NB5R2_MOUSE
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 03-AUG-2022, entry version 113.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 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 -!- 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 -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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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 CCDS; CCDS57579.1; -. [Q3KNK3-2]
DR CCDS; CCDS85373.1; -. [Q3KNK3-1]
DR RefSeq; NP_001192156.1; NM_001205227.1. [Q3KNK3-2]
DR RefSeq; NP_796190.1; NM_177216.4. [Q3KNK3-1]
DR RefSeq; XP_017177793.1; XM_017322304.1. [Q3KNK3-1]
DR RefSeq; XP_017177794.1; XM_017322305.1. [Q3KNK3-1]
DR AlphaFoldDB; Q3KNK3; -.
DR SMR; Q3KNK3; -.
DR STRING; 10090.ENSMUSP00000050061; -.
DR iPTMnet; Q3KNK3; -.
DR PhosphoSitePlus; Q3KNK3; -.
DR MaxQB; Q3KNK3; -.
DR PeptideAtlas; Q3KNK3; -.
DR PRIDE; Q3KNK3; -.
DR ProteomicsDB; 252782; -. [Q3KNK3-1]
DR ProteomicsDB; 252783; -. [Q3KNK3-2]
DR Antibodypedia; 24030; 138 antibodies from 23 providers.
DR Ensembl; ENSMUST00000052438; ENSMUSP00000050061; ENSMUSG00000048065. [Q3KNK3-2]
DR Ensembl; ENSMUST00000208217; ENSMUSP00000146504; ENSMUSG00000048065. [Q3KNK3-1]
DR GeneID; 320635; -.
DR KEGG; mmu:320635; -.
DR UCSC; uc009jbi.2; mouse. [Q3KNK3-1]
DR UCSC; uc012frx.2; mouse. [Q3KNK3-2]
DR CTD; 51700; -.
DR MGI; MGI:2444415; Cyb5r2.
DR VEuPathDB; HostDB:ENSMUSG00000048065; -.
DR eggNOG; KOG0534; Eukaryota.
DR GeneTree; ENSGT00940000153962; -.
DR HOGENOM; CLU_003827_9_2_1; -.
DR InParanoid; Q3KNK3; -.
DR OMA; NKHDHIA; -.
DR OrthoDB; 1311668at2759; -.
DR PhylomeDB; Q3KNK3; -.
DR TreeFam; TF314333; -.
DR Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR BioGRID-ORCS; 320635; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q3KNK3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3KNK3; protein.
DR Bgee; ENSMUSG00000048065; Expressed in animal zygote and 40 other tissues.
DR Genevisible; Q3KNK3; MM.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; ISO:MGI.
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; Alternative splicing; FAD; Flavoprotein; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism.
FT CHAIN 1..276
FT /note="NADH-cytochrome b5 reductase 2"
FT /id="PRO_0000287549"
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"
FT VAR_SEQ 130
FT /note="G -> GCQTRAAEVKNIFIFLG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025560"
FT CONFLICT 132
FT /note="L -> I (in Ref. 2; AAI07239)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="S -> G (in Ref. 2; AAI07239)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="I -> T (in Ref. 2; AAI07239)"
FT /evidence="ECO:0000305"
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
