ID NB5R3_BOVIN Reviewed; 300 AA. AC P07514; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 16-JUN-2009, entry version 96. 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=DIA1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=Black Angus; TISSUE=Liver; RX MEDLINE=86008250; PubMed=3900065; RA Ozols J., Korza G., Heinemann F.S., Hediger M.A., Strittmatter P.; RT "Complete amino acid sequence of steer liver microsomal NADH- RT cytochrome b5 reductase."; RL J. Biol. Chem. 260:11953-11961(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS. RX MEDLINE=92129336; PubMed=1370824; RA Strittmatter P., Kittler J.M., Coghill J.E., Ozols J.; RT "Characterization of lysyl residues of NADH-cytochrome b5 reductase RT implicated in charge-pairing with active-site carboxyl residues of RT cytochrome b5 by site-directed mutagenesis of an expression vector for RT the flavoprotein."; RL J. Biol. Chem. 267:2519-2523(1992). RN [3] RP PROTEIN SEQUENCE OF 26-52. RX MEDLINE=88007457; PubMed=3654589; RA Tamura M., Yubisui T., Takeshita M., Kawabata S., Miyata T., RA Iwanaga S.; RT "Structural comparison of bovine erythrocyte, brain, and liver NADH- RT cytochrome b5 reductase by HPLC mapping."; RL J. Biochem. 101:1147-1159(1987). RN [4] RP PROTEIN SEQUENCE OF 1-36, AND MYRISTOYLATION AT GLY-1. RX MEDLINE=85030460; PubMed=6436247; RA Ozols J., Carr S.A., Strittmatter P.; RT "Identification of the NH2-terminal blocking group of NADH-cytochrome RT b5 reductase as myristic acid and the complete amino acid sequence of RT the membrane-binding domain."; RL J. Biol. Chem. 259:13349-13354(1984). RN [5] RP PROTEIN SEQUENCE OF 16-43. RX MEDLINE=84061926; PubMed=6643503; RA Kensil C.R., Hediger M.A., Ozols J., Strittmatter P.; RT "Isolation and partial characterization of the NH2-terminal membrane- RT binding domain of NADH-cytochrome b5 reductase."; RL J. Biol. Chem. 258:14656-14663(1983). CC -!- FUNCTION: Desaturation and elongation of fatty acids, cholesterol CC biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin CC reduction. CC -!- CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + CC 2 ferrocytochrome b5. CC -!- COFACTOR: FAD. CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH- CC cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity). CC -!- SUBCELLULAR LOCATION: NADH-cytochrome b5 reductase 3 membrane- CC bound form: Endoplasmic reticulum membrane; Lipid-anchor; CC Cytoplasmic side. Mitochondrion outer membrane; Lipid-anchor; CC Cytoplasmic side. Note=The enzyme exists in two forms, a membrane- CC bound form on the cytoplasmic side of the endoplasmic reticulum CC and also on the mitochondrial outer membrane and in soluble form CC in erythrocytes. CC -!- SUBCELLULAR LOCATION: NADH-cytochrome b5 reductase 3 soluble form: CC Cytoplasm. CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide CC cytochrome reductase family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M83104; AAA30483.1; -; mRNA. DR IPI; IPI00868665; -. DR PIR; A42328; RDBOB5. DR RefSeq; NP_001096720.1; -. DR UniGene; Bt.4873; -. DR HSSP; P20070; 1I7P. DR SMR; P07514; 30-300. DR Ensembl; ENSBTAG00000016516; Bos taurus. DR GeneID; 515773; -. DR KEGG; bta:515773; -. DR HOVERGEN; P07514; -. DR BRENDA; 1.6.2.2; 251. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. 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; Cytoplasm; KW Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; KW Lipid synthesis; Lipoprotein; Membrane; Mitochondrion; KW Mitochondrion outer membrane; Myristate; NAD; Oxidoreductase; KW Phosphoprotein; Steroid biosynthesis; Sterol biosynthesis. FT CHAIN 1 300 NADH-cytochrome b5 reductase 3 membrane- FT bound form. FT /FTId=PRO_0000019389. FT CHAIN 26 300 NADH-cytochrome b5 reductase 3 soluble FT form. FT /FTId=PRO_0000019391. FT DOMAIN 39 151 FAD-binding FR-type. FT NP_BIND 131 146 FAD (By similarity). FT NP_BIND 170 205 FAD (By similarity). FT MOD_RES 41 41 N6-acetyllysine (By similarity). FT MOD_RES 42 42 Phosphotyrosine (By similarity). FT MOD_RES 119 119 N6-acetyllysine (By similarity). FT MOD_RES 129 129 Phosphotyrosine (By similarity). FT LIPID 1 1 N-myristoyl glycine. FT MUTAGEN 41 41 K->E: Decrease of activity. FT MUTAGEN 125 125 K->E: Decrease of activity. FT MUTAGEN 163 163 K->E: Decrease of activity. FT CONFLICT 15 15 V -> L (in Ref. 1; AA sequence and 4; AA FT sequence). FT CONFLICT 134 134 K -> G (in Ref. 1; AA sequence). FT CONFLICT 162 162 K -> S (in Ref. 1; AA sequence). FT CONFLICT 226 226 N -> D (in Ref. 1; AA sequence). SQ SEQUENCE 300 AA; 33990 MW; 11B29F57F9309F3E CRC64; GAQLSTLGHV VLSPVWFLYS LIMKLFQRST PAITLENPDI KYPLRLIDKE VISHDTRRFR FALPSPEHIL GLPVGQHIYL SARIDGNLVI RPYTPVSSDD DKGFVDLVIK VYFKDTHPKF PAGGKMSQYL ESMKIGDTIE FRGPNGLLVY QGKGKFAIRP DKKSDPVIKT VKSVGMIAGG TGITPMLQVI RAIMKDPDDH TVCHLLFANQ TEKDILLRPE LEELRNEHSA RFKLWYTVDK APEAWDYSQG FVNEEMIRDH LPPPEEEPLV LMCGPPPMIQ YACLPNLDRV GHPKERCFAF //