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ACADV_RAT
ID   ACADV_RAT               Reviewed;         655 AA.
AC   P45953;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Very long-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000305|PubMed:1730632};
DE            Short=VLCAD {ECO:0000303|PubMed:8034667};
DE            EC=1.3.8.9 {ECO:0000269|PubMed:1730632, ECO:0000269|PubMed:8034667};
DE   Flags: Precursor;
GN   Name=Acadvl {ECO:0000312|RGD:2014};
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP   ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=8034667; DOI=10.1016/s0021-9258(17)32278-0;
RA   Aoyama T., Ueno I., Kamijo T., Hashimoto T.;
RT   "Rat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial acyl-CoA
RT   dehydrogenase gene product, is a rate-limiting enzyme in long-chain fatty
RT   acid beta-oxidation system. cDNA and deduced amino acid sequence and
RT   distinct specificities of the cDNA-expressed protein.";
RL   J. Biol. Chem. 269:19088-19094(1994).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, SUBSTRATE SPECIFICITY,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=1730632; DOI=10.1016/s0021-9258(18)48390-1;
RA   Izai K., Uchida Y., Orii T., Yamamoto S., Hashimoto T.;
RT   "Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. I.
RT   Purification and properties of very-long-chain acyl-coenzyme A
RT   dehydrogenase.";
RL   J. Biol. Chem. 267:1027-1033(1992).
CC   -!- FUNCTION: Very long-chain specific acyl-CoA dehydrogenase is one of the
CC       acyl-CoA dehydrogenases that catalyze the first step of mitochondrial
CC       fatty acid beta-oxidation, an aerobic process breaking down fatty acids
CC       into acetyl-CoA and allowing the production of energy from fats
CC       (PubMed:8034667, PubMed:1730632). The first step of fatty acid beta-
CC       oxidation consists in the removal of one hydrogen from C-2 and C-3 of
CC       the straight-chain fatty acyl-CoA thioester, resulting in the formation
CC       of trans-2-enoyl-CoA (PubMed:8034667, PubMed:1730632). Among the
CC       different mitochondrial acyl-CoA dehydrogenases, very long-chain
CC       specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with
CC       saturated 12 to 24 carbons long primary chains (PubMed:1730632).
CC       {ECO:0000269|PubMed:1730632, ECO:0000269|PubMed:8034667}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a very-long-chain 2,3-saturated fatty acyl-CoA + H(+) +
CC         oxidized [electron-transfer flavoprotein] = a very-long-chain (2E)-
CC         enoyl-CoA + reduced [electron-transfer flavoprotein];
CC         Xref=Rhea:RHEA:19181, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:83724, ChEBI:CHEBI:83728; EC=1.3.8.9;
CC         Evidence={ECO:0000269|PubMed:1730632, ECO:0000269|PubMed:8034667};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19182;
CC         Evidence={ECO:0000305|PubMed:1730632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC         Evidence={ECO:0000269|PubMed:1730632};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297;
CC         Evidence={ECO:0000305|PubMed:1730632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC         tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61405;
CC         Evidence={ECO:0000269|PubMed:1730632};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC         Evidence={ECO:0000305|PubMed:1730632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer
CC         flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:61526;
CC         Evidence={ECO:0000269|PubMed:1730632, ECO:0000269|PubMed:8034667};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC         Evidence={ECO:0000305|PubMed:1730632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer
CC         flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:71412;
CC         Evidence={ECO:0000269|PubMed:1730632, ECO:0000269|PubMed:8034667};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241;
CC         Evidence={ECO:0000305|PubMed:1730632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:74691;
CC         Evidence={ECO:0000269|PubMed:1730632};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC         Evidence={ECO:0000305|PubMed:1730632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=docosanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:65059, ChEBI:CHEBI:74692;
CC         Evidence={ECO:0000269|PubMed:1730632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC         tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693;
CC         Evidence={ECO:0000269|PubMed:1730632};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233;
CC         Evidence={ECO:0000305|PubMed:1730632};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:1730632};
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC       {ECO:0000269|PubMed:1730632, ECO:0000269|PubMed:8034667}.
CC   -!- SUBUNIT: Homodimer (PubMed:1730632). Homodimerizes after import into
CC       the mitochondrion (By similarity). {ECO:0000250|UniProtKB:P49748,
CC       ECO:0000269|PubMed:1730632}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:1730632, ECO:0000269|PubMed:8034667}; Peripheral
CC       membrane protein {ECO:0000250|UniProtKB:P49748}.
CC   -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC       {ECO:0000269|PubMed:8034667}.
CC   -!- PTM: S-nitrosylation at Cys-237 in liver improves catalytic efficiency.
CC       {ECO:0000250|UniProtKB:P50544}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; D30647; BAA06331.1; -; mRNA.
DR   PIR; A54872; A54872.
DR   RefSeq; NP_037023.1; NM_012891.2.
DR   AlphaFoldDB; P45953; -.
DR   SMR; P45953; -.
DR   BioGRID; 247402; 2.
DR   STRING; 10116.ENSRNOP00000024973; -.
DR   ChEMBL; CHEMBL2176830; -.
DR   SwissLipids; SLP:000001587; -.
DR   CarbonylDB; P45953; -.
DR   iPTMnet; P45953; -.
DR   PhosphoSitePlus; P45953; -.
DR   jPOST; P45953; -.
DR   PaxDb; P45953; -.
DR   PRIDE; P45953; -.
DR   GeneID; 25363; -.
DR   KEGG; rno:25363; -.
DR   UCSC; RGD:2014; rat.
DR   CTD; 37; -.
DR   RGD; 2014; Acadvl.
DR   eggNOG; KOG0137; Eukaryota.
DR   InParanoid; P45953; -.
DR   OrthoDB; 819314at2759; -.
DR   PhylomeDB; P45953; -.
DR   Reactome; R-RNO-77305; Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
DR   UniPathway; UPA00660; -.
DR   PRO; PR:P45953; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:RGD.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:RGD.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IDA:RGD.
DR   GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IDA:RGD.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IDA:RGD.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
DR   GO; GO:0009062; P:fatty acid catabolic process; ISO:RGD.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISO:RGD.
DR   GO; GO:0046322; P:negative regulation of fatty acid oxidation; ISO:RGD.
DR   GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:RGD.
DR   GO; GO:0009409; P:response to cold; ISO:RGD.
DR   GO; GO:0001659; P:temperature homeostasis; ISO:RGD.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; FAD; Fatty acid metabolism;
KW   Flavoprotein; Lipid metabolism; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; S-nitrosylation; Transit peptide.
FT   TRANSIT         1..40
FT                   /note="Mitochondrion"
FT   CHAIN           41..655
FT                   /note="Very long-chain specific acyl-CoA dehydrogenase,
FT                   mitochondrial"
FT                   /id="PRO_0000000518"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          41..482
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   REGION          483..516
FT                   /note="Membrane-anchoring"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   COMPBIAS        23..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        462
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   BINDING         214..223
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   BINDING         249..251
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   BINDING         461..463
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   BINDING         464..466
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   BINDING         562
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   MOD_RES         51
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         71
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         71
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         127
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         127
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         195
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         237
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         239
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   MOD_RES         239
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         268
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         276
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         276
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         278
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         278
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         298
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         316
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         331
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   MOD_RES         331
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         372
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         482
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         482
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   MOD_RES         522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49748"
FT   MOD_RES         550
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         556
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         556
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
FT   MOD_RES         639
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50544"
SQ   SEQUENCE   655 AA;  70749 MW;  E808EDEB0E4595D7 CRC64;
     MQSARMTPSV GRQLLRLGAR SSRSAALQGQ PRPTSAQRLY ASEATQAVLE KPETLSSDAS
     TREKPARAES KSFAVGMFKG QLTTDQVFPY PSVLNEGQTQ FLKELVGPVA RFFEEVNDPA
     KNDSLEKVEE DTLQGLKELG AFGLQVPSEL GGLGLSNTQY ARLAEIVGMH DLGVSVTLGA
     HQSIGFKGIL LYGTKAQKEK YLPRVASGQA LAAFCLTEPS SGSDVASIRS SAVPSPCGKY
     YTLNGSKIWI SNGGLADIFT VFAKTPIKDA ATGAVKEKIT AFVVERSFGG VTHGLPEKKM
     GIKASNTSEV YFDGVKVPAE NVLGEVGDGF KVAVNILNNG RFGMAATLAG TMKAIIAKAV
     DHATNRTQFG DKIHNFGVIQ EKLARMAILQ YVTESMAYML SANMDQGFKD FQIEAAISKI
     FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDIRIFRI FEGTNDILRL FVALQGCMDK
     GKELTGLGNA LKNPLGNVGL LIGEASKQLR RRTGIGSGLS LSGIVHPELS RSGELAVQAL
     EQFATVVEAK LMKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGYPTAQHEK
     MLCDSWCIEA ATRIRENMAS LQSNPQQQEL FRNFRSISKA MVENGGLVTS NPLRV
 
 
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