NB5R5_MOUSE
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 03-AUG-2022, entry version 100.
DE RecName: Full=NADH-cytochrome b5 reductase-like;
DE EC=1.6.2.2;
GN Name=Cyb5rl;
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: 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 -!- 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_001346552.1. [B1AS42-1]
DR RefSeq; NP_780680.1; NM_175471.3. [B1AS42-3]
DR AlphaFoldDB; B1AS42; -.
DR SMR; B1AS42; -.
DR STRING; 10090.ENSMUSP00000102369; -.
DR PhosphoSitePlus; B1AS42; -.
DR PaxDb; B1AS42; -.
DR PRIDE; B1AS42; -.
DR ProteomicsDB; 287610; -. [B1AS42-1]
DR ProteomicsDB; 287611; -. [B1AS42-2]
DR ProteomicsDB; 287612; -. [B1AS42-3]
DR ProteomicsDB; 287613; -. [B1AS42-4]
DR DNASU; 230582; -.
DR Ensembl; ENSMUST00000030364; ENSMUSP00000030364; ENSMUSG00000028621. [B1AS42-2]
DR Ensembl; ENSMUST00000106756; ENSMUSP00000102367; ENSMUSG00000028621. [B1AS42-3]
DR Ensembl; ENSMUST00000106758; ENSMUSP00000102369; ENSMUSG00000028621. [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 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; DIPPGHH; -.
DR OrthoDB; 1311668at2759; -.
DR PhylomeDB; B1AS42; -.
DR TreeFam; TF336549; -.
DR Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR BioGRID-ORCS; 230582; 0 hits in 57 CRISPR screens.
DR PRO; PR:B1AS42; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AS42; protein.
DR Bgee; ENSMUSG00000028621; Expressed in right kidney and 76 other tissues.
DR ExpressionAtlas; B1AS42; baseline and differential.
DR Genevisible; B1AS42; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IBA:GO_Central.
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; IPR019180; Oxidoreductase-like_N.
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 Pfam; PF09791; Oxidored-like; 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 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 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
