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THEM4_BOVIN
ID   THEM4_BOVIN             Reviewed;         237 AA.
AC   A1A4L1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Acyl-coenzyme A thioesterase THEM4;
DE            Short=Acyl-CoA thioesterase THEM4;
DE            EC=3.1.2.2 {ECO:0000250|UniProtKB:Q5T1C6};
DE   AltName: Full=Thioesterase superfamily member 4;
DE   Flags: Precursor;
GN   Name=THEM4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has acyl-CoA thioesterase activity towards medium and long-
CC       chain (C14 to C18) fatty acyl-CoA substrates, and probably plays a role
CC       in mitochondrial fatty acid metabolism (By similarity). Plays a role in
CC       the apoptotic process, possibly via its regulation of AKT1 activity (By
CC       similarity). {ECO:0000250|UniProtKB:Q5T1C6}.
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:0000250|UniProtKB:Q5T1C6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC         Evidence={ECO:0000250|UniProtKB:Q5T1C6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate;
CC         Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386;
CC         Evidence={ECO:0000250|UniProtKB:Q5T1C6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC         Evidence={ECO:0000250|UniProtKB:Q5T1C6};
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:0000250|UniProtKB:Q5T1C6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC         Evidence={ECO:0000250|UniProtKB:Q5T1C6};
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:0000250|UniProtKB:Q5T1C6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC         Evidence={ECO:0000250|UniProtKB:Q5T1C6};
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:0000250|UniProtKB:Q5T1C6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC         Evidence={ECO:0000250|UniProtKB:Q5T1C6};
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:Q5T1C6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC         Evidence={ECO:0000250|UniProtKB:Q5T1C6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57368;
CC         Evidence={ECO:0000250|UniProtKB:Q5T1C6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152;
CC         Evidence={ECO:0000250|UniProtKB:Q5T1C6};
CC   -!- SUBUNIT: Homodimer and homotetramer (By similarity). Interacts with
CC       AKT1 in the cytosol (By similarity). {ECO:0000250|UniProtKB:Q5T1C6}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T1C6}.
CC       Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q5T1C6}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q5T1C6}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:Q5T1C6}. Note=Released from the mitochondria
CC       into the cytosol in response to apoptotic stimuli.
CC       {ECO:0000250|UniProtKB:Q5T1C6}.
CC   -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q5T1C6}.
CC   -!- SIMILARITY: Belongs to the THEM4/THEM5 thioesterase family.
CC       {ECO:0000305}.
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DR   EMBL; BC126654; AAI26655.1; -; mRNA.
DR   RefSeq; NP_001073837.1; NM_001080368.1.
DR   AlphaFoldDB; A1A4L1; -.
DR   SMR; A1A4L1; -.
DR   STRING; 9913.ENSBTAP00000043816; -.
DR   PaxDb; A1A4L1; -.
DR   PRIDE; A1A4L1; -.
DR   GeneID; 787270; -.
DR   KEGG; bta:787270; -.
DR   CTD; 117145; -.
DR   eggNOG; KOG4781; Eukaryota.
DR   InParanoid; A1A4L1; -.
DR   OrthoDB; 1322443at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
DR   GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; ISS:UniProtKB.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR006683; Thioestr_dom.
DR   Pfam; PF03061; 4HBT; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cell membrane; Cell projection; Cytoplasm;
KW   Fatty acid metabolism; Hydrolase; Lipid metabolism; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..237
FT                   /note="Acyl-coenzyme A thioesterase THEM4"
FT                   /id="PRO_0000314178"
FT   ACT_SITE        161
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T1C6"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         203..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T1C6"
FT   MOD_RES         55
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UUI3"
FT   MOD_RES         66
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UUI3"
FT   MOD_RES         98
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UUI3"
FT   MOD_RES         204
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UUI3"
SQ   SEQUENCE   237 AA;  26812 MW;  369A2519BA8DEEC4 CRC64;
     MLRSCTAGLR SIWALRGRRE GAPRLSMDLQ PARRLFSTEK VIHKDWALPN PSWSKDLKLL
     FDQFMKKCED GSWERLPSYK RRSTQESEDF KTYFLDPKLV EEERLSQAQL FTRGFEDGLG
     FEYVIFKNND EKRTVCLFQG GPYLQGVPGL LHGGAMATMI DIALGSCTGG AVMTANLNIN
     FKRPVPLCSV VVINSQLDKL EGRKLFLSCN VRSVDEKTLY SEATGLFIKL DPEKSST
 
 
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