NB5R1_RAT
ID NB5R1_RAT Reviewed; 305 AA.
AC Q5EB81;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=NADH-cytochrome b5 reductase 1;
DE Short=b5R.1;
DE EC=1.6.2.2;
GN Name=Cyb5r1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation
CC and elongation of fatty acids, cholesterol biosynthesis, drug
CC metabolism, and, in erythrocyte, methemoglobin reduction.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; BC089945; AAH89945.1; -; mRNA.
DR RefSeq; NP_001013144.1; NM_001013126.1.
DR AlphaFoldDB; Q5EB81; -.
DR SMR; Q5EB81; -.
DR STRING; 10116.ENSRNOP00000057400; -.
DR iPTMnet; Q5EB81; -.
DR PhosphoSitePlus; Q5EB81; -.
DR jPOST; Q5EB81; -.
DR PaxDb; Q5EB81; -.
DR PRIDE; Q5EB81; -.
DR GeneID; 304805; -.
DR KEGG; rno:304805; -.
DR UCSC; RGD:1306084; rat.
DR CTD; 51706; -.
DR RGD; 1306084; Cyb5r1.
DR eggNOG; KOG0534; Eukaryota.
DR InParanoid; Q5EB81; -.
DR OrthoDB; 1311668at2759; -.
DR PhylomeDB; Q5EB81; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR PRO; PR:Q5EB81; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Membrane; NAD;
KW Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..305
FT /note="NADH-cytochrome b5 reductase 1"
FT /id="PRO_0000287547"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 44..156
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 136..166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 175..210
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 305 AA; 34223 MW; 759E91678EEB3D30 CRC64;
MGIQPSPVLL ASLGVGLFTL FGLALGTYLV RRSRRPQVTL QDPDEKYLLR LLDKTTVSHN
TRRFRFALPT AHHILGLPVG KHVYLSARID GSQVIRPYTP VTSDEDQGYV DLVIKVYLKG
VHPKFSEGGK MSQYLDSLKI GDVVEFRGPS GLLSYAGKGN FNIQPNKKSP PELRVAKKLG
MIAGGTGITP MLQLIRAILK VPEDPTQCFL LFANQTEKDI ILREDLEELQ AQYPIRFKLW
FTLDYPPEDW TYSKGFVTAD MIQEHLPAPA EDVLLLLCGP PPMVQLACHP NLDKLGYSQK
MRFTY