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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_HUMAN             Reviewed;         301 AA.
P00387; B1AHF2; B7Z7L3; O75675; Q8TDL8; Q8WTS8; Q9UEN4; Q9UEN5;
Q9UL55; Q9UL56;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 237.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-66.
TISSUE=Placenta;
PubMed=2479590; DOI=10.1016/0378-1119(89)90299-0;
Tomatsu S., Kobayashi Y., Fukumaki Y., Yubisui T., Orii T., Sakaki Y.;
"The organization and the complete nucleotide sequence of the human
NADH-cytochrome b5 reductase gene.";
Gene 80:353-361(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Voice M.W.;
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Yoon B., Chung H., Ko E., Lee D.;
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-66, AND VARIANTS
HM GLN-58; PRO-73 AND TYR-204.
TISSUE=Leukocyte;
Lan F.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-117.
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-301 (ISOFORM 1), AND VARIANT PRO-66.
TISSUE=Liver;
PubMed=3035541; DOI=10.1073/pnas.84.11.3609;
Yubisui T., Naitoh Y., Zenno S., Tamura M., Takeshita M., Sakaki Y.;
"Molecular cloning of cDNAs of human liver and placenta NADH-
cytochrome b5 reductase.";
Proc. Natl. Acad. Sci. U.S.A. 84:3609-3613(1987).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 101-250 (ISOFORM 1).
Diss J.K.J., Fraser S.P., Coombes R.C., Djamgoz M.B.A.;
"Upregulation of voltage-gated Na+ channel expression and metastatic
potential in human breast cancer: correlative studies on cell lines
and biopsy tissues.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[13]
PROTEIN SEQUENCE OF 2-25, AND MYRISTOYLATION AT GLY-2.
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).
[14]
PROTEIN SEQUENCE OF 27-301.
TISSUE=Erythrocyte;
PubMed=3700359;
Yubisui T., Miyata T., Iwanaga S., Tamura M., Takeshita M.;
"Complete amino acid sequence of NADH-cytochrome b5 reductase purified
from human erythrocytes.";
J. Biochem. 99:407-422(1986).
[15]
PROTEIN SEQUENCE OF 27-301.
TISSUE=Erythrocyte;
PubMed=6389526;
Yubisui T., Miyata T., Iwanaga S., Tamura M., Yoshida S.,
Takeshita M., Nakajima H.;
"Amino acid sequence of NADH-cytochrome b5 reductase of human
erythrocytes.";
J. Biochem. 96:579-582(1984).
[16]
ALTERNATIVE PROMOTER USAGE.
PubMed=9639531;
Bulbarelli A., Valentini A., De Silvestris M., Cappellini M.D.,
Borgese N.;
"An erythroid-specific transcript generates the soluble form of NADH-
cytochrome b5 reductase in humans.";
Blood 92:310-319(1998).
[17]
MUTAGENESIS OF CYSTEINE RESIDUES.
PubMed=2019583;
Shirabe K., Yubisui T., Nishino T., Takeshita M.;
"Role of cysteine residues in human NADH-cytochrome b5 reductase
studied by site-directed mutagenesis. Cys-273 and Cys-283 are located
close to the NADH-binding site but are not catalytically essential.";
J. Biol. Chem. 266:7531-7536(1991).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 31-301.
PubMed=15502298; DOI=10.1107/S0907444904020645;
Bando S., Takano T., Yubisui T., Shirabe K., Takeshita M.,
Nakagawa A.;
"Structure of human erythrocyte NADH-cytochrome b5 reductase.";
Acta Crystallogr. D 60:1929-1934(2004).
[25]
VARIANT METHB-CYB5R3 PRO-128.
PubMed=1898726;
Yubisui T., Shirabe K., Takeshita M., Kobayashi Y., Fukumaki Y.,
Sakaki Y., Takano T.;
"Structural role of serine 127 in the NADH-binding site of human NADH-
cytochrome b5 reductase.";
J. Biol. Chem. 266:66-70(1991).
[26]
VARIANTS METHB-CYB5R3 GLN-58 AND PRO-149.
PubMed=1707593;
Katsube T., Sakamoto N., Kobayashi Y., Seki R., Hirano M.,
Tanishima K., Tomoda A., Takazakura E., Yubisui T., Takeshita M.,
Sakaki Y., Fukumaki Y.;
"Exonic point mutations in NADH-cytochrome B5 reductase genes of
homozygotes for hereditary methemoglobinemia, types I and III:
putative mechanisms of tissue-dependent enzyme deficiency.";
Am. J. Hum. Genet. 48:799-808(1991).
[27]
VARIANT METHB-CYB5R3 MET-106.
PubMed=1400360;
Shirabe K., Yubisui T., Borgese N., Tang C.-Y., Hultquist D.E.,
Takeshita M.;
"Enzymatic instability of NADH-cytochrome b5 reductase as a cause of
hereditary methemoglobinemia type I (red cell type).";
J. Biol. Chem. 267:20416-20421(1992).
[28]
VARIANT METHB-CYB5R3 PHE-299 DEL.
PubMed=8119939;
Shirabe K., Fujimoto Y., Yubisui T., Takeshita M.;
"An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase
gene results in hereditary methemoglobinemia type II (generalized
type). A functional implication for the role of the COOH-terminal
region of the enzyme.";
J. Biol. Chem. 269:5952-5957(1994).
[29]
VARIANTS METHB-CYB5R3 ARG-204 AND MET-273 DEL.
PubMed=7718898;
Vieira L.M., Kaplan J.-C., Kahn A., Leroux A.;
"Four new mutations in the NADH-cytochrome b5 reductase gene from
patients with recessive congenital methemoglobinemia type II.";
Blood 85:2254-2262(1995).
[30]
VARIANT SER-117.
PubMed=9048929; DOI=10.1007/s004390050347;
Jenkins M.M., Prchal J.T.;
"A high-frequency polymorphism of NADH-cytochrome b5 reductase in
African-Americans.";
Hum. Genet. 99:248-250(1997).
[31]
VARIANT METHB-CYB5R3 PRO-73.
PubMed=9695975; DOI=10.1046/j.1365-2141.1998.00782.x;
Wu Y.-S., Huang C.-H., Wan Y., Huang Q.-J., Zhu Z.-Y.;
"Identification of a novel point mutation (Leu72-to-Pro) in the NADH-
cytochrome b5 reductase gene of a patient with hereditary
methaemoglobinaemia type I.";
Br. J. Haematol. 102:575-577(1998).
[32]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-83 AND 171-187, AND VARIANT
METHB-CYB5R3 VAL-179.
PubMed=9886302; DOI=10.1046/j.1365-2141.1998.01123.x;
Higasa K., Manabe J.I., Yubisui T., Sumimoto H., Pung-Amritt P.,
Tanphaichitr V.S., Fukumaki Y.;
"Molecular basis of hereditary methaemoglobinaemia, types I and II:
two novel mutations in the NADH-cytochrome b5 reductase gene.";
Br. J. Haematol. 103:922-930(1998).
[33]
VARIANT METHB-CYB5R3 TYR-204.
PubMed=10807796;
Wang Y., Wu Y.-S., Zheng P.-Z., Yang W.-X., Fang G.-A., Tang Y.-C.,
Xie F., Lan F.-H., Zhu Z.-Y.;
"A novel mutation in the NADH-cytochrome b5 reductase gene of a
Chinese patient with recessive congenital methemoglobinemia.";
Blood 95:3250-3255(2000).
[34]
VARIANT METHB-CYB5R3 GLN-58.
PubMed=15622768;
Huang C.-H., Xie Y., Wang Y., Wu Y.-S.;
"Arginine-glutamine replacement at residue 57 of NADH-cytochrome b5
reductase in Chinese hereditary methemoglobinemia.";
Zhonghua Xue Ye Xue Za Zhi 18:200-203(1997).
[35]
VARIANTS METHB-CYB5R3 GLU-256 DEL AND ASP-292.
PubMed=12393396; DOI=10.1182/blood-2002-05-1405;
Percy M.J., Gillespie M.J.S., Savage G., Hughes A.E., McMullin M.F.,
Lappin T.R.J.;
"Familial idiopathic methemoglobinemia revisited: original cases
reveal 2 novel mutations in NADH-cytochrome b5 reductase.";
Blood 100:3447-3449(2002).
[36]
CHARACTERIZATION OF VARIANTS METHB-CYB5R3 GLU-256 DEL AND ASP-292.
PubMed=15953014; DOI=10.1111/j.1365-2141.2005.05526.x;
Percy M.J., Crowley L.J., Davis C.A., McMullin M.F., Savage G.,
Hughes J., McMahon C., Quinn R.J.M., Smith O., Barber M.J.,
Lappin T.R.J.;
"Recessive congenital methaemoglobinaemia: functional characterization
of the novel D239G mutation in the NADH-binding lobe of cytochrome b5
reductase.";
Br. J. Haematol. 129:847-853(2005).
-!- 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;
-!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
cytochrome b5 reductase (CYB5R3) and MOSC2. {ECO:0000250}.
-!- INTERACTION:
P69905:HBA2; NbExp=2; IntAct=EBI-1046040, EBI-714680;
-!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane;
Lipid-anchor; Cytoplasmic side. Mitochondrion outer membrane;
Lipid-anchor; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Produces the
soluble form found in erythrocytes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
Name=1; Synonyms=M;
IsoId=P00387-1; Sequence=Displayed;
Name=2; Synonyms=S;
IsoId=P00387-2; Sequence=VSP_010200;
Name=3;
IsoId=P00387-3; Sequence=VSP_042827;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed at late stages of
erythroid maturation.
-!- POLYMORPHISM: Ser-117 seems to only be found in persons of African
origin. The allele frequency is 0.23 in African Americans. It was
not found in Caucasians, Asians, Indo-Aryans, or Arabs. There
seems to be no effect on the enzyme activity.
{ECO:0000269|PubMed:9048929}.
-!- DISEASE: Methemoglobinemia CYB5R3-related (METHB-CYB5R3)
[MIM:250800]: A form of methemoglobinemia, a hematologic disease
characterized by the presence of excessive amounts of
methemoglobin in blood cells, resulting in decreased oxygen
carrying capacity of the blood, cyanosis and hypoxia. There are
two types of methemoglobinemia CYB5R3-related. In type 1, the
defect affects the soluble form of the enzyme, is restricted to
red blood cells, and causes well-tolerated methemoglobinemia. In
type 2, the defect affects both the soluble and microsomal forms
of the enzyme and is thus generalized, affecting red cells,
leukocytes and all body tissues. Type 2 methemoglobinemia is
associated with mental deficiency and other neurologic symptoms.
{ECO:0000269|PubMed:10807796, ECO:0000269|PubMed:12393396,
ECO:0000269|PubMed:1400360, ECO:0000269|PubMed:15622768,
ECO:0000269|PubMed:15953014, ECO:0000269|PubMed:1707593,
ECO:0000269|PubMed:1898726, ECO:0000269|PubMed:7718898,
ECO:0000269|PubMed:8119939, ECO:0000269|PubMed:9695975,
ECO:0000269|PubMed:9886302}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide
cytochrome reductase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/dia1/";
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EMBL; M28713; AAA59900.1; -; Genomic_DNA.
EMBL; M28705; AAA59900.1; JOINED; Genomic_DNA.
EMBL; M28706; AAA59900.1; JOINED; Genomic_DNA.
EMBL; M28707; AAA59900.1; JOINED; Genomic_DNA.
EMBL; M28708; AAA59900.1; JOINED; Genomic_DNA.
EMBL; M28709; AAA59900.1; JOINED; Genomic_DNA.
EMBL; M28710; AAA59900.1; JOINED; Genomic_DNA.
EMBL; M28711; AAA59900.1; JOINED; Genomic_DNA.
EMBL; Y09501; CAA70696.1; -; mRNA.
EMBL; AF361370; AAL87744.1; -; mRNA.
EMBL; AJ010116; CAA09006.1; -; mRNA.
EMBL; AJ010117; CAA09007.1; -; mRNA.
EMBL; AJ010118; CAA09008.1; -; mRNA.
EMBL; AY341030; AAP88936.1; -; Genomic_DNA.
EMBL; BT009821; AAP88823.1; -; mRNA.
EMBL; CR456435; CAG30321.1; -; mRNA.
EMBL; AF061830; AAF06818.1; -; Genomic_DNA.
EMBL; AF061831; AAF06819.1; -; Genomic_DNA.
EMBL; AK302204; BAH13649.1; -; mRNA.
EMBL; Z93241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004821; AAH04821.1; -; mRNA.
EMBL; AJ310899; CAC84523.1; -; mRNA.
EMBL; AJ310900; CAC84524.1; -; mRNA.
EMBL; M16461; AAA52306.1; -; mRNA.
EMBL; M16462; AAA52307.1; -; mRNA.
CCDS; CCDS14040.1; -. [P00387-2]
CCDS; CCDS33658.1; -. [P00387-1]
CCDS; CCDS54535.1; -. [P00387-3]
PIR; JS0468; RDHUB5.
RefSeq; NP_000389.1; NM_000398.6. [P00387-1]
RefSeq; NP_001123291.1; NM_001129819.2. [P00387-2]
RefSeq; NP_001165131.1; NM_001171660.1. [P00387-3]
RefSeq; NP_001165132.1; NM_001171661.1. [P00387-2]
RefSeq; NP_015565.1; NM_007326.4. [P00387-2]
UniGene; Hs.561064; -.
PDB; 1M91; Model; -; A=1-301.
PDB; 1UMK; X-ray; 1.75 A; A=27-301.
PDBsum; 1M91; -.
PDBsum; 1UMK; -.
ProteinModelPortal; P00387; -.
SMR; P00387; -.
BioGrid; 108071; 47.
DIP; DIP-50463N; -.
IntAct; P00387; 66.
STRING; 9606.ENSP00000354468; -.
ChEMBL; CHEMBL2146; -.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB00157; NADH.
iPTMnet; P00387; -.
PhosphoSitePlus; P00387; -.
SwissPalm; P00387; -.
BioMuta; CYB5R3; -.
DMDM; 127846; -.
REPRODUCTION-2DPAGE; IPI00446235; -.
EPD; P00387; -.
MaxQB; P00387; -.
PaxDb; P00387; -.
PeptideAtlas; P00387; -.
PRIDE; P00387; -.
ProteomicsDB; 51238; -.
ProteomicsDB; 51239; -. [P00387-2]
ProteomicsDB; 51240; -. [P00387-3]
TopDownProteomics; P00387-1; -. [P00387-1]
TopDownProteomics; P00387-2; -. [P00387-2]
DNASU; 1727; -.
Ensembl; ENST00000352397; ENSP00000338461; ENSG00000100243. [P00387-1]
Ensembl; ENST00000361740; ENSP00000354468; ENSG00000100243. [P00387-3]
Ensembl; ENST00000402438; ENSP00000385679; ENSG00000100243. [P00387-2]
Ensembl; ENST00000407332; ENSP00000384457; ENSG00000100243. [P00387-2]
Ensembl; ENST00000407623; ENSP00000384834; ENSG00000100243. [P00387-2]
GeneID; 1727; -.
KEGG; hsa:1727; -.
UCSC; uc003bcx.4; human. [P00387-1]
CTD; 1727; -.
DisGeNET; 1727; -.
EuPathDB; HostDB:ENSG00000100243.20; -.
GeneCards; CYB5R3; -.
HGNC; HGNC:2873; CYB5R3.
HPA; HPA001566; -.
MalaCards; CYB5R3; -.
MIM; 250800; phenotype.
MIM; 613213; gene.
neXtProt; NX_P00387; -.
OpenTargets; ENSG00000100243; -.
Orphanet; 621; Hereditary methemoglobinemia.
PharmGKB; PA27331; -.
eggNOG; KOG0534; Eukaryota.
eggNOG; COG0543; LUCA.
GeneTree; ENSGT00940000153962; -.
HOGENOM; HOG000175005; -.
HOVERGEN; HBG052580; -.
InParanoid; P00387; -.
KO; K00326; -.
OMA; HNTAIYR; -.
OrthoDB; EOG091G0EIS; -.
PhylomeDB; P00387; -.
TreeFam; TF314333; -.
BioCyc; MetaCyc:HS02015-MONOMER; -.
BRENDA; 1.6.2.2; 2681.
Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P00387; -.
EvolutionaryTrace; P00387; -.
GeneWiki; CYB5R3; -.
GenomeRNAi; 1727; -.
PRO; PR:P00387; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100243; Expressed in 239 organ(s), highest expression level in thoracic aorta.
CleanEx; HS_CYB5R3; -.
ExpressionAtlas; P00387; baseline and differential.
Genevisible; P00387; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005833; C:hemoglobin complex; TAS:ProtInc.
GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
GO; GO:0043531; F:ADP binding; IEA:Ensembl.
GO; GO:0016208; F:AMP binding; IEA:Ensembl.
GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; TAS:Reactome.
GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
GO; GO:0051287; F:NAD binding; IEA:Ensembl.
GO; GO:0008015; P:blood circulation; TAS:ProtInc.
GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0019852; P:L-ascorbic acid metabolic process; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
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 promoter usage;
Alternative splicing; Cholesterol biosynthesis;
Cholesterol metabolism; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Endoplasmic reticulum;
FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Lipoprotein;
Membrane; Mitochondrion; Mitochondrion outer membrane; Myristate; NAD;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome;
Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
Sterol metabolism.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805}.
CHAIN 2 301 NADH-cytochrome b5 reductase 3 membrane-
bound form.
/FTId=PRO_0000019392.
CHAIN 27 301 NADH-cytochrome b5 reductase 3 soluble
form.
/FTId=PRO_0000019394.
DOMAIN 40 152 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 132 147 FAD. {ECO:0000250}.
NP_BIND 171 206 FAD. {ECO:0000250}.
MOD_RES 42 42 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 43 43 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 120 120 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9DCN2}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:2498303,
ECO:0000269|PubMed:25255805}.
VAR_SEQ 1 23 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_010200.
VAR_SEQ 1 7 MGAQLST -> MNRSLLVGCMQSKDIWGREESICERLKQDG
LDVERAESWE (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042827.
VARIANT 58 58 R -> Q (in METHB-CYB5R3; type 1; 62% of
activity; dbSNP:rs121965007).
{ECO:0000269|PubMed:15622768,
ECO:0000269|PubMed:1707593,
ECO:0000269|Ref.4}.
/FTId=VAR_004619.
VARIANT 66 66 S -> P (in dbSNP:rs1130706).
{ECO:0000269|PubMed:2479590,
ECO:0000269|PubMed:3035541,
ECO:0000269|Ref.4}.
/FTId=VAR_018419.
VARIANT 73 73 L -> P (in METHB-CYB5R3; type 1;
dbSNP:rs121965013).
{ECO:0000269|PubMed:9695975,
ECO:0000269|Ref.4}.
/FTId=VAR_010750.
VARIANT 106 106 V -> M (in METHB-CYB5R3; type 1; 77% of
activity; dbSNP:rs121965009).
{ECO:0000269|PubMed:1400360}.
/FTId=VAR_004620.
VARIANT 117 117 T -> S (in dbSNP:rs1800457).
{ECO:0000269|PubMed:9048929,
ECO:0000269|Ref.5}.
/FTId=VAR_010751.
VARIANT 128 128 S -> P (in METHB-CYB5R3; type 2;
Hiroshima; dbSNP:rs121965006).
{ECO:0000269|PubMed:1898726}.
/FTId=VAR_004621.
VARIANT 149 149 L -> P (in METHB-CYB5R3;
dbSNP:rs121965008).
{ECO:0000269|PubMed:1707593}.
/FTId=VAR_004622.
VARIANT 179 179 A -> V (in METHB-CYB5R3; type 1;
dbSNP:rs201232518).
{ECO:0000269|PubMed:9886302}.
/FTId=VAR_010752.
VARIANT 204 204 C -> R (in METHB-CYB5R3; type 2;
dbSNP:rs121965011).
{ECO:0000269|PubMed:7718898}.
/FTId=VAR_010753.
VARIANT 204 204 C -> Y (in METHB-CYB5R3; type 1;
dbSNP:rs121965015).
{ECO:0000269|PubMed:10807796,
ECO:0000269|Ref.4}.
/FTId=VAR_010754.
VARIANT 256 256 Missing (in METHB-CYB5R3; type 1; retains
approximately 38% of residual diaphorase
activity). {ECO:0000269|PubMed:12393396,
ECO:0000269|PubMed:15953014}.
/FTId=VAR_037315.
VARIANT 273 273 Missing (in METHB-CYB5R3; type 2).
{ECO:0000269|PubMed:7718898}.
/FTId=VAR_010755.
VARIANT 292 292 G -> D (in METHB-CYB5R3; type 1; retains
approximately 58% of residual diaphorase
activity; dbSNP:rs121965016).
{ECO:0000269|PubMed:12393396,
ECO:0000269|PubMed:15953014}.
/FTId=VAR_037316.
VARIANT 299 299 Missing (in METHB-CYB5R3; type2; almost
complete loss of activity).
{ECO:0000269|PubMed:8119939}.
/FTId=VAR_004623.
CONFLICT 28 32 QRSTP -> RWPRA (in Ref. 11; AAA52307).
{ECO:0000305}.
CONFLICT 29 29 R -> G (in Ref. 1; AAA59900).
{ECO:0000305}.
CONFLICT 31 31 T -> K (in Ref. 4; CAA09006/CAA09007/
CAA09008). {ECO:0000305}.
CONFLICT 34 35 IT -> LA (in Ref. 11; AAA52307).
{ECO:0000305}.
CONFLICT 187 188 ML -> IV (in Ref. 4; CAA09006/CAA09007).
{ECO:0000305}.
CONFLICT 191 192 IR -> MS (in Ref. 4; CAA09006/CAA09007).
{ECO:0000305}.
CONFLICT 192 192 R -> G (in Ref. 11; AAA52306).
{ECO:0000305}.
CONFLICT 233 234 FK -> CN (in Ref. 4; CAA09006/CAA09007).
{ECO:0000305}.
CONFLICT 280 280 I -> N (in Ref. 3; AAL87744).
{ECO:0000305}.
STRAND 43 52 {ECO:0000244|PDB:1UMK}.
STRAND 54 63 {ECO:0000244|PDB:1UMK}.
STRAND 78 85 {ECO:0000244|PDB:1UMK}.
STRAND 88 94 {ECO:0000244|PDB:1UMK}.
STRAND 104 111 {ECO:0000244|PDB:1UMK}.
STRAND 115 118 {ECO:0000244|PDB:1UMK}.
HELIX 126 133 {ECO:0000244|PDB:1UMK}.
STRAND 139 146 {ECO:0000244|PDB:1UMK}.
STRAND 148 153 {ECO:0000244|PDB:1UMK}.
STRAND 156 159 {ECO:0000244|PDB:1UMK}.
STRAND 168 171 {ECO:0000244|PDB:1UMK}.
STRAND 173 180 {ECO:0000244|PDB:1UMK}.
HELIX 181 183 {ECO:0000244|PDB:1UMK}.
HELIX 184 195 {ECO:0000244|PDB:1UMK}.
STRAND 203 212 {ECO:0000244|PDB:1UMK}.
HELIX 213 215 {ECO:0000244|PDB:1UMK}.
HELIX 219 228 {ECO:0000244|PDB:1UMK}.
TURN 230 232 {ECO:0000244|PDB:1UMK}.
STRAND 233 241 {ECO:0000244|PDB:1UMK}.
STRAND 247 252 {ECO:0000244|PDB:1UMK}.
HELIX 255 261 {ECO:0000244|PDB:1UMK}.
HELIX 265 267 {ECO:0000244|PDB:1UMK}.
STRAND 270 275 {ECO:0000244|PDB:1UMK}.
HELIX 277 282 {ECO:0000244|PDB:1UMK}.
HELIX 285 291 {ECO:0000244|PDB:1UMK}.
HELIX 295 297 {ECO:0000244|PDB:1UMK}.
STRAND 298 300 {ECO:0000244|PDB:1UMK}.
SEQUENCE 301 AA; 34235 MW; FDCDCDC4EC3570B4 CRC64;
MGAQLSTLGH MVLFPVWFLY SLLMKLFQRS TPAITLESPD IKYPLRLIDR EIISHDTRRF
RFALPSPQHI LGLPVGQHIY LSARIDGNLV VRPYTPISSD DDKGFVDLVI KVYFKDTHPK
FPAGGKMSQY LESMQIGDTI EFRGPSGLLV YQGKGKFAIR PDKKSNPIIR TVKSVGMIAG
GTGITPMLQV IRAIMKDPDD HTVCHLLFAN QTEKDILLRP ELEELRNKHS ARFKLWYTLD
RAPEAWDYGQ GFVNEEMIRD HLPPPEEEPL VLMCGPPPMI QYACLPNLDH VGHPTERCFV
F


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