ACADS_HUMAN
ID ACADS_HUMAN Reviewed; 412 AA.
AC P16219; P78331;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Short-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE Short=SCAD;
DE EC=1.3.8.1 {ECO:0000269|PubMed:21237683};
DE AltName: Full=Butyryl-CoA dehydrogenase;
DE Flags: Precursor;
GN Name=ACADS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2565344; DOI=10.1172/jci114058;
RA Naito E., Ozasa H., Ikeda Y., Tanaka K.;
RT "Molecular cloning and nucleotide sequence of complementary DNAs encoding
RT human short chain acyl-coenzyme A dehydrogenase and the study of the
RT molecular basis of human short chain acyl-coenzyme A dehydrogenase
RT deficiency.";
RL J. Clin. Invest. 83:1605-1613(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9383286; DOI=10.1007/s003359900612;
RA Corydon M.J., Andresen B.S., Bross P., Kjeldsen M., Andreasen P.H.,
RA Eiberg H., Koelvraa S., Gregersen N.;
RT "Structural organization of the human short-chain acyl-CoA dehydrogenase
RT gene.";
RL Mamm. Genome 8:922-926(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V.,
RA Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M.,
RA Lathrop M., Cox R.D., Bell G.I.;
RT "Transcription map of the 5cM region surrounding the hepatocyte nuclear
RT factor-1a/MODY3 gene on chromosome 12.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retinal pigment epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 25-34.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=21237683; DOI=10.1016/j.ymgme.2010.12.005;
RA He M., Pei Z., Mohsen A.W., Watkins P., Murdoch G., Van Veldhoven P.P.,
RA Ensenauer R., Vockley J.;
RT "Identification and characterization of new long chain acyl-CoA
RT dehydrogenases.";
RL Mol. Genet. Metab. 102:418-429(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-412 IN COMPLEX WITH FAD AND
RP SUBSTRATE ANALOG, AND COFACTOR.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB14.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [11]
RP VARIANTS ACADSD.
RX PubMed=1692038; DOI=10.1172/jci114607;
RA Naito E., Indo Y., Tanaka K.;
RT "Identification of two variant short chain acyl-coenzyme A dehydrogenase
RT alleles, each containing a different point mutation in a patient with short
RT chain acyl-coenzyme A dehydrogenase deficiency.";
RL J. Clin. Invest. 85:1575-1582(1990).
RN [12]
RP VARIANTS ACADSD CYS-92; ARG-177 AND CYS-383, AND VARIANTS TRP-171 AND
RP SER-209.
RX PubMed=9499414; DOI=10.1093/hmg/7.4.619;
RA Gregersen N., Winter V.S., Corydon M.J., Corydon T.J., Rinaldo P.,
RA Ribes A., Martinez G., Bennett M.J., Vianey-Saban C., Bhala A., Hale D.E.,
RA Lehnert W., Kmoch S., Roig M., Riudor E., Eiberg H., Andresen B.S.,
RA Bross P., Bolund L.A., Koelvraa S.;
RT "Identification of four new mutations in the short-chain acyl-CoA
RT dehydrogenase (SCAD) gene in two patients: one of the variant alleles,
RT 511C-->T, is present at an unexpectedly high frequency in the general
RT population, as was the case for 625G-->A, together conferring
RT susceptibility to ethylmalonic aciduria.";
RL Hum. Mol. Genet. 7:619-627(1998).
RN [13]
RP VARIANTS ACADSD SER-90; GLU-104 DEL; VAL-192; TRP-325; LEU-353 AND TRP-380,
RP VARIANTS TRP-171 AND SER-209, CHARACTERIZATION OF VARIANTS ACADSD SER-90;
RP GLU-104 DEL; VAL-192; TRP-325; LEU-353 AND TRP-380, CHARACTERIZATION OF
RP VARIANTS TRP-171 AND SER-209, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11134486; DOI=10.1203/00006450-200101000-00008;
RA Corydon M.J., Vockley J., Rinaldo P., Rhead W.J., Kjeldsen M., Winter V.S.,
RA Riggs C., Babovic-Vuksanovic D., Smeitink J., De Jong J., Levy H.,
RA Sewell A.C., Roe C., Matern D., Dasouki M., Gregersen N.;
RT "Role of common gene variations in the molecular pathogenesis of short-
RT chain acyl-CoA dehydrogenase deficiency.";
RL Pediatr. Res. 49:18-23(2001).
CC -!- FUNCTION: Short-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 (By
CC similarity). The first step of fatty acid beta-oxidation consists in
CC the removal of one hydrogen from C-2 and C-3 of the straight-chain
CC fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-
CC CoA (By similarity). Among the different mitochondrial acyl-CoA
CC dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts
CC specifically on acyl-CoAs with saturated 4 to 6 carbons long primary
CC chains (PubMed:21237683, PubMed:11134486).
CC {ECO:0000250|UniProtKB:P15651, ECO:0000269|PubMed:11134486,
CC ECO:0000269|PubMed:21237683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47196,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:87487,
CC ChEBI:CHEBI:87488; EC=1.3.8.1;
CC Evidence={ECO:0000269|PubMed:21237683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47197;
CC Evidence={ECO:0000305|PubMed:11134486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.1;
CC Evidence={ECO:0000269|PubMed:21237683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24005;
CC Evidence={ECO:0000305|PubMed:11134486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentanoyl-
CC CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:43456, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57389, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:86160;
CC Evidence={ECO:0000250|UniProtKB:Q3ZBF6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457;
CC Evidence={ECO:0000305|PubMed:11134486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000269|PubMed:21237683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC Evidence={ECO:0000305|PubMed:11134486};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|Ref.10};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|Ref.10};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:11134486}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.10}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q3ZBF6}.
CC -!- DISEASE: Acyl-CoA dehydrogenase short-chain deficiency (ACADSD)
CC [MIM:201470]: An inborn error of mitochondrial fatty acid beta-
CC oxidation resulting in acute acidosis and muscle weakness in infants,
CC and a form of lipid-storage myopathy in adults.
CC {ECO:0000269|PubMed:11134486, ECO:0000269|PubMed:1692038,
CC ECO:0000269|PubMed:9499414}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Butyryl-CoA dehydrogenase entry;
CC URL="https://en.wikipedia.org/wiki/Butyryl_CoA_dehydrogenase";
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DR EMBL; M26393; AAA60307.1; -; mRNA.
DR EMBL; Z80345; CAB02492.1; -; Genomic_DNA.
DR EMBL; Z80347; CAB02492.1; JOINED; Genomic_DNA.
DR EMBL; U83992; AAD00552.1; -; Genomic_DNA.
DR EMBL; U83991; AAD00552.1; JOINED; Genomic_DNA.
DR EMBL; BC025963; AAH25963.1; -; mRNA.
DR CCDS; CCDS9207.1; -.
DR PIR; A30605; A30605.
DR RefSeq; NP_000008.1; NM_000017.3.
DR RefSeq; NP_001289483.1; NM_001302554.1.
DR PDB; 2VIG; X-ray; 1.90 A; A/B/C/D/E/F/G/H=30-412.
DR PDBsum; 2VIG; -.
DR AlphaFoldDB; P16219; -.
DR SMR; P16219; -.
DR BioGRID; 106553; 19.
DR IntAct; P16219; 12.
DR MINT; P16219; -.
DR STRING; 9606.ENSP00000242592; -.
DR DrugBank; DB03059; Acetoacetyl-CoA.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB00157; NADH.
DR SwissLipids; SLP:000001403; -.
DR iPTMnet; P16219; -.
DR MetOSite; P16219; -.
DR PhosphoSitePlus; P16219; -.
DR BioMuta; ACADS; -.
DR DMDM; 113019; -.
DR DOSAC-COBS-2DPAGE; P16219; -.
DR SWISS-2DPAGE; P16219; -.
DR UCD-2DPAGE; P16219; -.
DR EPD; P16219; -.
DR jPOST; P16219; -.
DR MassIVE; P16219; -.
DR MaxQB; P16219; -.
DR PaxDb; P16219; -.
DR PeptideAtlas; P16219; -.
DR PRIDE; P16219; -.
DR ProteomicsDB; 53323; -.
DR Antibodypedia; 1579; 277 antibodies from 31 providers.
DR DNASU; 35; -.
DR Ensembl; ENST00000242592.9; ENSP00000242592.4; ENSG00000122971.9.
DR GeneID; 35; -.
DR KEGG; hsa:35; -.
DR MANE-Select; ENST00000242592.9; ENSP00000242592.4; NM_000017.4; NP_000008.1.
DR UCSC; uc001tza.5; human.
DR CTD; 35; -.
DR DisGeNET; 35; -.
DR GeneCards; ACADS; -.
DR GeneReviews; ACADS; -.
DR HGNC; HGNC:90; ACADS.
DR HPA; ENSG00000122971; Tissue enhanced (liver, skeletal muscle).
DR MalaCards; ACADS; -.
DR MIM; 201470; phenotype.
DR MIM; 606885; gene.
DR neXtProt; NX_P16219; -.
DR OpenTargets; ENSG00000122971; -.
DR Orphanet; 26792; Short chain acyl-CoA dehydrogenase deficiency.
DR PharmGKB; PA24426; -.
DR VEuPathDB; HostDB:ENSG00000122971; -.
DR eggNOG; KOG0139; Eukaryota.
DR GeneTree; ENSGT00940000158866; -.
DR HOGENOM; CLU_018204_0_2_1; -.
DR InParanoid; P16219; -.
DR OMA; RDVKLNQ; -.
DR OrthoDB; 589058at2759; -.
DR PhylomeDB; P16219; -.
DR TreeFam; TF105019; -.
DR BioCyc; MetaCyc:HS04619-MON; -.
DR PathwayCommons; P16219; -.
DR Reactome; R-HSA-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
DR Reactome; R-HSA-77352; Beta oxidation of butanoyl-CoA to acetyl-CoA.
DR SABIO-RK; P16219; -.
DR SignaLink; P16219; -.
DR UniPathway; UPA00660; -.
DR BioGRID-ORCS; 35; 10 hits in 1077 CRISPR screens.
DR ChiTaRS; ACADS; human.
DR EvolutionaryTrace; P16219; -.
DR GenomeRNAi; 35; -.
DR Pharos; P16219; Tbio.
DR PRO; PR:P16219; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P16219; protein.
DR Bgee; ENSG00000122971; Expressed in right lobe of liver and 156 other tissues.
DR ExpressionAtlas; P16219; baseline and differential.
DR Genevisible; P16219; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:BHF-UCL.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046359; P:butyrate catabolic process; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:ProtInc.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:BHF-UCL.
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 3D-structure; Acetylation; Direct protein sequencing; Disease variant; FAD;
KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1286669"
FT CHAIN 25..412
FT /note="Short-chain specific acyl-CoA dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000000498"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 152..161
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 161
FT /ligand="substrate"
FT BINDING 185..187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 269..272
FT /ligand="substrate"
FT BINDING 297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 365..369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 393
FT /ligand="substrate"
FT BINDING 394..396
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.10"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT MOD_RES 51
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT MOD_RES 51
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT MOD_RES 72
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT MOD_RES 129
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT MOD_RES 129
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT MOD_RES 208
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT MOD_RES 262
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT MOD_RES 262
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT MOD_RES 306
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT MOD_RES 306
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07417"
FT VARIANT 46
FT /note="R -> W (in ACADSD; dbSNP:rs121908003)"
FT /id="VAR_000310"
FT VARIANT 90
FT /note="G -> S (in ACADSD; loss of acyl-CoA dehydrogenase
FT activity; dbSNP:rs121908005)"
FT /evidence="ECO:0000269|PubMed:11134486"
FT /id="VAR_013565"
FT VARIANT 92
FT /note="G -> C (in ACADSD; dbSNP:rs121908004)"
FT /evidence="ECO:0000269|PubMed:9499414"
FT /id="VAR_000311"
FT VARIANT 104
FT /note="Missing (in ACADSD; loss of acyl-CoA dehydrogenase
FT activity; dbSNP:rs387906308)"
FT /evidence="ECO:0000269|PubMed:11134486"
FT /id="VAR_013566"
FT VARIANT 107
FT /note="R -> C (in ACADSD; dbSNP:rs61732144)"
FT /id="VAR_000312"
FT VARIANT 171
FT /note="R -> W (69% of wild-type acyl-CoA dehydrogenase
FT activity; confers susceptibility to ethylmalonicaciduria;
FT dbSNP:rs1800556)"
FT /evidence="ECO:0000269|PubMed:11134486,
FT ECO:0000269|PubMed:9499414"
FT /id="VAR_013567"
FT VARIANT 177
FT /note="W -> R (in ACADSD; dbSNP:rs57443665)"
FT /evidence="ECO:0000269|PubMed:9499414"
FT /id="VAR_000314"
FT VARIANT 192
FT /note="A -> V (in ACADSD; loss of acyl-CoA dehydrogenase
FT activity; dbSNP:rs28940874)"
FT /evidence="ECO:0000269|PubMed:11134486"
FT /id="VAR_013568"
FT VARIANT 209
FT /note="G -> S (86% of wild-type acyl-CoA dehydrogenase
FT activity; confers susceptibility to ethylmalonicaciduria;
FT dbSNP:rs1799958)"
FT /evidence="ECO:0000269|PubMed:11134486,
FT ECO:0000269|PubMed:9499414"
FT /id="VAR_000315"
FT VARIANT 325
FT /note="R -> W (in ACADSD; loss of acyl-CoA dehydrogenase
FT activity; dbSNP:rs121908006)"
FT /evidence="ECO:0000269|PubMed:11134486"
FT /id="VAR_013569"
FT VARIANT 353
FT /note="S -> L (in ACADSD; loss of acyl-CoA dehydrogenase
FT activity; dbSNP:rs28941773)"
FT /evidence="ECO:0000269|PubMed:11134486"
FT /id="VAR_013570"
FT VARIANT 380
FT /note="R -> W (in ACADSD; loss of acyl-CoA dehydrogenase
FT activity; dbSNP:rs28940875)"
FT /evidence="ECO:0000269|PubMed:11134486"
FT /id="VAR_013571"
FT VARIANT 383
FT /note="R -> C (in ACADSD; dbSNP:rs28940872)"
FT /evidence="ECO:0000269|PubMed:9499414"
FT /id="VAR_000316"
FT VARIANT 383
FT /note="R -> H (in dbSNP:rs35233375)"
FT /id="VAR_033458"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:2VIG"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:2VIG"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 176..187
FT /evidence="ECO:0007829|PDB:2VIG"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 238..249
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:2VIG"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 260..296
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 308..336
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 342..367
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 368..372
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 378..388
FT /evidence="ECO:0007829|PDB:2VIG"
FT TURN 389..392
FT /evidence="ECO:0007829|PDB:2VIG"
FT HELIX 395..411
FT /evidence="ECO:0007829|PDB:2VIG"
SQ SEQUENCE 412 AA; 44297 MW; 3E946ADFC3DA3C0E CRC64;
MAAALLARAS GPARRALCPR AWRQLHTIYQ SVELPETHQM LLQTCRDFAE KELFPIAAQV
DKEHLFPAAQ VKKMGGLGLL AMDVPEELGG AGLDYLAYAI AMEEISRGCA STGVIMSVNN
SLYLGPILKF GSKEQKQAWV TPFTSGDKIG CFALSEPGNG SDAGAASTTA RAEGDSWVLN
GTKAWITNAW EASAAVVFAS TDRALQNKGI SAFLVPMPTP GLTLGKKEDK LGIRGSSTAN
LIFEDCRIPK DSILGEPGMG FKIAMQTLDM GRIGIASQAL GIAQTALDCA VNYAENRMAF
GAPLTKLQVI QFKLADMALA LESARLLTWR AAMLKDNKKP FIKEAAMAKL AASEAATAIS
HQAIQILGGM GYVTEMPAER HYRDARITEI YEGTSEIQRL VIAGHLLRSY RS
