ID   ACADM_RAT               Reviewed;         421 AA.
AC   P08503;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   16-JUN-2009, entry version 86.
DE   RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE            Short=MCAD;
DE            EC=1.3.99.3;
DE   Flags: Precursor;
GN   Name=Acadm;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   MEDLINE=87280028; PubMed=3611054;
RA   Matsubara Y., Kraus J.P., Ozasa H., Glassberg R., Finocchiaro G.,
RA   Ikeda Y., Mole J., Rosenberg L.E., Tanaka K.;
RT   "Molecular cloning and nucleotide sequence of cDNA encoding the entire
RT   precursor of rat liver medium chain acyl coenzyme A dehydrogenase.";
RL   J. Biol. Chem. 262:10104-10108(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 11-81.
RX   MEDLINE=91230137; PubMed=2029527; DOI=10.1016/0167-4838(91)90542-8;
RA   Inagaki T., Ohishi N., Tsukagoshi N., Udaka S., Ghisla S., Yagi K.;
RT   "Structurally different rat liver medium-chain acyl CoA dehydrogenases
RT   directed by complementary DNAs differing in their 5'-region.";
RL   Biochim. Biophys. Acta 1077:285-290(1991).
CC   -!- FUNCTION: This enzyme is specific for acyl chain lengths of 4 to
CC       16.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA +
CC       reduced acceptor.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-
CC       oxidation.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases
CC       of different substrate specificities are present in mammalian
CC       tissues.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
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DR   EMBL; J02791; AAA40670.1; -; mRNA.
DR   IPI; IPI00212015; -.
DR   PIR; A28436; DERTCM.
DR   RefSeq; NP_058682.1; -.
DR   UniGene; Rn.6302; -.
DR   HSSP; P11310; 1EGD.
DR   SMR; P08503; 35-421.
DR   PRIDE; P08503; -.
DR   Ensembl; ENSRNOG00000009845; Rattus norvegicus.
DR   GeneID; 24158; -.
DR   KEGG; rno:24158; -.
DR   RGD; 2012; Acadm.
DR   HOVERGEN; P08503; -.
DR   BRENDA; 1.3.99.3; 248.
DR   NextBio; 602449; -.
DR   ArrayExpress; P08503; -.
DR   GermOnline; ENSRNOG00000009845; Rattus norvegicus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IDA:RGD.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid stimulus; IEP:RGD.
DR   GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006092; Acyl-CoA_DH_N.
DR   InterPro; IPR006090; Acyl-CoA_Oxase/DH_1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_M.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR013764; AcylCoA_oxidase/DH_1/2_C.
DR   Gene3D; G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
DR   Gene3D; G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
DR   Gene3D; G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1.
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   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Fatty acid metabolism; Flavoprotein;
KW   Lipid metabolism; Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     25       Mitochondrion.
FT   CHAIN        26    421       Medium-chain specific acyl-CoA
FT                                dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000000506.
FT   NP_BIND     158    167       FAD (By similarity).
FT   NP_BIND     191    193       FAD (By similarity).
FT   NP_BIND     306    308       FAD (By similarity).
FT   NP_BIND     316    317       FAD (By similarity).
FT   NP_BIND     374    378       FAD (By similarity).
FT   NP_BIND     403    405       FAD (By similarity).
FT   REGION      278    281       Substrate binding (By similarity).
FT   ACT_SITE    401    401       Proton acceptor (By similarity).
FT   BINDING     167    167       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     402    402       Substrate; via amide nitrogen (By
FT                                similarity).
SQ   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
//