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ACOT2_RAT
ID   ACOT2_RAT               Reviewed;         453 AA.
AC   O55171; O88268;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Acyl-coenzyme A thioesterase 2, mitochondrial;
DE            Short=Acyl-CoA thioesterase 2;
DE            EC=3.1.2.2 {ECO:0000269|PubMed:7744868};
DE   AltName: Full=ARTISt/p43;
DE   AltName: Full=Acyl coenzyme A thioester hydrolase;
DE   AltName: Full=MTE-I {ECO:0000303|PubMed:7744868};
DE   AltName: Full=Very-long-chain acyl-CoA thioesterase {ECO:0000303|PubMed:7744868};
DE   Flags: Precursor;
GN   Name=Acot2; Synonyms=Mte1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 147-166 AND 168-178.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=9445388; DOI=10.1042/bj3290601;
RA   Svensson L.T., Engberg S.T., Aoyama T., Usuda N., Alexson S.E.H.,
RA   Hashimoto T.;
RT   "Molecular cloning and characterization of a mitochondrial peroxisome
RT   proliferator-induced acyl-CoA thioesterase from rat liver.";
RL   Biochem. J. 329:601-608(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-197.
RC   TISSUE=Liver;
RX   PubMed=9703974; DOI=10.1006/bbrc.1998.9048;
RA   Yamada J., Suga K., Furihata T., Kitahara M., Watanabe T., Hosokawa M.,
RA   Satoh T., Suga T.;
RT   "cDNA cloning and genomic organization of peroxisome proliferator-inducible
RT   long-chain acyl-CoA hydrolase from rat liver cytosol.";
RL   Biochem. Biophys. Res. Commun. 248:608-612(1998).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION BY
RP   DI(2-ETHYLHEXYL)PHTALATE, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=7744868; DOI=10.1074/jbc.270.20.12177;
RA   Svensson L.T., Alexson S.E., Hiltunen J.K.;
RT   "Very long chain and long chain acyl-CoA thioesterases in rat liver
RT   mitochondria. Identification, purification, characterization, and induction
RT   by peroxisome proliferators.";
RL   J. Biol. Chem. 270:12177-12183(1995).
CC   -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC       and coenzyme A (CoASH), regulating their respective intracellular
CC       levels (By similarity). Displays higher activity toward long chain acyl
CC       CoAs (C14-C20) (PubMed:7744868). The enzyme is involved in enhancing
CC       the hepatic fatty acid oxidation in mitochondria (By similarity).
CC       {ECO:0000250|UniProtKB:Q9QYR9, ECO:0000269|PubMed:7744868}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC         Evidence={ECO:0000269|PubMed:7744868};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC         Evidence={ECO:0000305|PubMed:7744868};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC         Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC         Evidence={ECO:0000269|PubMed:7744868};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC         Evidence={ECO:0000305|PubMed:7744868};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC         Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC         Evidence={ECO:0000269|PubMed:7744868};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC         Evidence={ECO:0000305|PubMed:7744868};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+);
CC         Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380;
CC         Evidence={ECO:0000269|PubMed:7744868};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC         Evidence={ECO:0000305|PubMed:7744868};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+);
CC         Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC         Evidence={ECO:0000269|PubMed:7744868};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC         Evidence={ECO:0000305|PubMed:7744868};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC         Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC         Evidence={ECO:0000269|PubMed:7744868};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC         Evidence={ECO:0000305|PubMed:7744868};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+);
CC         Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC         Evidence={ECO:0000250|UniProtKB:P49753};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC         Evidence={ECO:0000250|UniProtKB:P49753};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+);
CC         Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540;
CC         Evidence={ECO:0000250|UniProtKB:P49753};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132;
CC         Evidence={ECO:0000250|UniProtKB:P49753};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9E)-octadecenoyl-CoA + H2O = (9E)-octadecenoate + CoA + H(+);
CC         Xref=Rhea:RHEA:40723, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30825, ChEBI:CHEBI:57287, ChEBI:CHEBI:77537;
CC         Evidence={ECO:0000250|UniProtKB:P49753};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724;
CC         Evidence={ECO:0000250|UniProtKB:P49753};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate
CC         + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57383; Evidence={ECO:0000250|UniProtKB:Q9QYR9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144;
CC         Evidence={ECO:0000250|UniProtKB:Q9QYR9};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=16 uM for C10-acyl-CoA {ECO:0000269|PubMed:7744868};
CC         KM=5 uM for C12-acyl-CoA {ECO:0000269|PubMed:7744868};
CC         KM=3 uM for C14-acyl-CoA {ECO:0000269|PubMed:7744868};
CC         KM=6 uM for C16-acyl-CoA {ECO:0000269|PubMed:7744868};
CC         KM=3 uM for C18-acyl-CoA {ECO:0000269|PubMed:7744868};
CC         KM=2 uM for C20-acyl-CoA {ECO:0000269|PubMed:7744868};
CC         Vmax=1 umol/min/mg enzyme with C10-acyl-CoA as substrate
CC         {ECO:0000269|PubMed:7744868};
CC         Vmax=2.2 umol/min/mg enzyme with C12-acyl-CoA as substrate
CC         {ECO:0000269|PubMed:7744868};
CC         Vmax=4.2 umol/min/mg enzyme with C14-acyl-CoA as substrate
CC         {ECO:0000269|PubMed:7744868};
CC         Vmax=4.5 umol/min/mg enzyme with C16-acyl-CoA as substrate
CC         {ECO:0000269|PubMed:7744868};
CC         Vmax=3.3 umol/min/mg enzyme with C18-acyl-CoA as substrate
CC         {ECO:0000269|PubMed:7744868};
CC         Vmax=3.1 umol/min/mg enzyme with C20-acyl-CoA as substrate
CC         {ECO:0000269|PubMed:7744868};
CC       pH dependence:
CC         Optimum pH is 8-9. {ECO:0000269|PubMed:7744868};
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000305|PubMed:7744868}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7744868}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:7744868}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in heart and brown fat.
CC       Strongly induced in liver, and weakly in kidney, in peroxisome
CC       proliferator treated rat. {ECO:0000269|PubMed:7744868}.
CC   -!- INDUCTION: Regulated by peroxisome proliferator, via the peroxisome
CC       proliferator-activated receptors (PPARs). {ECO:0000269|PubMed:7744868}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; Y09333; CAA70513.1; -; mRNA.
DR   EMBL; AB010429; BAA32539.1; -; mRNA.
DR   AlphaFoldDB; O55171; -.
DR   SMR; O55171; -.
DR   STRING; 10116.ENSRNOP00000013515; -.
DR   ESTHER; ratno-acot2; Acyl-CoA_Thioesterase.
DR   iPTMnet; O55171; -.
DR   PhosphoSitePlus; O55171; -.
DR   jPOST; O55171; -.
DR   PaxDb; O55171; -.
DR   PRIDE; O55171; -.
DR   UCSC; RGD:621055; rat.
DR   RGD; 621055; Acot2.
DR   eggNOG; ENOG502QQ8Z; Eukaryota.
DR   InParanoid; O55171; -.
DR   PhylomeDB; O55171; -.
DR   BRENDA; 3.1.2.2; 5301.
DR   BRENDA; 3.1.2.20; 5301.
DR   Reactome; R-RNO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   Reactome; R-RNO-9033241; Peroxisomal protein import.
DR   UniPathway; UPA00199; -.
DR   PRO; PR:O55171; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:RGD.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:RGD.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IDA:RGD.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:RGD.
DR   GO; GO:0070849; P:response to epidermal growth factor; IEP:RGD.
DR   GO; GO:0009725; P:response to hormone; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IDA:HGNC-UCL.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0042760; P:very long-chain fatty acid catabolic process; IDA:RGD.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:RGD.
DR   Gene3D; 2.60.40.2240; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR   InterPro; IPR014940; BAAT_C.
DR   InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR   InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR   Pfam; PF08840; BAAT_C; 1.
DR   Pfam; PF04775; Bile_Hydr_Trans; 1.
DR   PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Fatty acid metabolism; Hydrolase;
KW   Lipid metabolism; Mitochondrion; Reference proteome; Serine esterase;
KW   Transit peptide.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..453
FT                   /note="Acyl-coenzyme A thioesterase 2, mitochondrial"
FT                   /id="PRO_0000034066"
FT   ACT_SITE        273
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P49753"
FT   ACT_SITE        365
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P49753"
FT   ACT_SITE        399
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P49753"
FT   MOD_RES         83
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QYR9"
FT   MOD_RES         447
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QYR9"
FT   CONFLICT        51..52
FT                   /note="GS -> AG (in Ref. 2; BAA32539)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90..92
FT                   /note="HAR -> RAL (in Ref. 2; BAA32539)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="W -> R (in Ref. 2; BAA32539)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   453 AA;  49701 MW;  F48C2C61475072B2 CRC64;
     MVASSFAVLR ASRLCQWGWK SWTQLSGPPP LSTGGRTTFA RTNATLSLEP GSRSCWDEPL
     SITVRGLAPE QPVTLRAALR DEKGALFRAH ARYRADAGGE LDLARAPALG GSFTGLEPMG
     LIWAMEPERP LWRLVKRDVQ KPYVVELEVL DGHEPDGGQR LAQAVHERHF MAPGVRRVPV
     RDGRVRATLF LPPEPGPFPE IIDLFGVGGG LLEYRASLLA GKGFAVMALA YYNYDDLPKT
     METMRIEYFE EAVNYLRGHP EVKGPGIGLL GISKGGELGL AMASFLKGIT AAVVINGSVA
     AVGNTVCYKD ETIPPVSLLR DKVKMTKDGL LDVVEALQSP LVDKKSFIPV ERSDTTFLFL
     VGQDDHNWKS EFYAREASKR LQAHGKEKPQ IICYPEAGHY IEPPYFPLCS AGMHLLVGAN
     ITFGGEPKPH SVAQLDAWQQ LQTFFHKQLS GKS
 
 
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