ACADV_BOVIN
ID ACADV_BOVIN Reviewed; 655 AA.
AC P48818; A5D9C7; Q3SZ66;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Very long-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000305};
DE Short=VLCAD {ECO:0000305};
DE EC=1.3.8.9 {ECO:0000250|UniProtKB:P49748};
DE Flags: Precursor;
GN Name=ACADVL {ECO:0000250|UniProtKB:P49748}; Synonyms=VLCAD;
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 [MRNA].
RC TISSUE=Heart;
RA Zhang X., Liu W., Zhu H., Sun X.;
RT "The molecular cloning and the nucleotide sequence of cDNA encoding the
RT precursor of the mitochondrial very-long-chain acyl-CoA dehydrogenase from
RT bovine heart.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. The
CC first step of fatty acid beta-oxidation consists in the removal of one
CC hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA
CC thioester, resulting in the formation of trans-2-enoyl-CoA. 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.
CC {ECO:0000250|UniProtKB:P49748}.
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:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19182;
CC Evidence={ECO:0000250|UniProtKB:P49748};
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:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297;
CC Evidence={ECO:0000250|UniProtKB:P49748};
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:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC Evidence={ECO:0000250|UniProtKB:P49748};
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:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC Evidence={ECO:0000250|UniProtKB:P49748};
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:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241;
CC Evidence={ECO:0000250|UniProtKB:P49748};
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:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC Evidence={ECO:0000250|UniProtKB:P49748};
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:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229;
CC Evidence={ECO:0000250|UniProtKB:P49748};
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:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P49748}.
CC -!- SUBUNIT: Homodimer. Homodimerizes after import into the mitochondrion.
CC {ECO:0000250|UniProtKB:P49748}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P49748}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49748}.
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; U30817; AAA74051.1; -; mRNA.
DR EMBL; BT030546; ABQ12986.1; -; mRNA.
DR EMBL; BC103104; AAI03105.1; -; mRNA.
DR RefSeq; NP_776919.1; NM_174494.2.
DR AlphaFoldDB; P48818; -.
DR SMR; P48818; -.
DR IntAct; P48818; 35.
DR STRING; 9913.ENSBTAP00000003999; -.
DR PaxDb; P48818; -.
DR PeptideAtlas; P48818; -.
DR PRIDE; P48818; -.
DR Ensembl; ENSBTAT00000003999; ENSBTAP00000003999; ENSBTAG00000003072.
DR GeneID; 282130; -.
DR KEGG; bta:282130; -.
DR CTD; 37; -.
DR VEuPathDB; HostDB:ENSBTAG00000003072; -.
DR VGNC; VGNC:50246; ACADVL.
DR eggNOG; KOG0137; Eukaryota.
DR GeneTree; ENSGT00940000158535; -.
DR HOGENOM; CLU_018204_11_2_1; -.
DR InParanoid; P48818; -.
DR OMA; NAFMGLR; -.
DR OrthoDB; 819314at2759; -.
DR TreeFam; TF105053; -.
DR UniPathway; UPA00660; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000003072; Expressed in corpus luteum and 105 other tissues.
DR ExpressionAtlas; P48818; baseline and differential.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IEA:Ensembl.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
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; 2.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Phosphoprotein; Reference proteome; S-nitrosylation; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 41..655
FT /note="Very long-chain specific acyl-CoA dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000000514"
FT REGION 22..66
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 47..66
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 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 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 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 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"
FT CONFLICT 2
FT /note="R -> Q (in Ref. 1; AAA74051)"
FT /evidence="ECO:0000305"
FT CONFLICT 7..8
FT /note="AQ -> TA (in Ref. 1; AAA74051)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="T -> L (in Ref. 1; AAA74051)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="Q -> T (in Ref. 1; AAA74051)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="R -> P (in Ref. 1; AAA74051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 70649 MW; 677FCBD01AD3DA8B CRC64;
MRAARMAQST GRQLLRLRGV SSWPGELLGQ PRPGPARRPY ASGVAQAAVD QSDSQPSEAS
TREKRANSVS KSFAVGTFKG QLTTDQVFPY PSVLNEDQTQ FLKELVGPVT RFFEEVNDAA
KNDMLERVEE TTMQGLKELG AFGLQVPNEL GGVGLCNTQY ARLVEIVGMY DLGVGIVLGA
HQSIGFKGIL LFGTKAQKEK YLPKLASGET IAAFCLTEPS SGSDAASIRS SAVPSPCGKY
YTLNGSKIWI SNGGLADIFT VFAKTPVTDT ATGAVKEKIT AFVVERSFGG VTHGPPEKKM
GIKASNTAEV YFDGVRVPAE NVLGEVGGGF KVAMHILNNG RFGMAAALAG TMKGIIAKAV
DHAANRTQFG EKIHNFGLIQ EKLARMAMLQ YVTESMAYMV SANMDQGSTD FQIEAAISKI
FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDLRIFRI FEGTNDILRL FVALQGCMDK
GKELSGLGNA LKNPFGNAGL LLGEAGKQLR RRAGLGSGLS LSGIVHQELS RSGELAVQAL
EQFATVVEAK LIKHKKDIIN EQFLLQRLAD SAIDLYAMVV VLSRASRSLS EGHPTAQHEK
MLCDSWCIEA AARIRENMTA LQSDPQQQEL FRNFKSISKA LVERGGVVTS NPLGF
