroxisome biogenesis; Reference proteome;
Serine esterase.
CHAIN 1 319 Acyl-coenzyme A thioesterase 8.
/FTId=PRO_0000202152.
MOTIF 317 319 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 232 232 Charge relay system. {ECO:0000250}.
ACT_SITE 254 254 Charge relay system. {ECO:0000250}.
ACT_SITE 304 304 Charge relay system. {ECO:0000250}.
MUTAGEN 78 78 H->A: Reduces Acyl-CoA thioesterase
activity and peroxisome proliferation.
{ECO:0000269|PubMed:15194431}.
CONFLICT 291 293 LWR -> VWS (in Ref. 2; CAA60024).
{ECO:0000305}.
CONFLICT 319 319 L -> R (in Ref. 2; CAA60024).
{ECO:0000305}.
SEQUENCE 319 AA; 35914 MW; 8345C6E5EABF3326 CRC64;
MSSPQAPEDG QGCGDRGDPP GDLRSVLVTT VLNLEPLDED LFRGRHYWVP AKRLFGGQIV
GQALVAAAKS VSEDVHVHSL HCYFVRAGDP KLPVLYQVER TRTGSSFSVR SVKAVQHGKP
IFICQASFQQ AQPSPMQHQF SMPTVPPPEE LLDCETLIDQ YLRDPNLQKR YPLALNRIAA
QEVPIEIKPV NPSPLSQLQR MEPKQMFWVR ARGYIGEGDM KMHCCVAAYI SDYAFLGTAL
LPHQWQHKVH FMVSLDHSMW FHAPFRADHW MLYECESPWA GGSRGLVHGR LWRQDGVLAV
TCAQEGVIRV KPQVSESKL


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