NB5R3_CANLF
ID NB5R3_CANLF Reviewed; 301 AA.
AC Q0X0E5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=NADH-cytochrome b5 reductase 3 {ECO:0000305};
DE Short=B5R;
DE Short=Cytochrome b5 reductase;
DE EC=1.6.2.2 {ECO:0000250|UniProtKB:P00387};
DE AltName: Full=Diaphorase-1;
DE Contains:
DE RecName: Full=NADH-cytochrome b5 reductase 3 membrane-bound form;
DE Contains:
DE RecName: Full=NADH-cytochrome b5 reductase 3 soluble form;
GN Name=CYB5R3; Synonyms=C5BR, DIA1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ano H., Ebisu S., Kondoh S., Hagio M., Makimura S.;
RT "Cloning of canine NADH cytochrome b5 reductase mRNA.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Trachea;
RX PubMed=16814740; DOI=10.1016/j.abb.2006.04.021;
RA Roma G.W., Crowley L.J., Barber M.J.;
RT "Expression and characterization of a functional canine variant of
RT cytochrome b5 reductase.";
RL Arch. Biochem. Biophys. 452:69-82(2006).
CC -!- FUNCTION: Transfers two electrons from NADH to two molecules of
CC cytochrome b5 through an enzyme-bound FAD. Electrons from the reduced
CC cytochrome b5 are then transferred to various electron acceptors,
CC thereby participating in methemoglobin reduction in red blood cells and
CC in the desaturation and elongation of fatty acids, cholesterol
CC biosynthesis and cytochrome P-450-mediated drug metabolism other
CC tissues. {ECO:0000250|UniProtKB:P00387}.
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 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 -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC cytochrome b5 reductase (CYB5R3) and MTARC2 (By similarity). Interacts
CC with MTLN; the interaction is required to maintain cellular lipid
CC composition and leads to stimulation of mitochondrial respiratory
CC complex I activity (By similarity). {ECO:0000250|UniProtKB:P83686,
CC ECO:0000250|UniProtKB:Q9DCN2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P00387}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P00387}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P00387}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P00387}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P00387}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P00387}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; AB185964; BAF02366.1; -; mRNA.
DR EMBL; DQ141222; ABA12483.1; -; mRNA.
DR RefSeq; NP_001041549.1; NM_001048084.1.
DR AlphaFoldDB; Q0X0E5; -.
DR SMR; Q0X0E5; -.
DR STRING; 9615.ENSCAFP00000039720; -.
DR PaxDb; Q0X0E5; -.
DR PRIDE; Q0X0E5; -.
DR Ensembl; ENSCAFT00000099594; ENSCAFP00000074037; ENSCAFG00000000953.
DR Ensembl; ENSCAFT00030007099; ENSCAFP00030006224; ENSCAFG00030003804.
DR Ensembl; ENSCAFT00845026065; ENSCAFP00845020554; ENSCAFG00845014552.
DR GeneID; 474479; -.
DR KEGG; cfa:474479; -.
DR CTD; 1727; -.
DR VEuPathDB; HostDB:ENSCAFG00845014552; -.
DR VGNC; VGNC:50283; CYB5R3.
DR eggNOG; KOG0534; Eukaryota.
DR GeneTree; ENSGT00940000153962; -.
DR InParanoid; Q0X0E5; -.
DR OrthoDB; 1311668at2759; -.
DR Reactome; R-CFA-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-CFA-6798695; Neutrophil degranulation.
DR Proteomes; UP000002254; Chromosome 10.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1903958; C:nitric-oxide synthase complex; IEA:Ensembl.
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:0050421; F:nitrite reductase (NO-forming) activity; IEA:Ensembl.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:Ensembl.
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 Acetylation; Cholesterol biosynthesis; Cholesterol metabolism;
KW Endoplasmic reticulum; FAD; Flavoprotein; Lipid biosynthesis;
KW Lipid metabolism; Lipoprotein; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Myristate; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07514"
FT CHAIN 2..301
FT /note="NADH-cytochrome b5 reductase 3 membrane-bound form"
FT /id="PRO_0000289590"
FT CHAIN 27..301
FT /note="NADH-cytochrome b5 reductase 3 soluble form"
FT /id="PRO_0000289591"
FT DOMAIN 40..152
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 132..147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 171..206
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00387"
FT MOD_RES 43
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00387"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN2"
FT MOD_RES 120
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN2"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P00387"
SQ SEQUENCE 301 AA; 34139 MW; 76FB38B457AFF841 CRC64;
MGAQLSTLGH VVLSPVWFLY NLLMKLFQRS TPAITLESPD IKYPLRLIDK EVINHDTRRF
RFALPSPQHI LGLPVGQHIY LSARIDGNLV IRPYTPVSSD DDKGFVDLVI KVYFKDTHPK
FPAGGKMSQY LESMKIGDTI EFRGPNGLLV YQGKGKFAIR PDKKSNPIIK TVKSVGMIAG
GTGITPMLQV IRAIIKDPHD PTVCHLLFAN QTEKDILLRP ELEELRNEHS ARFKLWYTVD
KAPEAWDYSQ GFVNEEMIRD HLPPPEEEPL ILMCGPPPMI QYACLPNLDR VGHPKERCFA
F
