ID   NB5R2_RAT               Reviewed;         276 AA.
AC   Q6AY12;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=NADH-cytochrome b5 reductase 2;
DE            Short=b5R.2;
DE            EC=1.6.2.2;
GN   Name=Cyb5r2;
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=Testis;
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. Responsible
CC       for NADH-dependent lucigenin chemiluminescence in spermatozoa by
CC       reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-
CC       disulfophenyl]-2H tetrazolium monosodium salt (WST-1) (By similarity).
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   -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC       reductase family. {ECO:0000305}.
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DR   EMBL; BC079235; AAH79235.1; -; mRNA.
DR   RefSeq; NP_001014266.1; NM_001014244.1.
DR   AlphaFoldDB; Q6AY12; -.
DR   SMR; Q6AY12; -.
DR   STRING; 10116.ENSRNOP00000026744; -.
DR   PhosphoSitePlus; Q6AY12; -.
DR   jPOST; Q6AY12; -.
DR   PaxDb; Q6AY12; -.
DR   PRIDE; Q6AY12; -.
DR   GeneID; 365345; -.
DR   KEGG; rno:365345; -.
DR   UCSC; RGD:1308421; rat.
DR   CTD; 51700; -.
DR   RGD; 1308421; Cyb5r2.
DR   VEuPathDB; HostDB:ENSRNOG00000019751; -.
DR   eggNOG; KOG0534; Eukaryota.
DR   HOGENOM; CLU_003827_9_2_1; -.
DR   InParanoid; Q6AY12; -.
DR   OrthoDB; 1311668at2759; -.
DR   PhylomeDB; Q6AY12; -.
DR   Reactome; R-RNO-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR   PRO; PR:Q6AY12; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019751; Expressed in testis and 18 other tissues.
DR   ExpressionAtlas; Q6AY12; baseline and differential.
DR   Genevisible; Q6AY12; RN.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; ISO:RGD.
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   Acetylation; FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; NAD;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT   CHAIN           1..276
FT                   /note="NADH-cytochrome b5 reductase 2"
FT                   /id="PRO_0000287550"
FT   DOMAIN          15..127
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         107..137
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         146..181
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00387"
FT   MOD_RES         18
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P00387"
SQ   SEQUENCE   276 AA;  31239 MW;  2B44235766324E96 CRC64;
     MSVKKKDLIT LQDPEAKYPL PLIEKEQINH NTRRFRFGLP SPDHVLGLPV GNYVHLLAQI
     NNELVIRAYT PVSSDDDQGF VDLIIKIYFK NVHPKYPEGG KMTQYLENMK IGDTILFRGP
     TGRLFYNEPG TLLIKTDKTS EPEKKLVHHL GMIAGGTGIT PMLQLIRHIT KDTSDGTRMS
     LLFANQTEED ILLRKELEEV ATTHQNQFSL WYTLDRPPSG WEYSSGFITA DMIKEHLPPP
     GEATLILVCG PPPLIQEAAH PSLEQLGYTK DMIFTY