NB5R1_MOUSE
ID NB5R1_MOUSE Reviewed; 305 AA.
AC Q9DB73; Q91W81;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=NADH-cytochrome b5 reductase 1;
DE Short=b5R.1;
DE EC=1.6.2.2;
DE AltName: Full=NAD(P)H:quinone oxidoreductase type 3 polypeptide A2;
GN Name=Cyb5r1; Synonyms=Nqo3a2;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Kidney, and Salivary gland;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DB73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DB73-2; Sequence=VSP_025557, VSP_025558;
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; AK005159; BAB23850.1; -; mRNA.
DR EMBL; AK159663; BAE35270.1; -; mRNA.
DR EMBL; AK167178; BAE39313.1; -; mRNA.
DR EMBL; BC016266; AAH16266.1; -; mRNA.
DR EMBL; BC024618; AAH24618.1; -; mRNA.
DR CCDS; CCDS15308.1; -. [Q9DB73-1]
DR RefSeq; NP_082333.1; NM_028057.2. [Q9DB73-1]
DR AlphaFoldDB; Q9DB73; -.
DR SMR; Q9DB73; -.
DR BioGRID; 215095; 6.
DR STRING; 10090.ENSMUSP00000027726; -.
DR iPTMnet; Q9DB73; -.
DR PhosphoSitePlus; Q9DB73; -.
DR EPD; Q9DB73; -.
DR jPOST; Q9DB73; -.
DR MaxQB; Q9DB73; -.
DR PaxDb; Q9DB73; -.
DR PeptideAtlas; Q9DB73; -.
DR PRIDE; Q9DB73; -.
DR ProteomicsDB; 252780; -. [Q9DB73-1]
DR ProteomicsDB; 252781; -. [Q9DB73-2]
DR Antibodypedia; 2536; 271 antibodies from 28 providers.
DR DNASU; 72017; -.
DR Ensembl; ENSMUST00000027726; ENSMUSP00000027726; ENSMUSG00000026456. [Q9DB73-1]
DR Ensembl; ENSMUST00000154237; ENSMUSP00000133385; ENSMUSG00000026456. [Q9DB73-2]
DR GeneID; 72017; -.
DR KEGG; mmu:72017; -.
DR UCSC; uc007cru.1; mouse. [Q9DB73-1]
DR CTD; 51706; -.
DR MGI; MGI:1919267; Cyb5r1.
DR VEuPathDB; HostDB:ENSMUSG00000026456; -.
DR eggNOG; KOG0534; Eukaryota.
DR GeneTree; ENSGT00940000160784; -.
DR HOGENOM; CLU_1214431_0_0_1; -.
DR InParanoid; Q9DB73; -.
DR OMA; QAQHPNR; -.
DR OrthoDB; 1311668at2759; -.
DR PhylomeDB; Q9DB73; -.
DR TreeFam; TF314333; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR BioGRID-ORCS; 72017; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Cyb5r1; mouse.
DR PRO; PR:Q9DB73; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9DB73; protein.
DR Bgee; ENSMUSG00000026456; Expressed in stroma of bone marrow and 252 other tissues.
DR ExpressionAtlas; Q9DB73; baseline and differential.
DR Genevisible; Q9DB73; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; FAD; Flavoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; NAD; Oxidoreductase; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..305
FT /note="NADH-cytochrome b5 reductase 1"
FT /id="PRO_0000287546"
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"
FT VAR_SEQ 159..228
FT /note="GNFNIQPNKKSPPELRVAKKLGMIAGGTGITPMLQLIRAILKVPEDPTQCFL
FT LFANQTERDIILREDLEE -> ESACVHGCTWAKSPEATMLYGKADFTLWRLPEETYAS
FT PSFTKDFPLAKDQKRKLFSSSHGDDPSTVPCLW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025557"
FT VAR_SEQ 229..305
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025558"
SQ SEQUENCE 305 AA; 34135 MW; 847B9AAFD99ED035 CRC64;
MGIQPSPVLL ASLGVGLLTL LGLALGTYLV RRSRRPQVTL QDPDEKYLLR LLDKTTVSHN
TRRFRFALPT AHHILGLPVG KHVYLSARID GSLVIRPYTP VTSDEDQGYV DLVIKVYLKG
VHPKFPEGGK MSQYLDSLKI GDMVEFRGPS GLLSYAGKGN FNIQPNKKSP PELRVAKKLG
MIAGGTGITP MLQLIRAILK VPEDPTQCFL LFANQTERDI ILREDLEELQ AQYPNRFKLW
FTLDSPPEDW TYSKGFVTAD MIQEHLPAPA EDVLLLLCGP PPMVQLACHP NLDKLGYSQK
MRFTY
