ID   NB5R5_MOUSE             Reviewed;         316 AA.
AC   B1AS42; B1AS41; Q571N5; Q80W48; Q99KB7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   04-NOV-2026, entry version 119.
DE   RecName: Full=NADH-cytochrome b5 reductase-like;
DE            EC=1.6.2.2 {ECO:0000250|UniProtKB:P00387};
GN   Name=Cyb5rl {ECO:0000312|MGI:MGI:1919657};
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 4).
RC   STRAIN=ICR; TISSUE=Embryonic tail;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT   complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT   by screening of terminal sequences of cDNA clones randomly sampled from
RT   size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
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: Putative NADH-cytochrome b5 reductases family protein. May
CC       participate in fatty acid desaturation and elongation, cholesterol
CC       biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin
CC       reduction. {ECO:0000250|UniProtKB:P00387}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC         NAD(+) + H(+); 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         Evidence={ECO:0000250|UniProtKB:P00387};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46681;
CC         Evidence={ECO:0000250|UniProtKB:P00387};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P00387};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=B1AS42-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B1AS42-2; Sequence=VSP_033851;
CC       Name=3;
CC         IsoId=B1AS42-3; Sequence=VSP_033849, VSP_033850;
CC       Name=4;
CC         IsoId=B1AS42-4; Sequence=VSP_033848, VSP_033852, VSP_033853;
CC   -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC       reductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH04750.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD90340.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK220154; BAD90340.1; ALT_INIT; mRNA.
DR   EMBL; AL607132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004750; AAH04750.1; ALT_INIT; mRNA.
DR   EMBL; BC043687; AAH43687.1; -; mRNA.
DR   CCDS; CCDS38829.1; -. [B1AS42-3]
DR   CCDS; CCDS84765.1; -. [B1AS42-1]
DR   RefSeq; NP_001333481.1; NM_001346552.2. [B1AS42-1]
DR   RefSeq; NP_001364012.1; NM_001377083.1. [B1AS42-1]
DR   RefSeq; NP_001364013.1; NM_001377084.1. [B1AS42-1]
DR   RefSeq; NP_780680.1; NM_175471.4. [B1AS42-3]
DR   RefSeq; XP_036019908.1; XM_036164015.1. [B1AS42-1]
DR   RefSeq; XP_036019910.1; XM_036164017.1. [B1AS42-2]
DR   AlphaFoldDB; B1AS42; -.
DR   SMR; B1AS42; -.
DR   FunCoup; B1AS42; 629.
DR   STRING; 10090.ENSMUSP00000102369; -.
DR   PhosphoSitePlus; B1AS42; -.
DR   SwissPalm; B1AS42; -.
DR   PaxDb; 10090-ENSMUSP00000102369; -.
DR   ProteomicsDB; 287610; -. [B1AS42-1]
DR   ProteomicsDB; 287611; -. [B1AS42-2]
DR   DNASU; 230582; -.
DR   Ensembl; ENSMPUT00000006741; ENSMPUP00000006628; ENSMPUG00000006682.
DR   Ensembl; ENSMUST00000030364.13; ENSMUSP00000030364.7; ENSMUSG00000028621.18. [B1AS42-2]
DR   Ensembl; ENSMUST00000106756.9; ENSMUSP00000102367.3; ENSMUSG00000028621.18. [B1AS42-3]
DR   Ensembl; ENSMUST00000106758.8; ENSMUSP00000102369.2; ENSMUSG00000028621.18. [B1AS42-1]
DR   GeneID; 230582; -.
DR   KEGG; mmu:230582; -.
DR   UCSC; uc008tzb.1; mouse. [B1AS42-3]
DR   UCSC; uc008tzc.1; mouse. [B1AS42-2]
DR   UCSC; uc008tzd.1; mouse. [B1AS42-1]
DR   AGR; MGI:1919657; -.
DR   CTD; 606495; -.
DR   MGI; MGI:1919657; Cyb5rl.
DR   VEuPathDB; HostDB:ENSMUSG00000028621; -.
DR   eggNOG; KOG0534; Eukaryota.
DR   GeneTree; ENSGT00920000149170; -.
DR   HOGENOM; CLU_003827_9_3_1; -.
DR   InParanoid; B1AS42; -.
DR   OMA; AAHAHKQ; -.
DR   PhylomeDB; B1AS42; -.
DR   Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR   BioGRID-ORCS; 230582; 0 hits in 60 CRISPR screens.
DR   PRO; PR:B1AS42; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; B1AS42; protein.
DR   Bgee; ENSMUSG00000028621; Expressed in right kidney and 79 other cell types or tissues.
DR   ExpressionAtlas; B1AS42; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-ARBA.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0090524; F:cytochrome-b5 reductase activity, acting on NADH; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   CDD; cd06183; cyt_b5_reduct_like; 1.
DR   FunFam; 2.40.30.10:FF:000105; NADH-cytochrome b5 reductase; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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; IPR019180; Oxidoreductase-like_N.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR   PANTHER; PTHR19370:SF184; NADH-CYTOCHROME B5 REDUCTASE-LIKE; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF09791; Oxidored-like; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..316
FT                   /note="NADH-cytochrome b5 reductase-like"
FT                   /id="PRO_0000337042"
FT   DOMAIN          17..53
FT                   /note="Oxidoreductase-like"
FT   DOMAIN          76..178
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         127
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P00387"
FT   BINDING         129
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P00387"
FT   BINDING         146
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P00387"
FT   BINDING         153
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P00387"
FT   BINDING         154
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P00387"
FT   BINDING         158..173
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         183..215
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..85
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15449545"
FT                   /id="VSP_033848"
FT   VAR_SEQ         1..60
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033849"
FT   VAR_SEQ         61..67
FT                   /note="KQPPESQ -> MNNKDLE (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033850"
FT   VAR_SEQ         146..180
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033851"
FT   VAR_SEQ         250..283
FT                   /note="EVSPEQLPWSYRDKTHFGRLGQELVAELVACCRR -> ASPSPSYRGGSRLT
FT                   EVLDQGGARTGPVCLTLLSL (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15449545"
FT                   /id="VSP_033852"
FT   VAR_SEQ         284..316
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15449545"
FT                   /id="VSP_033853"
SQ   SEQUENCE   316 AA;  35884 MW;  A5D49CF710DD7AFA CRC64;
     MAETEEEEDS EAWLRLKPVE PLPSQCCGSG CSPCVFDLYY RDLERWETAR ARNDRSLLSG
     KQPPESQSCS AKLSPETFLA FHISTMEKVT KDTYLVRFTL PGNSRLGLRP GQHLILRGVV
     DGLEIQRAYT PISPVTAEGY FDVLIKCYRT GLMSQYVESW RTGDTAFWRG PFGSFLYEPK
     KYGELLMLAA GTGLAPMVPI LQSITDDEDD ETFVTLVGCF KTFEGIYLKT FFQEQARFWN
     VQTFFVLSQE VSPEQLPWSY RDKTHFGRLG QELVAELVAC CRRKPFTLVC GSPAFNEDMA
     RCLLSAGLTE DSYFLF
//