CY24B_HUMAN
ID CY24B_HUMAN Reviewed; 570 AA.
AC P04839; A8K138; Q2PP16;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=Cytochrome b-245 heavy chain;
DE EC=1.-.-.-;
DE AltName: Full=CGD91-phox;
DE AltName: Full=Cytochrome b(558) subunit beta;
DE Short=Cytochrome b558 subunit beta;
DE AltName: Full=Heme-binding membrane glycoprotein gp91phox;
DE AltName: Full=NADPH oxidase 2;
DE AltName: Full=Neutrophil cytochrome b 91 kDa polypeptide;
DE AltName: Full=Superoxide-generating NADPH oxidase heavy chain subunit;
DE AltName: Full=gp91-1;
DE AltName: Full=gp91-phox;
DE AltName: Full=p22 phagocyte B-cytochrome;
GN Name=CYBB {ECO:0000312|HGNC:HGNC:2578}; Synonyms=NOX2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CGDX ASP-41 AND ARG-537, AND
RP VARIANTS ARG-364 AND GLU-517.
RX PubMed=12139950; DOI=10.1006/clim.2002.5230;
RA Jirapongsananuruk O., Niemela J.E., Malech H.L., Fleisher T.A.;
RT "CYBB mutation analysis in X-linked chronic granulomatous disease.";
RL Clin. Immunol. 104:73-76(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-570.
RX PubMed=2425263; DOI=10.1038/322032a0;
RA Royer-Pokora B., Kunkel L.M., Monaco A.P., Goff S.C., Newburger P.E.,
RA Baehner R.L., Cole F.S., Curnutte J.T., Orkin S.H.;
RT "Cloning the gene for an inherited human disorder -- chronic granulomatous
RT disease -- on the basis of its chromosomal location.";
RL Nature 322:32-38(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RX PubMed=3600768; DOI=10.1038/327717a0;
RA Dinauer M.C., Orkin S.H., Brown R., Jesaitis A.J., Parkos C.A.;
RT "The glycoprotein encoded by the X-linked chronic granulomatous disease
RT locus is a component of the neutrophil cytochrome b complex.";
RL Nature 327:717-720(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-267.
RC TISSUE=Peripheral blood;
RX PubMed=9790760; DOI=10.1006/geno.1998.5510;
RA Kumatori A., Faizunnessa N.N., Suzuki S., Moriuchi T., Kurozumi H.,
RA Nakamura M.;
RT "Nonhomologous recombination between the cytochrome b558 heavy chain gene
RT (CYBB) and LINE-1 causes an X-linked chronic granulomatous disease.";
RL Genomics 53:123-128(1998).
RN [9]
RP PROTEIN SEQUENCE OF 2-44, AND SUBUNIT.
RX PubMed=3600769; DOI=10.1038/327720a0;
RA Teahan C., Rowe P., Parker P., Totty N., Segal A.W.;
RT "The X-linked chronic granulomatous disease gene codes for the beta-chain
RT of cytochrome b-245.";
RL Nature 327:720-721(1987).
RN [10]
RP CHARACTERIZATION AS A PROTON CHANNEL.
RX PubMed=10578014; DOI=10.1085/jgp.114.6.771;
RA Henderson L.M., Meech R.W.;
RT "Evidence that the product of the human X-linked CGD gene, gp91-phox, is a
RT voltage-gated H(+) pathway.";
RL J. Gen. Physiol. 114:771-786(1999).
RN [11]
RP SUBUNIT, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=19028840; DOI=10.1096/fj.08-114553;
RA Raad H., Paclet M.H., Boussetta T., Kroviarski Y., Morel F., Quinn M.T.,
RA Gougerot-Pocidalo M.A., Dang P.M., El-Benna J.;
RT "Regulation of the phagocyte NADPH oxidase activity: phosphorylation of
RT gp91phox/NOX2 by protein kinase C enhances its diaphorase activity and
RT binding to Rac2, p67phox, and p47phox.";
RL FASEB J. 23:1011-1022(2009).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-132; ASN-149 AND ASN-240.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP INTERACTION WITH CYBC1, AND SUBCELLULAR LOCATION.
RX PubMed=28351984; DOI=10.1084/jem.20161382;
RA Thomas D.C., Clare S., Sowerby J.M., Pardo M., Juss J.K., Goulding D.A.,
RA van der Weyden L., Storisteanu D., Prakash A., Espeli M., Flint S.,
RA Lee J.C., Hoenderdos K., Kane L., Harcourt K., Mukhopadhyay S., Umrania Y.,
RA Antrobus R., Nathan J.A., Adams D.J., Bateman A., Choudhary J.S.,
RA Lyons P.A., Condliffe A.M., Chilvers E.R., Dougan G., Smith K.G.;
RT "Eros is a novel transmembrane protein that controls the phagocyte
RT respiratory burst and is essential for innate immunity.";
RL J. Exp. Med. 214:1111-1128(2017).
RN [15]
RP STRUCTURE BY NMR OF 556-570 IN COMPLEX WITH NCF1, AND INTERACTION WITH
RP NCF1.
RX PubMed=9224653; DOI=10.1042/bj3250249;
RA Adams E.R., Dratz E.A., Gizachew D., Deleo F.R., Yu L., Volpp B.D.,
RA Vlases M., Jesaitis A.J., Quinn M.T.;
RT "Interaction of human neutrophil flavocytochrome b with cytosolic proteins:
RT transferred-NOESY NMR studies of a gp91phox C-terminal peptide bound to
RT p47phox.";
RL Biochem. J. 325:249-257(1997).
RN [16]
RP INVOLVEMENT IN CGDX, AND VARIANT CGDX HIS-415.
RX PubMed=2556453; DOI=10.1172/jci114393;
RA Dinauer M.C., Curnutte J.T., Rosen H.R., Orkin S.H.;
RT "A missense mutation in the neutrophil cytochrome b heavy chain in
RT cytochrome-positive X-linked chronic granulomatous disease.";
RL J. Clin. Invest. 84:2012-2016(1989).
RN [17]
RP VARIANTS CGDX ARG-101; THR-156; TYR-209; SER-244 AND ALA-389.
RX PubMed=1710153;
RA Bolscher B.G.J.M., de Boer M., de Klein A., Weening R.S., Roos D.;
RT "Point mutations in the beta-subunit of cytochrome b558 leading to X-linked
RT chronic granulomatous disease.";
RL Blood 77:2482-2487(1991).
RN [18]
RP VARIANT CGDX GLU-57.
RX PubMed=8101486; DOI=10.1007/bf01955051;
RA Ariga T., Sakiyama Y., Tomizawa K., Imajoh-Ohmi S., Kanegasaki S.,
RA Matsumoto S.;
RT "A newly recognized point mutation in the cytochrome b558 heavy chain gene
RT replacing alanine57 by glutamic acid, in a patient with cytochrome b
RT positive X-linked chronic granulomatous disease.";
RL Eur. J. Pediatr. 152:469-472(1993).
RN [19]
RP VARIANT CGDX HIS-339.
RX PubMed=7927345; DOI=10.1007/bf00201609;
RA Ariga T., Sakiyama Y., Matsumoto S.;
RT "Two novel point mutations in the cytochrome b 558 heavy chain gene,
RT detected in two Japanese patients with X-linked chronic granulomatous
RT disease.";
RL Hum. Genet. 94:441-441(1994).
RN [20]
RP VARIANT CGDX GLY-500.
RX PubMed=8182143; DOI=10.1172/jci117207;
RA Leusen J.H.W., de Boer M., Bolscher B.G.J.M., Hilarius P.M., Weening R.S.,
RA Ochs H.D., Roos D., Verhoeven A.J.;
RT "A point mutation in gp91-phox of cytochrome b558 of the human NADPH
RT oxidase leading to defective translocation of the cytosolic proteins p47-
RT phox and p67-phox.";
RL J. Clin. Invest. 93:2120-2126(1994).
RN [21]
RP VARIANTS CGDX ILE-205; PHE-215 DEL AND GLN-342.
RX PubMed=8916969;
RA Hui Y.F., Chan S.Y., Lau Y.L.;
RT "Identification of mutations in seven Chinese patients with X-linked
RT chronic granulomatous disease.";
RL Blood 88:4021-4028(1996).
RN [22]
RP ERRATUM OF PUBMED:8916969.
RA Hui Y.F., Chan S.Y., Lau Y.L.;
RL Blood 89:1843-1843(1996).
RN [23]
RP VARIANT CGDX PHE-215 DEL.
RX PubMed=9111587; DOI=10.1111/j.1600-0609.1997.tb00928.x;
RA Jendrossek V., Ritzel A., Neubauer B., Heyden S., Gahr M.;
RT "An in-frame triplet deletion within the gp91-phox gene in an adult X-
RT linked chronic granulomatous disease patient with residual NADPH-oxidase
RT activity.";
RL Eur. J. Haematol. 58:78-85(1997).
RN [24]
RP VARIANTS CGDX ARG-20; SER-54; ARG-59; ARG-119; THR-156; GLN-209; ASN-222;
RP ARG-222; TYR-222; LEU-223; ARG-244; LYS-309; LYS-315 DEL; GLU-322; PHE-325;
RP PRO-333; HIS-339; PRO-356; ARG-405; GLU-408; ARG-408; HIS-415; LEU-415;
RP PRO-422; ARG-453; CYS-516; ASP-534 AND ARG-537.
RX PubMed=9585602; DOI=10.1086/301874;
RA Rae J., Newburger P.E., Dinauer M.C., Noack D., Hopkins P.J., Kuruto R.,
RA Curnutte J.T.;
RT "X-linked chronic granulomatous disease: mutations in the CYBB gene
RT encoding the gp91-phox component of respiratory-burst oxidase.";
RL Am. J. Hum. Genet. 62:1320-1331(1998).
RN [25]
RP VARIANT CGDX TYR-101.
RX PubMed=9856476; DOI=10.1007/s004390050836;
RA Tsuda M., Kaneda M., Sakiyama T., Inana I., Owada M., Kiryu C.,
RA Shiraishi T., Kakinuma K.;
RT "A novel mutation at a probable heme-binding ligand in neutrophil
RT cytochrome b558 in atypical X-linked chronic granulomatous disease.";
RL Hum. Genet. 103:377-381(1998).
RN [26]
RP VARIANTS CGDX ARG-179 AND 298-THR--THR-302 DEL.
RX PubMed=9794433;
RA Dusi S., Nadalini K.A., Donini M., Zentilin L., Wientjes F.B., Roos D.,
RA Giacca M., Rossi F.;
RT "Nicotinamide-adenine dinucleotide phosphate oxidase assembly and
RT activation in EBV-transformed B lymphoblastoid cell lines of normal and
RT chronic granulomatous disease patients.";
RL J. Immunol. 161:4968-4974(1998).
RN [27]
RP VARIANTS CGDX MET-54; ASP-55; GLU-57; HIS-339 AND PHE-344.
RX PubMed=9667376; DOI=10.1203/00006450-199807000-00014;
RA Ariga T., Furuta H., Cho K., Sakiyama Y.;
RT "Genetic analysis of 13 families with X-linked chronic granulomatous
RT disease reveals a low proportion of sporadic patients and a high proportion
RT of sporadic carriers.";
RL Pediatr. Res. 44:85-92(1998).
RN [28]
RP VARIANTS CGDX PHE-193; ARG-222; TYR-338; HIS-339 AND PRO-546, AND VARIANT
RP ARG-364.
RX PubMed=10089913; DOI=10.1016/s0301-472x(98)00024-1;
RA Roesler J., Heyden S., Burdelski M., Schaefer H., Kreth H.-W., Lehmann R.,
RA Paul D., Marzahn J., Gahr M., Roesen-Wolff A.;
RT "Uncommon missense and splice mutations and resulting biochemical
RT phenotypes in German patients with X-linked chronic granulomatous
RT disease.";
RL Exp. Hematol. 27:505-511(1999).
RN [29]
RP VARIANTS CGDX VAL-225 AND TYR-244.
RX PubMed=9888386;
RX DOI=10.1002/(sici)1098-1004(1999)13:1<29::aid-humu3>3.0.co;2-x;
RA Patino P.J., Perez J.E., Lopez J.A., Condino-Neto A., Grumach A.S.,
RA Botero J.H., Curnutte J.T., Garcia de Olarte D.;
RT "Molecular analysis of chronic granulomatous disease caused by defects in
RT gp91-phox.";
RL Hum. Mutat. 13:29-37(1999).
RN [30]
RP VARIANTS CGDX MET-54; ASP-55; GLU-57; TYR-101; ARG-209; GLY-224; LYS-309;
RP TYR-338; HIS-339; PHE-344; GLU-389; PRO-420 AND ARG-516.
RX PubMed=10914676; DOI=10.1007/s004390000288;
RA Ishibashi F., Nunoi H., Endo F., Matsuda I., Kanegasaki S.;
RT "Statistical and mutational analysis of chronic granulomatous disease in
RT Japan with special reference to gp91-phox and p22-phox deficiency.";
RL Hum. Genet. 106:473-481(2000).
RN [31]
RP VARIANTS CGDX 54-ARG-ALA-55 DEL; TRP-59; PRO-307 AND ARG-505.
RX PubMed=11462241; DOI=10.1002/humu.1166;
RA Gerard B., El Benna J., Alcain F., Gougerot-Pocidalo M.-A., Grandchamp B.,
RA Chollet-Martin S.;
RT "Characterization of 11 novel mutations in the X-linked chronic
RT granulomatous disease (CYBB gene).";
RL Hum. Mutat. 18:163-163(2001).
RN [32]
RP VARIANTS CGDX ASN-303 AND ARG-304.
RX PubMed=11997083; DOI=10.1016/s0925-4439(01)00110-7;
RA Stasia M.J., Lardy B., Maturana A., Rousseau P., Martel C., Bordigoni P.,
RA Demaurex N., Morel F.;
RT "Molecular and functional characterization of a new X-linked chronic
RT granulomatous disease variant (X91+) case with a double missense mutation
RT in the cytosolic gp91phox C-terminal tail.";
RL Biochim. Biophys. Acta 1586:316-330(2002).
RN [33]
RP CHARACTERIZATION OF VARIANTS CGDX ASN-303 AND ARG-304.
RX PubMed=15338276; DOI=10.1007/s00439-004-1173-z;
RA Bionda C., Li X.J., van Bruggen R., Eppink M., Roos D., Morel F.,
RA Stasia M.-J.;
RT "Functional analysis of two-amino acid substitutions in gp91 phox in a
RT patient with X-linked flavocytochrome b558-positive chronic granulomatous
RT disease by means of transgenic PLB-985 cells.";
RL Hum. Genet. 115:418-427(2004).
RN [34]
RP VARIANT CGDX ARG-408.
RX PubMed=18773283; DOI=10.1007/s10875-008-9243-y;
RA Bakri F.G., Martel C., Khuri-Bulos N., Mahafzah A., El-Khateeb M.S.,
RA Al-Wahadneh A.M., Hayajneh W.A., Hamamy H.A., Maquet E., Molin M.,
RA Stasia M.J.;
RT "First report of clinical, functional, and molecular investigation of
RT chronic granulomatous disease in nine Jordanian families.";
RL J. Clin. Immunol. 29:215-230(2009).
RN [35]
RP VARIANTS IMD34 PRO-178 AND PRO-231.
RX PubMed=21278736; DOI=10.1038/ni.1992;
RA Bustamante J., Arias A.A., Vogt G., Picard C., Galicia L.B., Prando C.,
RA Grant A.V., Marchal C.C., Hubeau M., Chapgier A., de Beaucoudrey L.,
RA Puel A., Feinberg J., Valinetz E., Janniere L., Besse C., Boland A.,
RA Brisseau J.M., Blanche S., Lortholary O., Fieschi C., Emile J.F.,
RA Boisson-Dupuis S., Al-Muhsen S., Woda B., Newburger P.E., Condino-Neto A.,
RA Dinauer M.C., Abel L., Casanova J.L.;
RT "Germline CYBB mutations that selectively affect macrophages in kindreds
RT with X-linked predisposition to tuberculous mycobacterial disease.";
RL Nat. Immunol. 12:213-221(2011).
RN [36]
RP VARIANTS CGDX ASP-488 AND GLU-500.
RX PubMed=22125116; DOI=10.1002/humu.22003;
RA Boog B., Quach A., Costabile M., Smart J., Quinn P., Singh H., Gold M.,
RA Booker G., Choo S., Hii C.S., Ferrante A.;
RT "Identification and functional characterization of two novel mutations in
RT the alpha-helical loop (residues 484-503) of CYBB/gp91(phox) resulting in
RT the rare X91(+) variant of chronic granulomatous disease.";
RL Hum. Mutat. 33:471-475(2012).
RN [37]
RP VARIANTS CGDX ASN-299; ASP-338; HIS-339; PHE-344 AND GLU-412.
RX PubMed=23910690; DOI=10.1016/j.jaci.2013.05.039;
RA Koker M.Y., Camcioglu Y., van Leeuwen K., Kilic S.S., Barlan I., Yilmaz M.,
RA Metin A., de Boer M., Avcilar H., Patiroglu T., Yildiran A., Yegin O.,
RA Tezcan I., Sanal O., Roos D.;
RT "Clinical, functional, and genetic characterization of chronic
RT granulomatous disease in 89 Turkish patients.";
RL J. Allergy Clin. Immunol. 132:1156-1163(2013).
RN [38]
RP VARIANT CGDX GLY-409.
RX PubMed=27666509; DOI=10.1016/j.micpath.2016.09.020;
RA Khan T.A., Kalsoom K., Iqbal A., Asif H., Rahman H., Farooq S.O.,
RA Naveed H., Nasir U., Amin M.U., Hussain M., Tipu H.N., Florea A.;
RT "A novel missense mutation in the NADPH binding domain of CYBB abolishes
RT the NADPH oxidase activity in a male patient with increased susceptibility
RT to infections.";
RL Microb. Pathog. 100:163-169(2016).
CC -!- FUNCTION: Critical component of the membrane-bound oxidase of
CC phagocytes that generates superoxide. It is the terminal component of a
CC respiratory chain that transfers single electrons from cytoplasmic
CC NADPH across the plasma membrane to molecular oxygen on the exterior.
CC Also functions as a voltage-gated proton channel that mediates the H(+)
CC currents of resting phagocytes. It participates in the regulation of
CC cellular pH and is blocked by zinc.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- SUBUNIT: Composed of a heavy chain (beta) and a light chain (alpha).
CC Component of an NADPH oxidase complex composed of a heterodimer formed
CC by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1,
CC NCF2 and NCF4. Interacts with NCF1. Interacts with calprotectin
CC (S100A8/9). Interacts with NRROS; the interaction is direct and impairs
CC formation of a stable NADPH oxidase complex (PubMed:19028840,
CC PubMed:3600769, PubMed:9224653). Interacts with CYBC1; CYBC1 may act as
CC a chaperone stabilizing Cytochrome b-245 heterodimer (PubMed:28351984).
CC Interacts with NCF2; the interaction is enhanced in the presence of
CC GBP7 (By similarity). The CYBA-CYBB complex interacts with GBP7 (By
CC similarity). {ECO:0000250|UniProtKB:Q61093,
CC ECO:0000269|PubMed:19028840, ECO:0000269|PubMed:28351984,
CC ECO:0000269|PubMed:3600769, ECO:0000269|PubMed:9224653}.
CC -!- INTERACTION:
CC P04839; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-6253630, EBI-2680384;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Note=As unassembled monomer may localize to the endoplasmic reticulum.
CC {ECO:0000305|PubMed:28351984}.
CC -!- TISSUE SPECIFICITY: Detected in neutrophils (at protein level).
CC {ECO:0000269|PubMed:19028840}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19159218}.
CC -!- PTM: Phosphorylated on Ser and Thr residues.
CC {ECO:0000269|PubMed:19028840}.
CC -!- PTM: Undergoes 'Lys-48'-linked polyubiquitination, likely by RNF145,
CC triggering endoplasmic reticulum-associated degradation.
CC {ECO:0000250|UniProtKB:Q61093}.
CC -!- DISEASE: Granulomatous disease, chronic, X-linked (CGDX) [MIM:306400]:
CC A form of chronic granulomatous disease, a primary immunodeficiency
CC characterized by severe recurrent bacterial and fungal infections,
CC along with manifestations of chronic granulomatous inflammation. It
CC results from an impaired ability of phagocytes to mount a burst of
CC reactive oxygen species in response to pathogens.
CC {ECO:0000269|PubMed:10089913, ECO:0000269|PubMed:10914676,
CC ECO:0000269|PubMed:11462241, ECO:0000269|PubMed:11997083,
CC ECO:0000269|PubMed:12139950, ECO:0000269|PubMed:15338276,
CC ECO:0000269|PubMed:1710153, ECO:0000269|PubMed:18773283,
CC ECO:0000269|PubMed:22125116, ECO:0000269|PubMed:23910690,
CC ECO:0000269|PubMed:2556453, ECO:0000269|PubMed:27666509,
CC ECO:0000269|PubMed:7927345, ECO:0000269|PubMed:8101486,
CC ECO:0000269|PubMed:8182143, ECO:0000269|PubMed:8916969,
CC ECO:0000269|PubMed:9111587, ECO:0000269|PubMed:9585602,
CC ECO:0000269|PubMed:9667376, ECO:0000269|PubMed:9794433,
CC ECO:0000269|PubMed:9856476, ECO:0000269|PubMed:9888386}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Immunodeficiency 34 (IMD34) [MIM:300645]: A form of Mendelian
CC susceptibility to mycobacterial disease, a rare condition characterized
CC by predisposition to illness caused by moderately virulent
CC mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine,
CC environmental non-tuberculous mycobacteria, and by the more virulent
CC Mycobacterium tuberculosis. Other microorganisms rarely cause severe
CC clinical disease in individuals with susceptibility to mycobacterial
CC infections, with the exception of Salmonella which infects less than
CC 50% of these individuals. {ECO:0000269|PubMed:21278736}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27635.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA29327.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=CYBBbase; Note=CYBB deficiency database;
CC URL="http://structure.bmc.lu.se/idbase/CYBBbase/";
CC -!- WEB RESOURCE: Name=Mendelian genes cytochrome b-245, beta polypeptide
CC (CYBB); Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/CYBB";
CC ---------------------------------------------------------------------------
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DR EMBL; X04011; CAA27635.1; ALT_INIT; mRNA.
DR EMBL; AF469769; AAL76082.1; -; Genomic_DNA.
DR EMBL; AF469757; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469758; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469759; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469760; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469761; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469762; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469763; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469764; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469765; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469766; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469767; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; AF469768; AAL76082.1; JOINED; Genomic_DNA.
DR EMBL; DQ314869; ABC40728.1; -; Genomic_DNA.
DR EMBL; AK289753; BAF82442.1; -; mRNA.
DR EMBL; CH471141; EAW59453.1; -; Genomic_DNA.
DR EMBL; BC032720; AAH32720.1; -; mRNA.
DR EMBL; X05895; CAA29327.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB013904; BAA34183.1; -; Genomic_DNA.
DR CCDS; CCDS14242.1; -.
DR PIR; S70773; S70773.
DR RefSeq; NP_000388.2; NM_000397.3.
DR PDB; 3A1F; X-ray; 2.00 A; A=385-570.
DR PDBsum; 3A1F; -.
DR AlphaFoldDB; P04839; -.
DR SMR; P04839; -.
DR BioGRID; 107916; 18.
DR ComplexPortal; CPX-1017; Phagocyte NADPH oxidase complex, RAC1 variant.
DR ComplexPortal; CPX-6134; Phagocyte NADPH oxidase complex, RAC2 variant.
DR ComplexPortal; CPX-6135; Phagocyte NADPH oxidase complex, RAC3 variant.
DR DIP; DIP-42005N; -.
DR IntAct; P04839; 4.
DR STRING; 9606.ENSP00000367851; -.
DR BindingDB; P04839; -.
DR ChEMBL; CHEMBL1287627; -.
DR DrugBank; DB00514; Dextromethorphan.
DR GuidetoPHARMACOLOGY; 3002; -.
DR PeroxiBase; 5962; HsNOx02.
DR TCDB; 5.B.1.1.1; the phagocyte (gp91(phox)) nadph oxidase family.
DR GlyConnect; 1165; 2 N-Linked glycans (1 site).
DR GlyGen; P04839; 6 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P04839; -.
DR PhosphoSitePlus; P04839; -.
DR SwissPalm; P04839; -.
DR BioMuta; CYBB; -.
DR DMDM; 115211; -.
DR CPTAC; CPTAC-1181; -.
DR CPTAC; CPTAC-1203; -.
DR EPD; P04839; -.
DR jPOST; P04839; -.
DR MassIVE; P04839; -.
DR MaxQB; P04839; -.
DR PaxDb; P04839; -.
DR PeptideAtlas; P04839; -.
DR PRIDE; P04839; -.
DR ProteomicsDB; 51748; -.
DR ABCD; P04839; 1 sequenced antibody.
DR Antibodypedia; 24864; 513 antibodies from 40 providers.
DR DNASU; 1536; -.
DR Ensembl; ENST00000378588.5; ENSP00000367851.4; ENSG00000165168.8.
DR GeneID; 1536; -.
DR KEGG; hsa:1536; -.
DR MANE-Select; ENST00000378588.5; ENSP00000367851.4; NM_000397.4; NP_000388.2.
DR UCSC; uc004ddr.3; human.
DR CTD; 1536; -.
DR DisGeNET; 1536; -.
DR GeneCards; CYBB; -.
DR GeneReviews; CYBB; -.
DR HGNC; HGNC:2578; CYBB.
DR HPA; ENSG00000165168; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; CYBB; -.
DR MIM; 300481; gene.
DR MIM; 300645; phenotype.
DR MIM; 306400; phenotype.
DR neXtProt; NX_P04839; -.
DR OpenTargets; ENSG00000165168; -.
DR Orphanet; 379; Chronic granulomatous disease.
DR Orphanet; 319623; X-linked mendelian susceptibility to mycobacterial diseases due to CYBB deficiency.
DR PharmGKB; PA27076; -.
DR VEuPathDB; HostDB:ENSG00000165168; -.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000160244; -.
DR HOGENOM; CLU_005646_3_1_1; -.
DR InParanoid; P04839; -.
DR OMA; KPSMKYK; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; P04839; -.
DR TreeFam; TF105354; -.
DR PathwayCommons; P04839; -.
DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; P04839; -.
DR SIGNOR; P04839; -.
DR BioGRID-ORCS; 1536; 9 hits in 700 CRISPR screens.
DR ChiTaRS; CYBB; human.
DR GeneWiki; CYBB; -.
DR GenomeRNAi; 1536; -.
DR Pharos; P04839; Tchem.
DR PRO; PR:P04839; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P04839; protein.
DR Bgee; ENSG00000165168; Expressed in monocyte and 171 other tissues.
DR ExpressionAtlas; P04839; baseline and differential.
DR Genevisible; P04839; HS.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043020; C:NADPH oxidase complex; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IMP:BHF-UCL.
DR GO; GO:0020037; F:heme binding; IMP:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; TAS:BHF-UCL.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR GO; GO:1904845; P:cellular response to L-glutamine; IEA:Ensembl.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0022900; P:electron transport chain; IEA:GOC.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0097411; P:hypoxia-inducible factor-1alpha signaling pathway; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0045730; P:respiratory burst; IMP:BHF-UCL.
DR GO; GO:1904044; P:response to aldosterone; IEA:Ensembl.
DR GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0042554; P:superoxide anion generation; IDA:BHF-UCL.
DR GO; GO:0006801; P:superoxide metabolic process; IDA:BHF-UCL.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chronic granulomatous disease;
KW Direct protein sequencing; Disease variant; Electron transport; FAD;
KW Flavoprotein; Glycoprotein; Heme; Ion channel; Ion transport; Iron;
KW Isopeptide bond; Membrane; Metal-binding; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation; Voltage-gated channel.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3600769"
FT CHAIN 2..570
FT /note="Cytochrome b-245 heavy chain"
FT /id="PRO_0000210145"
FT TOPO_DOM 2..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..286
FT /note="Ferric oxidoreductase"
FT DOMAIN 287..397
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 101
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 115
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 209
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 222
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 338..344
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 506
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 567
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT VARIANT 18
FT /note="W -> C (in CGDX)"
FT /id="VAR_047264"
FT VARIANT 20
FT /note="G -> R (in CGDX; dbSNP:rs151344455)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007873"
FT VARIANT 41
FT /note="Y -> D (in CGDX; dbSNP:rs151344453)"
FT /evidence="ECO:0000269|PubMed:12139950"
FT /id="VAR_025613"
FT VARIANT 54..55
FT /note="Missing (in CGDX)"
FT /evidence="ECO:0000269|PubMed:11462241"
FT /id="VAR_047265"
FT VARIANT 54
FT /note="R -> M (in CGDX; dbSNP:rs151344479)"
FT /evidence="ECO:0000269|PubMed:10914676,
FT ECO:0000269|PubMed:23910690, ECO:0000269|PubMed:9667376"
FT /id="VAR_025614"
FT VARIANT 54
FT /note="R -> S (in CGDX; dbSNP:rs151344456)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007874"
FT VARIANT 55
FT /note="A -> D (in CGDX; dbSNP:rs151344480)"
FT /evidence="ECO:0000269|PubMed:10914676,
FT ECO:0000269|PubMed:9667376"
FT /id="VAR_025615"
FT VARIANT 57
FT /note="A -> E (in CGDX; dbSNP:rs151344481)"
FT /evidence="ECO:0000269|PubMed:10914676,
FT ECO:0000269|PubMed:8101486, ECO:0000269|PubMed:9667376"
FT /id="VAR_008845"
FT VARIANT 59
FT /note="C -> R (in CGDX; dbSNP:rs151344457)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007875"
FT VARIANT 59
FT /note="C -> W (in CGDX; dbSNP:rs151344488)"
FT /evidence="ECO:0000269|PubMed:11462241"
FT /id="VAR_047266"
FT VARIANT 101
FT /note="H -> R (in CGDX; dbSNP:rs137854591)"
FT /evidence="ECO:0000269|PubMed:1710153"
FT /id="VAR_002432"
FT VARIANT 101
FT /note="H -> Y (in CGDX; dbSNP:rs137854594)"
FT /evidence="ECO:0000269|PubMed:10914676,
FT ECO:0000269|PubMed:9856476"
FT /id="VAR_007876"
FT VARIANT 119
FT /note="H -> R (in CGDX; dbSNP:rs151344458)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007877"
FT VARIANT 156
FT /note="A -> T (in CGDX; dbSNP:rs137854590)"
FT /evidence="ECO:0000269|PubMed:1710153,
FT ECO:0000269|PubMed:9585602"
FT /id="VAR_002433"
FT VARIANT 178
FT /note="T -> P (in IMD34; dbSNP:rs151344497)"
FT /evidence="ECO:0000269|PubMed:21278736"
FT /id="VAR_065365"
FT VARIANT 179
FT /note="G -> R (in CGDX; dbSNP:rs151344491)"
FT /evidence="ECO:0000269|PubMed:9794433"
FT /id="VAR_047267"
FT VARIANT 193
FT /note="S -> F (in CGDX; dbSNP:rs151344493)"
FT /evidence="ECO:0000269|PubMed:10089913"
FT /id="VAR_047268"
FT VARIANT 205
FT /note="F -> I (in CGDX; dbSNP:rs151344496)"
FT /evidence="ECO:0000269|PubMed:8916969"
FT /id="VAR_047269"
FT VARIANT 209
FT /note="H -> Q (in CGDX; dbSNP:rs151344459)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007878"
FT VARIANT 209
FT /note="H -> R (in CGDX; dbSNP:rs151344482)"
FT /evidence="ECO:0000269|PubMed:10914676"
FT /id="VAR_025616"
FT VARIANT 209
FT /note="H -> Y (in CGDX; dbSNP:rs137854587)"
FT /evidence="ECO:0000269|PubMed:1710153"
FT /id="VAR_002434"
FT VARIANT 215
FT /note="Missing (in CGDX)"
FT /evidence="ECO:0000269|PubMed:8916969,
FT ECO:0000269|PubMed:9111587"
FT /id="VAR_007879"
FT VARIANT 222
FT /note="H -> N (in CGDX; dbSNP:rs151344460)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007880"
FT VARIANT 222
FT /note="H -> R (in CGDX; dbSNP:rs151344462)"
FT /evidence="ECO:0000269|PubMed:10089913,
FT ECO:0000269|PubMed:9585602"
FT /id="VAR_007881"
FT VARIANT 222
FT /note="H -> Y (in CGDX; dbSNP:rs151344460)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007882"
FT VARIANT 223
FT /note="G -> L (in CGDX; requires 2 nucleotide
FT substitutions; dbSNP:rs151344463 and dbSNP:rs151344464)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007883"
FT VARIANT 224
FT /note="A -> G (in CGDX; dbSNP:rs151344483)"
FT /evidence="ECO:0000269|PubMed:10914676"
FT /id="VAR_025617"
FT VARIANT 225
FT /note="E -> V (in CGDX; dbSNP:rs151344494)"
FT /evidence="ECO:0000269|PubMed:9888386"
FT /id="VAR_002435"
FT VARIANT 231
FT /note="Q -> P (in IMD34; dbSNP:rs151344498)"
FT /evidence="ECO:0000269|PubMed:21278736"
FT /id="VAR_065366"
FT VARIANT 244
FT /note="C -> R (in CGDX; dbSNP:rs151344465)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007884"
FT VARIANT 244
FT /note="C -> S (in CGDX; dbSNP:rs137854589)"
FT /evidence="ECO:0000269|PubMed:1710153"
FT /id="VAR_002436"
FT VARIANT 244
FT /note="C -> Y (in CGDX; dbSNP:rs137854589)"
FT /evidence="ECO:0000269|PubMed:9888386"
FT /id="VAR_002437"
FT VARIANT 298..302
FT /note="Missing (in CGDX)"
FT /evidence="ECO:0000269|PubMed:9794433"
FT /id="VAR_047270"
FT VARIANT 299
FT /note="K -> N (in CGDX)"
FT /evidence="ECO:0000269|PubMed:23910690"
FT /id="VAR_071861"
FT VARIANT 303
FT /note="H -> N (in CGDX; completely inhibits NADPH oxidase
FT activity; NADPH oxidase assembly is abolished;
FT dbSNP:rs137854595)"
FT /evidence="ECO:0000269|PubMed:11997083,
FT ECO:0000269|PubMed:15338276"
FT /id="VAR_016880"
FT VARIANT 304
FT /note="P -> R (in CGDX; reduces NADPH oxidase activity to
FT 4% of wild-type; translocation to the membrane of the
FT phagosome is only attenuated; dbSNP:rs137854596)"
FT /evidence="ECO:0000269|PubMed:11997083,
FT ECO:0000269|PubMed:15338276"
FT /id="VAR_016881"
FT VARIANT 307
FT /note="T -> P (in CGDX; dbSNP:rs151344489)"
FT /evidence="ECO:0000269|PubMed:11462241"
FT /id="VAR_047271"
FT VARIANT 309
FT /note="E -> K (in CGDX; dbSNP:rs151344466)"
FT /evidence="ECO:0000269|PubMed:10914676,
FT ECO:0000269|PubMed:9585602"
FT /id="VAR_007885"
FT VARIANT 315
FT /note="Missing (in CGDX)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_047272"
FT VARIANT 322
FT /note="G -> E (in CGDX; dbSNP:rs151344467)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007886"
FT VARIANT 325
FT /note="I -> F (in CGDX; dbSNP:rs151344468)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007887"
FT VARIANT 333
FT /note="S -> P (in CGDX; dbSNP:rs151344469)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007888"
FT VARIANT 338
FT /note="H -> D (in CGDX)"
FT /evidence="ECO:0000269|PubMed:23910690"
FT /id="VAR_071862"
FT VARIANT 338
FT /note="H -> Y (in CGDX; dbSNP:rs151344484)"
FT /evidence="ECO:0000269|PubMed:10089913,
FT ECO:0000269|PubMed:10914676"
FT /id="VAR_025618"
FT VARIANT 339
FT /note="P -> H (in CGDX; dbSNP:rs151344470)"
FT /evidence="ECO:0000269|PubMed:10089913,
FT ECO:0000269|PubMed:10914676, ECO:0000269|PubMed:23910690,
FT ECO:0000269|PubMed:7927345, ECO:0000269|PubMed:9585602,
FT ECO:0000269|PubMed:9667376"
FT /id="VAR_002438"
FT VARIANT 342
FT /note="L -> Q (in CGDX; dbSNP:rs151344495)"
FT /evidence="ECO:0000269|PubMed:8916969"
FT /id="VAR_047273"
FT VARIANT 344
FT /note="S -> F (in CGDX; dbSNP:rs151344485)"
FT /evidence="ECO:0000269|PubMed:10914676,
FT ECO:0000269|PubMed:23910690, ECO:0000269|PubMed:9667376"
FT /id="VAR_025619"
FT VARIANT 356
FT /note="R -> P (in CGDX; dbSNP:rs151344471)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007889"
FT VARIANT 364
FT /note="G -> R (in dbSNP:rs141756032)"
FT /evidence="ECO:0000269|PubMed:10089913,
FT ECO:0000269|PubMed:12139950"
FT /id="VAR_025620"
FT VARIANT 389
FT /note="G -> A (in CGDX; dbSNP:rs137854586)"
FT /evidence="ECO:0000269|PubMed:1710153"
FT /id="VAR_002439"
FT VARIANT 389
FT /note="G -> E (in CGDX; dbSNP:rs137854586)"
FT /evidence="ECO:0000269|PubMed:10914676"
FT /id="VAR_025621"
FT VARIANT 405
FT /note="M -> R (in CGDX; dbSNP:rs151344472)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007890"
FT VARIANT 408
FT /note="G -> E (in CGDX; dbSNP:rs151344474)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007891"
FT VARIANT 408
FT /note="G -> R (in CGDX; dbSNP:rs151344473)"
FT /evidence="ECO:0000269|PubMed:18773283,
FT ECO:0000269|PubMed:9585602"
FT /id="VAR_007892"
FT VARIANT 409
FT /note="A -> G (in CGDX)"
FT /evidence="ECO:0000269|PubMed:27666509"
FT /id="VAR_078386"
FT VARIANT 412
FT /note="G -> E (in CGDX)"
FT /evidence="ECO:0000269|PubMed:23910690"
FT /id="VAR_071863"
FT VARIANT 415
FT /note="P -> H (in CGDX; dbSNP:rs137854585)"
FT /evidence="ECO:0000269|PubMed:2556453,
FT ECO:0000269|PubMed:9585602"
FT /id="VAR_002440"
FT VARIANT 415
FT /note="P -> L (in CGDX; dbSNP:rs137854585)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007893"
FT VARIANT 420
FT /note="L -> P (in CGDX; dbSNP:rs151344486)"
FT /evidence="ECO:0000269|PubMed:10914676"
FT /id="VAR_025622"
FT VARIANT 422
FT /note="S -> P (in CGDX; dbSNP:rs151344475)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007894"
FT VARIANT 453
FT /note="W -> R (in CGDX; dbSNP:rs151344476)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007895"
FT VARIANT 472
FT /note="G -> S (in dbSNP:rs13306300)"
FT /id="VAR_047274"
FT VARIANT 488
FT /note="A -> D (in CGDX)"
FT /evidence="ECO:0000269|PubMed:22125116"
FT /id="VAR_068012"
FT VARIANT 500
FT /note="D -> E (in CGDX)"
FT /evidence="ECO:0000269|PubMed:22125116"
FT /id="VAR_068013"
FT VARIANT 500
FT /note="D -> G (in CGDX; dbSNP:rs137854593)"
FT /evidence="ECO:0000269|PubMed:8182143"
FT /id="VAR_002441"
FT VARIANT 505
FT /note="L -> R (in CGDX; dbSNP:rs151344490)"
FT /evidence="ECO:0000269|PubMed:11462241"
FT /id="VAR_047275"
FT VARIANT 516
FT /note="W -> C (in CGDX; dbSNP:rs151344477)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007896"
FT VARIANT 516
FT /note="W -> R (in CGDX; dbSNP:rs151344487)"
FT /evidence="ECO:0000269|PubMed:10914676"
FT /id="VAR_025623"
FT VARIANT 517
FT /note="D -> E (in dbSNP:rs151344452)"
FT /evidence="ECO:0000269|PubMed:12139950"
FT /id="VAR_025624"
FT VARIANT 534
FT /note="V -> D (in CGDX; dbSNP:rs151344478)"
FT /evidence="ECO:0000269|PubMed:9585602"
FT /id="VAR_007897"
FT VARIANT 537
FT /note="C -> R (in CGDX; dbSNP:rs151344454)"
FT /evidence="ECO:0000269|PubMed:12139950,
FT ECO:0000269|PubMed:9585602"
FT /id="VAR_007898"
FT VARIANT 546
FT /note="L -> P (in CGDX; dbSNP:rs151344492)"
FT /evidence="ECO:0000269|PubMed:10089913"
FT /id="VAR_047276"
FT CONFLICT 14
FT /note="V -> A (in Ref. 6 and 4)"
FT /evidence="ECO:0000305"
FT HELIX 393..398
FT /evidence="ECO:0007829|PDB:3A1F"
FT STRAND 401..409
FT /evidence="ECO:0007829|PDB:3A1F"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:3A1F"
FT HELIX 413..429
FT /evidence="ECO:0007829|PDB:3A1F"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:3A1F"
FT TURN 448..451
FT /evidence="ECO:0007829|PDB:3A1F"
FT HELIX 452..467
FT /evidence="ECO:0007829|PDB:3A1F"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:3A1F"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:3A1F"
FT HELIX 516..526
FT /evidence="ECO:0007829|PDB:3A1F"
FT STRAND 531..538
FT /evidence="ECO:0007829|PDB:3A1F"
FT HELIX 540..552
FT /evidence="ECO:0007829|PDB:3A1F"
FT STRAND 562..566
FT /evidence="ECO:0007829|PDB:3A1F"
SQ SEQUENCE 570 AA; 65336 MW; 7E84051BD4000CE3 CRC64;
MGNWAVNEGL SIFVILVWLG LNVFLFVWYY RVYDIPPKFF YTRKLLGSAL ALARAPAACL
NFNCMLILLP VCRNLLSFLR GSSACCSTRV RRQLDRNLTF HKMVAWMIAL HSAIHTIAHL
FNVEWCVNAR VNNSDPYSVA LSELGDRQNE SYLNFARKRI KNPEGGLYLA VTLLAGITGV
VITLCLILII TSSTKTIRRS YFEVFWYTHH LFVIFFIGLA IHGAERIVRG QTAESLAVHN
ITVCEQKISE WGKIKECPIP QFAGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKV
VTHPFKTIEL QMKKKGFKME VGQYIFVKCP KVSKLEWHPF TLTSAPEEDF FSIHIRIVGD
WTEGLFNACG CDKQEFQDAW KLPKIAVDGP FGTASEDVFS YEVVMLVGAG IGVTPFASIL
KSVWYKYCNN ATNLKLKKIY FYWLCRDTHA FEWFADLLQL LESQMQERNN AGFLSYNIYL
TGWDESQANH FAVHHDEEKD VITGLKQKTL YGRPNWDNEF KTIASQHPNT RIGVFLCGPE
ALAETLSKQS ISNSESGPRG VHFIFNKENF
