ID   ACADS_MOUSE             Reviewed;         412 AA.
AC   Q07417;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 84.
DE   RecName: Full=Short-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE            Short=SCAD;
DE            EC=1.3.99.2;
DE   AltName: Full=Butyryl-CoA dehydrogenase;
DE   Flags: Precursor;
GN   Name=Acads;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94102742; PubMed=8276399; DOI=10.1006/geno.1993.1438;
RA   Kelly C.L., Hinsdale M.E., Wood P.A.;
RT   "Cloning and characterization of the mouse short-chain acyl-CoA
RT   dehydrogenase cDNA.";
RL   Genomics 18:137-140(1993).
CC   -!- CATALYTIC ACTIVITY: Butanoyl-CoA + acceptor = 2-butenoyl-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; L11163; AAA16714.1; -; mRNA.
DR   IPI; IPI00116591; -.
DR   PIR; I49605; I49605.
DR   UniGene; Mm.18759; -.
DR   HSSP; P15651; 1JQI.
DR   SMR; Q07417; 28-411.
DR   REPRODUCTION-2DPAGE; Q07417; -.
DR   PRIDE; Q07417; -.
DR   Ensembl; ENSMUSG00000029545; Mus musculus.
DR   MGI; MGI:87868; Acads.
DR   HOGENOM; Q07417; -.
DR   HOVERGEN; Q07417; -.
DR   BRENDA; 1.3.99.2; 244.
DR   ArrayExpress; Q07417; -.
DR   Bgee; Q07417; -.
DR   CleanEx; MM_ACADS; -.
DR   GermOnline; ENSMUSG00000029545; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW   Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     24       Mitochondrion (By similarity).
FT   CHAIN        25    412       Short-chain specific acyl-CoA
FT                                dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000000499.
FT   NP_BIND     152    161       FAD (By similarity).
FT   NP_BIND     185    187       FAD (By similarity).
FT   NP_BIND     365    369       FAD (By similarity).
FT   NP_BIND     394    396       FAD (By similarity).
FT   ACT_SITE    392    392       Proton acceptor (By similarity).
FT   BINDING     297    297       FAD (By similarity).
SQ   SEQUENCE   412 AA;  44947 MW;  F78485BC764B79E3 CRC64;
     MAAALLARAR GPLRRALGVR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE KELVPIAAQL
     DREHLFPTAQ VKKMGELGLL AMDVPEELSG AGLGYLAYSI ALEEISRACA STGVIMSVNN
     SLYLGPILKF GSAQQKQQWI TPFTNGDKIG CFALSEPGNG SDAGAASTTA REEGDSWVLN
     GTKAWITNSW EASATVVFAS TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN
     LIFEDCRIPK ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRNAF
     GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMRKL AASEAATAIS
     HQAIQILGSM GYVTEMPAER YYRDARITEI YEGTSEIQRL VIAGHLLRSY RS
//