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Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (MCAD) (EC 1.3.8.7)

 ACADM_RAT               Reviewed;         421 AA.
P08503;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
10-MAY-2017, entry version 147.
RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial;
Short=MCAD;
EC=1.3.8.7;
Flags: Precursor;
Name=Acadm;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=3611054;
Matsubara Y., Kraus J.P., Ozasa H., Glassberg R., Finocchiaro G.,
Ikeda Y., Mole J., Rosenberg L.E., Tanaka K.;
"Molecular cloning and nucleotide sequence of cDNA encoding the entire
precursor of rat liver medium chain acyl coenzyme A dehydrogenase.";
J. Biol. Chem. 262:10104-10108(1987).
[2]
PROTEIN SEQUENCE OF 11-81.
PubMed=2029527; DOI=10.1016/0167-4838(91)90542-8;
Inagaki T., Ohishi N., Tsukagoshi N., Udaka S., Ghisla S., Yagi K.;
"Structurally different rat liver medium-chain acyl CoA dehydrogenases
directed by complementary DNAs differing in their 5'-region.";
Biochim. Biophys. Acta 1077:285-290(1991).
-!- FUNCTION: Acyl-CoA dehydrogenase specific for acyl chain lengths
of 4 to 16 that catalyzes the initial step of fatty acid beta-
oxidation. Utilizes the electron transfer flavoprotein (ETF) as an
electron acceptor to transfer electrons to the main mitochondrial
respiratory chain via ETF-ubiquinone oxidoreductase (ETF
dehydrogenase). {ECO:0000250|UniProtKB:P11310}.
-!- CATALYTIC ACTIVITY: A medium-chain acyl-CoA + electron-transfer
flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced
electron-transfer flavoprotein.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
-!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-
oxidation.
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- PTM: Acetylation at Lys-307 and Lys-311 in proximity of the
cofactor-binding sites reduces catalytic activity. These sites are
deacetylated by SIRT3 (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases
of different substrate specificities are present in mammalian
tissues.
-!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
{ECO:0000305}.
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EMBL; J02791; AAA40670.1; -; mRNA.
PIR; A28436; DERTCM.
RefSeq; NP_058682.2; NM_016986.2.
UniGene; Rn.6302; -.
ProteinModelPortal; P08503; -.
SMR; P08503; -.
IntAct; P08503; 1.
STRING; 10116.ENSRNOP00000013238; -.
ChEMBL; CHEMBL2176828; -.
iPTMnet; P08503; -.
PhosphoSitePlus; P08503; -.
PaxDb; P08503; -.
PRIDE; P08503; -.
GeneID; 24158; -.
KEGG; rno:24158; -.
CTD; 34; -.
RGD; 2012; Acadm.
eggNOG; KOG0140; Eukaryota.
eggNOG; COG1960; LUCA.
HOGENOM; HOG000131659; -.
HOVERGEN; HBG000224; -.
InParanoid; P08503; -.
KO; K00249; -.
PhylomeDB; P08503; -.
SABIO-RK; P08503; -.
UniPathway; UPA00660; -.
PRO; PR:P08503; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005759; C:mitochondrial matrix; IDA:BHF-UCL.
GO; GO:0031966; C:mitochondrial membrane; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:RGD.
GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:RGD.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL.
GO; GO:0016853; F:isomerase activity; IDA:RGD.
GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:InterPro.
GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:RGD.
GO; GO:0051793; P:medium-chain fatty acid catabolic process; IDA:RGD.
GO; GO:0051289; P:protein homotetramerization; IDA:RGD.
GO; GO:0046688; P:response to copper ion; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
CDD; cd01157; MCAD; 1.
Gene3D; 1.10.540.10; -; 1.
InterPro; IPR006089; Acyl-CoA_DH_CS.
InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
InterPro; IPR009075; AcylCo_DH/oxidase_C.
InterPro; IPR013786; AcylCoA_DH/ox_N.
InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
InterPro; IPR034180; MCAD.
Pfam; PF00441; Acyl-CoA_dh_1; 1.
Pfam; PF02770; Acyl-CoA_dh_M; 1.
Pfam; PF02771; Acyl-CoA_dh_N; 1.
SUPFAM; SSF47203; SSF47203; 1.
SUPFAM; SSF56645; SSF56645; 1.
PROSITE; PS00072; ACYL_COA_DH_1; 1.
PROSITE; PS00073; ACYL_COA_DH_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing; FAD;
Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion;
Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
TRANSIT 1 25 Mitochondrion.
CHAIN 26 421 Medium-chain specific acyl-CoA
dehydrogenase, mitochondrial.
/FTId=PRO_0000000506.
NP_BIND 158 167 FAD. {ECO:0000250}.
NP_BIND 191 193 FAD. {ECO:0000250}.
NP_BIND 306 308 FAD. {ECO:0000250}.
NP_BIND 316 317 FAD. {ECO:0000250}.
NP_BIND 374 378 FAD. {ECO:0000250}.
NP_BIND 403 405 FAD. {ECO:0000250}.
REGION 278 281 Substrate binding. {ECO:0000250}.
ACT_SITE 401 401 Proton acceptor. {ECO:0000250}.
BINDING 167 167 Substrate; via carbonyl oxygen.
{ECO:0000250}.
BINDING 402 402 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 413 413 Substrate. {ECO:0000250}.
MOD_RES 69 69 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 69 69 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 79 79 N6-acetyllysine.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 179 179 N6-succinyllysine.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 212 212 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 212 212 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 217 217 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 217 217 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 259 259 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 259 259 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 271 271 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 271 271 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 301 301 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11310}.
MOD_RES 351 351 Phosphothreonine.
{ECO:0000250|UniProtKB:P45952}.
SEQUENCE 421 AA; 46555 MW; 2CF076F8C919BDE8 CRC64;
MAAALRRGYK VLRSVSHFEC RAQHTKPSLK QEPGLGFSFE LTEQQKEFQT IARKFAREEI
IPVAPDYDKS GEYPFPLIKR AWELGLINTH IPESCGGLGL GTFDACLITE ELAYGCTGVQ
TAIEANSLGQ MPVIIAGNDQ QKKKYLGRMT EQPMMCAYCV TEPSAGSDVA GIKTKAEKKG
DEYVINGQKM WITNGGKANW YFVLTRSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM
GQRCSDTRGI TFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYFASIAKAF
AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIEKYK
N


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