ID NC5R_BOVIN STANDARD; PRT; 300 AA. AC P07514; DT 01-APR-1988 (Rel. 07, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE NADH-CYTOCHROME B5 REDUCTASE (EC 1.6.2.2). GN DIA1. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A., 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 [2] RP 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 [3] RP 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 SEQUENCE OF 1-36, AND MYRISTOYLATION. 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). 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(+) + CC 2 FERROCYTOCHROME B5. CC -!- COFACTOR: FAD. CC -!- PATHWAY: MICROSOMAL ELECTRON TRANSPORT SYSTEM. CC -!- SUBCELLULAR LOCATION: THE ENZYME EXISTS IN TWO FORMS: A MEMBRANE CC BOUND FORM ON THE CYTOPLASMIC SIDE OF THE ENDOPLASMIC RETICULUM CC AND IN SOLUBLE FORM IN ERYTHROCYTES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M83104; AAA30483.1; -. DR PIR; A23896; A23896. DR PIR; A26922; A26922. DR PIR; A22182; A22182. DR HSSP; P17571; 2CND. DR INTERPRO; IPR001433; -. DR INTERPRO; IPR001834; -. DR PFAM; PF00970; Cyt_reductase; 1. DR PFAM; PF00175; oxidored_fad; 1. DR PRINTS; PR00406; CYTB5RDTASE. KW Oxidoreductase; Flavoprotein; FAD; NAD; Membrane; Myristate; KW Lipoprotein; Endoplasmic reticulum. FT CHAIN 26 300 NADH-CYTOCHROME B5 REDUCTASE, SOLUBLE FT FORM. FT LIPID 1 1 MYRISTATE. FT NP_BIND 131 161 FAD (NAD PART) (BY SIMILARITY). FT NP_BIND 170 205 FAD (NAD PART) (BY SIMILARITY). 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. 2 AND 4). FT CONFLICT 134 134 K -> G (IN REF. 2). FT CONFLICT 162 162 K -> S (IN REF. 2). FT CONFLICT 226 226 N -> D (IN REF. 2). 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 //