ID   NB5R2_MOUSE             Reviewed;         276 AA.
AC   Q3KNK3; Q3UGG1; Q8BUG7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=NADH-cytochrome b5 reductase 2;
DE            Short=b5R.2;
DE            EC=1.6.2.2;
GN   Name=Cyb5r2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: NADH-cytochrome b5 reductases are involved in
CC       desaturation and elongation of fatty acids, cholesterol
CC       biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin
CC       reduction. Responsible for NADH-dependent lucigenin
CC       chemiluminescence in spermatozoa by reducing both lucigenin and 2-
CC       [4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H
CC       tetrazolium monosodium salt (WST-1) (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) +
CC       2 ferrocytochrome b5.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3KNK3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3KNK3-2; Sequence=VSP_025560;
CC         Note=No experimental confirmation available;
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; AK085272; BAC39408.1; -; mRNA.
DR   EMBL; AK147952; BAE28247.1; -; mRNA.
DR   EMBL; BC107238; AAI07239.1; -; mRNA.
DR   EMBL; BC107239; AAI07240.1; -; mRNA.
DR   IPI; IPI00310925; -.
DR   IPI; IPI00845753; -.
DR   RefSeq; NP_796190.1; -.
DR   UniGene; Mm.132828; -.
DR   Ensembl; ENSMUSG00000048065; Mus musculus.
DR   GeneID; 320635; -.
DR   KEGG; mmu:320635; -.
DR   MGI; MGI:2444415; Cyb5r2.
DR   HOVERGEN; Q3KNK3; -.
DR   OMA; Q3KNK3; PEAKYPL.
DR   BRENDA; 1.6.2.2; 244.
DR   NextBio; 397113; -.
DR   Bgee; Q3KNK3; -.
DR   CleanEx; MM_CYB5R2; -.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0016126; P:sterol biosynthetic process; 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   2: Evidence at transcript level;
KW   Alternative splicing; FAD; Flavoprotein; Lipid synthesis; NAD;
KW   Oxidoreductase; Phosphoprotein; Steroid biosynthesis;
KW   Sterol biosynthesis.
FT   CHAIN         1    276       NADH-cytochrome b5 reductase 2.
FT                                /FTId=PRO_0000287549.
FT   DOMAIN       15    127       FAD-binding FR-type.
FT   NP_BIND     107    137       FAD (By similarity).
FT   NP_BIND     146    181       FAD (By similarity).
FT   MOD_RES     177    177       Phosphothreonine (By similarity).
FT   VAR_SEQ     130    130       G -> GCQTRAAEVKNIFIFLG (in isoform 2).
FT                                /FTId=VSP_025560.
FT   CONFLICT    132    132       L -> I (in Ref. 2; AAI07239).
FT   CONFLICT    267    267       S -> G (in Ref. 2; AAI07239).
FT   CONFLICT    275    275       I -> T (in Ref. 2; AAI07239).
SQ   SEQUENCE   276 AA;  31360 MW;  56596AF2F33F33E3 CRC64;
     MSVKKKDLIT LQDPEAKYPL PLIEKEQISH NTRRFRFGLP SPDHVLGLPV GNYVHLLAQI
     NNELVIRAYT PVSSDDDQGF VDLIIKIYFK NVHPKYPEGG KMTQYLENMK IGDTILFRGP
     TGRLFYNEPG TLLIKANKTS EPEKKLVHHL GMIAGGTGIT PMLQLIRHIT KDTSDETRMS
     LLFANQTEED ILLRKELEEV ATTHHKQFNL WYTLDRPPSD WKYSSGFVSA DMIKEHLPPP
     GEDTLILVCG PPPLIQAAAH PSLEQLSYTK DMIFIY
//