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NADH-cytochrome b5 reductase 3 (B5R) (Cytochrome b5 reductase) (EC 1.6.2.2) (Diaphorase-1) [Cleaved into: NADH-cytochrome b5 reductase 3 membrane-bound form; NADH-cytochrome b5 reductase 3 soluble form]

 NB5R3_RAT               Reviewed;         301 AA.
P20070; Q64569; Q64720;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 177.
RecName: Full=NADH-cytochrome b5 reductase 3;
Short=B5R;
Short=Cytochrome b5 reductase;
EC=1.6.2.2;
AltName: Full=Diaphorase-1;
Contains:
RecName: Full=NADH-cytochrome b5 reductase 3 membrane-bound form;
Contains:
RecName: Full=NADH-cytochrome b5 reductase 3 soluble form;
Name=Cyb5r3; Synonyms=Dia1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=2391344;
Zenno S., Hattori M., Misumi Y., Yubisui T., Sakaki Y.;
"Molecular cloning of a cDNA encoding rat NADH-cytochrome b5 reductase
and the corresponding gene.";
J. Biochem. 107:810-816(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=3174630; DOI=10.1073/pnas.85.19.7246;
Pietrini G., Carrera P., Borgese N.;
"Two transcripts encode rat cytochrome b5 reductase.";
Proc. Natl. Acad. Sci. U.S.A. 85:7246-7250(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-37 (ISOFORMS 1; 2 AND 3), AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley, and Wistar; TISSUE=Liver, and Reticulocyte;
PubMed=1577871; DOI=10.1083/jcb.117.5.975;
Pietrini G., Aggujaro D., Carrera P., Malyszko J., Vitale A.,
Borgese N.;
"A single mRNA, transcribed from an alternative, erythroid-specific,
promoter, codes for two non-myristylated forms of NADH-cytochrome b5
reductase.";
J. Cell Biol. 117:975-986(1992).
[5]
PROTEIN SEQUENCE OF 2-25, AND MYRISTOYLATION AT GLY-2.
TISSUE=Liver;
PubMed=2498303; DOI=10.1093/oxfordjournals.jbchem.a122659;
Murakami K., Yubisui T., Takeshita M., Miyata T.;
"The NH2-terminal structures of human and rat liver microsomal NADH-
cytochrome b5 reductases.";
J. Biochem. 105:312-317(1989).
[6]
ALTERNATIVE SPLICING.
PubMed=8143727; DOI=10.1111/j.1432-1033.1994.tb18673.x;
Mota Vieira L., Kaplan J.-C., Kahn A., Leroux A.;
"Heterogeneity of the rat NADH-cytochrome-b5-reductase transcripts
resulting from multiple alternative first exons.";
Eur. J. Biochem. 220:729-737(1994).
[7]
ROLE OF MYRISTOYLATION.
PubMed=8978818; DOI=10.1083/jcb.135.6.1501;
Borgese N., Aggujaro D., Carrera P., Pietrini G., Bassetti M.;
"A role for N-myristoylation in protein targeting: NADH-cytochrome b5
reductase requires myristic acid for association with outer
mitochondrial but not ER membranes.";
J. Cell Biol. 135:1501-1513(1996).
[8]
FAD-BINDING.
PubMed=8812833; DOI=10.1006/prep.1996.0072;
Barber M.J., Quinn G.B.;
"High-level expression in Escherichia coli of the soluble, catalytic
domain of rat hepatic cytochrome b5 reductase.";
Protein Expr. Purif. 8:41-47(1996).
[9]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-301.
PubMed=11695905; DOI=10.1021/bi0106336;
Bewley M.C., Marohnic C.C., Barber M.J.;
"The structure and biochemistry of NADH-dependent cytochrome b5
reductase are now consistent.";
Biochemistry 40:13574-13582(2001).
-!- FUNCTION: Desaturation and elongation of fatty acids, cholesterol
biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin
reduction.
-!- CATALYTIC ACTIVITY:
Reaction=2 [Fe(III)-cytochrome b5] + NADH = 2 [Fe(II)-cytochrome
b5] + H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438,
Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
EC=1.6.2.2;
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:8812833};
-!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
cytochrome b5 reductase (CYB5R3) and MOSC2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane;
Lipid-anchor; Cytoplasmic side. Mitochondrion outer membrane;
Lipid-anchor; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Note=Produces the
soluble form found in erythrocytes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative initiation; Named isoforms=3;
Name=1; Synonyms=L-form reticulocyte reductase;
IsoId=P20070-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=R-form reticulocyte reductase;
IsoId=P20070-2; Sequence=VSP_009661;
Note=Produced by alternative promoter usage.;
Name=3; Synonyms=Soluble form;
IsoId=P20070-3; Sequence=VSP_009660;
Note=Produced by alternative initiation.;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are ubiquitously
expressed. Isoform 2 is expressed only in erythroid tissues,
reticulocytes and liver. {ECO:0000269|PubMed:1577871}.
-!- PTM: Only the isoform 1 is myristoyled.
-!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide
cytochrome reductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D00636; BAA00530.1; -; mRNA.
EMBL; J03867; AAA41008.1; -; mRNA.
EMBL; BC062066; AAH62066.1; -; mRNA.
EMBL; X65191; CAA46308.1; -; mRNA.
EMBL; X65191; CAA46309.1; -; mRNA.
EMBL; X65190; CAA46307.1; -; Genomic_DNA.
EMBL; X77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A40495; RDRTB5.
PIR; S23641; S23641.
RefSeq; NP_620232.1; NM_138877.1. [P20070-1]
RefSeq; XP_006242127.1; XM_006242065.3. [P20070-2]
UniGene; Rn.35994; -.
PDB; 1I7P; X-ray; 2.00 A; A=34-301.
PDB; 1IB0; X-ray; 2.30 A; A=34-301.
PDB; 1QX4; X-ray; 1.80 A; A/B=34-301.
PDBsum; 1I7P; -.
PDBsum; 1IB0; -.
PDBsum; 1QX4; -.
ProteinModelPortal; P20070; -.
SMR; P20070; -.
CORUM; P20070; -.
IntAct; P20070; 2.
STRING; 10116.ENSRNOP00000012878; -.
iPTMnet; P20070; -.
PhosphoSitePlus; P20070; -.
SwissPalm; P20070; -.
PaxDb; P20070; -.
PRIDE; P20070; -.
Ensembl; ENSRNOT00000064700; ENSRNOP00000061381; ENSRNOG00000009592. [P20070-1]
GeneID; 25035; -.
KEGG; rno:25035; -.
CTD; 1727; -.
RGD; 2502; Cyb5r3.
eggNOG; KOG0534; Eukaryota.
eggNOG; COG0543; LUCA.
GeneTree; ENSGT00940000153962; -.
HOGENOM; HOG000175005; -.
HOVERGEN; HBG052580; -.
InParanoid; P20070; -.
KO; K00326; -.
OMA; HNTAIYR; -.
OrthoDB; EOG091G0EIS; -.
PhylomeDB; P20070; -.
TreeFam; TF314333; -.
BRENDA; 1.6.2.2; 5301.
Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
Reactome; R-RNO-211945; Phase I - Functionalization of compounds.
Reactome; R-RNO-6798695; Neutrophil degranulation.
SABIO-RK; P20070; -.
EvolutionaryTrace; P20070; -.
PRO; PR:P20070; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000009592; Expressed in 10 organ(s), highest expression level in lung.
Genevisible; P20070; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC.
GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0043531; F:ADP binding; IDA:RGD.
GO; GO:0016208; F:AMP binding; IDA:RGD.
GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; TAS:RGD.
GO; GO:0071949; F:FAD binding; IBA:GO_Central.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
GO; GO:0051287; F:NAD binding; IDA:RGD.
GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 3.40.50.80; -; 1.
InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
InterPro; IPR017927; FAD-bd_FR_type.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR039261; FNR_nucleotide-bd.
InterPro; IPR001834; NADH-Cyt_B5_reductase.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00970; FAD_binding_6; 1.
Pfam; PF00175; NAD_binding_1; 1.
PRINTS; PR00406; CYTB5RDTASE.
PRINTS; PR00371; FPNCR.
SUPFAM; SSF52343; SSF52343; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation;
Alternative promoter usage; Cholesterol biosynthesis;
Cholesterol metabolism; Complete proteome; Cytoplasm;
Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein;
Lipid biosynthesis; Lipid metabolism; Lipoprotein; Membrane;
Mitochondrion; Mitochondrion outer membrane; Myristate; NAD;
Oxidoreductase; Phosphoprotein; Reference proteome;
Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
Sterol metabolism.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2498303}.
CHAIN 2 301 NADH-cytochrome b5 reductase 3 membrane-
bound form.
/FTId=PRO_0000019401.
CHAIN 27 301 NADH-cytochrome b5 reductase 3 soluble
form.
/FTId=PRO_0000019403.
DOMAIN 40 152 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 132 147 FAD.
NP_BIND 171 206 FAD.
MOD_RES 42 42 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00387}.
MOD_RES 43 43 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00387}.
MOD_RES 50 50 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9DCN2}.
MOD_RES 120 120 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9DCN2}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:2498303}.
VAR_SEQ 1 23 Missing (in isoform 3).
{ECO:0000303|PubMed:1577871}.
/FTId=VSP_009660.
VAR_SEQ 1 7 MGAQLST -> MLGPLLWTASLPV (in isoform 2).
{ECO:0000303|PubMed:1577871}.
/FTId=VSP_009661.
CONFLICT 105 105 F -> L (in Ref. 2; AAA41008).
{ECO:0000305}.
STRAND 43 52 {ECO:0000244|PDB:1QX4}.
STRAND 54 63 {ECO:0000244|PDB:1QX4}.
STRAND 78 85 {ECO:0000244|PDB:1QX4}.
STRAND 88 94 {ECO:0000244|PDB:1QX4}.
STRAND 104 111 {ECO:0000244|PDB:1QX4}.
STRAND 115 118 {ECO:0000244|PDB:1I7P}.
HELIX 126 132 {ECO:0000244|PDB:1QX4}.
STRAND 139 146 {ECO:0000244|PDB:1QX4}.
STRAND 148 153 {ECO:0000244|PDB:1QX4}.
STRAND 156 159 {ECO:0000244|PDB:1QX4}.
STRAND 168 171 {ECO:0000244|PDB:1QX4}.
STRAND 173 180 {ECO:0000244|PDB:1QX4}.
HELIX 181 183 {ECO:0000244|PDB:1QX4}.
HELIX 184 196 {ECO:0000244|PDB:1QX4}.
STRAND 203 212 {ECO:0000244|PDB:1QX4}.
HELIX 213 215 {ECO:0000244|PDB:1QX4}.
HELIX 219 228 {ECO:0000244|PDB:1QX4}.
TURN 230 232 {ECO:0000244|PDB:1QX4}.
STRAND 233 241 {ECO:0000244|PDB:1QX4}.
STRAND 247 252 {ECO:0000244|PDB:1QX4}.
HELIX 255 261 {ECO:0000244|PDB:1QX4}.
STRAND 269 275 {ECO:0000244|PDB:1QX4}.
HELIX 277 282 {ECO:0000244|PDB:1QX4}.
HELIX 285 291 {ECO:0000244|PDB:1QX4}.
HELIX 295 297 {ECO:0000244|PDB:1QX4}.
STRAND 298 300 {ECO:0000244|PDB:1QX4}.
SEQUENCE 301 AA; 34175 MW; 45431A644413905F CRC64;
MGAQLSTLSR VVLSPVWFVY SLFMKLFQRS SPAITLENPD IKYPLRLIDK EIISHDTRRF
RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD DDKGFVDLVV KVYFKDTHPK
FPAGGKMSQY LENMNIGDTI EFRGPNGLLV YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG
GTGITPMLQV IRAVLKDPND HTVCYLLFAN QSEKDILLRP ELEELRNEHS SRFKLWYTVD
KAPDAWDYSQ GFVNEEMIRD HLPPPGEETL ILMCGPPPMI QFACLPNLER VGHPKERCFT
F


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