ID   NB5R3_CANFA             Reviewed;         301 AA.
AC   Q0X0E5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=NADH-cytochrome b5 reductase 3;
DE            Short=Cytochrome b5 reductase;
DE            Short=B5R;
DE            EC=1.6.2.2;
DE   AltName: Full=Diaphorase-1;
DE   Contains:
DE     RecName: Full=NADH-cytochrome b5 reductase 3 membrane-bound form;
DE   Contains:
DE     RecName: Full=NADH-cytochrome b5 reductase 3 soluble form;
GN   Name=CYB5R3; Synonyms=C5BR, DIA1;
OS   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ano H., Ebisu S., Kondoh S., Hagio M., Makimura S.;
RT   "Cloning of canine NADH cytochrome b5 reductase mRNA.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=Trachea;
RX   PubMed=16814740; DOI=10.1016/j.abb.2006.04.021;
RA   Roma G.W., Crowley L.J., Barber M.J.;
RT   "Expression and characterization of a functional canine variant of
RT   cytochrome b5 reductase.";
RL   Arch. Biochem. Biophys. 452:69-82(2006).
CC   -!- FUNCTION: Desaturation and elongation of fatty acids, cholesterol
CC       biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin
CC       reduction (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) +
CC       2 ferrocytochrome b5.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC       cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Lipid-
CC       anchor; Cytoplasmic side (By similarity). Mitochondrion outer
CC       membrane; Lipid-anchor; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide
CC       cytochrome reductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
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DR   EMBL; AB185964; BAF02366.1; -; mRNA.
DR   EMBL; DQ141222; ABA12483.1; -; mRNA.
DR   RefSeq; NP_001041549.1; -.
DR   UniGene; Cfa.15074; -.
DR   SMR; Q0X0E5; 31-301.
DR   Ensembl; ENSCAFG00000000953; Canis familiaris.
DR   GeneID; 474479; -.
DR   KEGG; cfa:474479; -.
DR   HOVERGEN; Q0X0E5; -.
DR   BRENDA; 1.6.2.2; 463.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR001834; NADH-Cyt_B5_reductase.
DR   InterPro; IPR008333; OxRdtase_FAD-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cholesterol biosynthesis; Endoplasmic reticulum; FAD;
KW   Flavoprotein; Lipid synthesis; Lipoprotein; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Myristate; NAD; Oxidoreductase;
KW   Phosphoprotein; Steroid biosynthesis; Sterol biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    301       NADH-cytochrome b5 reductase 3 membrane-
FT                                bound form.
FT                                /FTId=PRO_0000289590.
FT   CHAIN        27    301       NADH-cytochrome b5 reductase 3 soluble
FT                                form.
FT                                /FTId=PRO_0000289591.
FT   DOMAIN       40    152       FAD-binding FR-type.
FT   NP_BIND     132    147       FAD (By similarity).
FT   NP_BIND     171    206       FAD (By similarity).
FT   MOD_RES      42     42       N6-acetyllysine (By similarity).
FT   MOD_RES      43     43       Phosphotyrosine (By similarity).
FT   MOD_RES     120    120       N6-acetyllysine (By similarity).
FT   MOD_RES     130    130       Phosphotyrosine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   301 AA;  34139 MW;  76FB38B457AFF841 CRC64;
     MGAQLSTLGH VVLSPVWFLY NLLMKLFQRS TPAITLESPD IKYPLRLIDK EVINHDTRRF
     RFALPSPQHI LGLPVGQHIY LSARIDGNLV IRPYTPVSSD DDKGFVDLVI KVYFKDTHPK
     FPAGGKMSQY LESMKIGDTI EFRGPNGLLV YQGKGKFAIR PDKKSNPIIK TVKSVGMIAG
     GTGITPMLQV IRAIIKDPHD PTVCHLLFAN QTEKDILLRP ELEELRNEHS ARFKLWYTVD
     KAPEAWDYSQ GFVNEEMIRD HLPPPEEEPL ILMCGPPPMI QYACLPNLDR VGHPKERCFA
     F
//