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 29-SEP-2021, entry version 226. 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 CGD 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 CGD, AND VARIANT CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 CGD 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 {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 (CGD) [MIM:306400]: A CC 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; P04839; -. DR BioGRID; 107916; 13. 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; 511 antibodies. DR DNASU; 1536; -. DR Ensembl; ENST00000378588; ENSP00000367851; ENSG00000165168. DR GeneID; 1536; -. DR KEGG; hsa:1536; -. 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 (blood, lung, 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; GHVMLLC; -. 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 SIGNOR; P04839; -. DR BioGRID-ORCS; 1536; 3 hits in 641 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 214 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: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:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; 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 NP_BIND 338..344 FT /note="FAD" FT /evidence="ECO:0000255" FT METAL 101 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000305" FT METAL 115 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000305" FT METAL 209 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000305" FT METAL 222 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000305" 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 CGD)" FT /id="VAR_047264" FT VARIANT 20 FT /note="G -> R (in CGD; dbSNP:rs151344455)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007873" FT VARIANT 41 FT /note="Y -> D (in CGD; dbSNP:rs151344453)" FT /evidence="ECO:0000269|PubMed:12139950" FT /id="VAR_025613" FT VARIANT 54..55 FT /note="Missing (in CGD)" FT /evidence="ECO:0000269|PubMed:11462241" FT /id="VAR_047265" FT VARIANT 54 FT /note="R -> M (in CGD; 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 CGD; dbSNP:rs151344456)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007874" FT VARIANT 55 FT /note="A -> D (in CGD; 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 CGD; 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 CGD; dbSNP:rs151344457)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007875" FT VARIANT 59 FT /note="C -> W (in CGD; dbSNP:rs151344488)" FT /evidence="ECO:0000269|PubMed:11462241" FT /id="VAR_047266" FT VARIANT 101 FT /note="H -> R (in CGD; dbSNP:rs137854591)" FT /evidence="ECO:0000269|PubMed:1710153" FT /id="VAR_002432" FT VARIANT 101 FT /note="H -> Y (in CGD; 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 CGD; dbSNP:rs151344458)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007877" FT VARIANT 156 FT /note="A -> T (in CGD; 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 CGD; dbSNP:rs151344491)" FT /evidence="ECO:0000269|PubMed:9794433" FT /id="VAR_047267" FT VARIANT 193 FT /note="S -> F (in CGD; dbSNP:rs151344493)" FT /evidence="ECO:0000269|PubMed:10089913" FT /id="VAR_047268" FT VARIANT 205 FT /note="F -> I (in CGD; dbSNP:rs151344496)" FT /evidence="ECO:0000269|PubMed:8916969" FT /id="VAR_047269" FT VARIANT 209 FT /note="H -> Q (in CGD; dbSNP:rs151344459)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007878" FT VARIANT 209 FT /note="H -> R (in CGD; dbSNP:rs151344482)" FT /evidence="ECO:0000269|PubMed:10914676" FT /id="VAR_025616" FT VARIANT 209 FT /note="H -> Y (in CGD; dbSNP:rs137854587)" FT /evidence="ECO:0000269|PubMed:1710153" FT /id="VAR_002434" FT VARIANT 215 FT /note="Missing (in CGD)" FT /evidence="ECO:0000269|PubMed:8916969, FT ECO:0000269|PubMed:9111587" FT /id="VAR_007879" FT VARIANT 222 FT /note="H -> N (in CGD; dbSNP:rs151344460)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007880" FT VARIANT 222 FT /note="H -> R (in CGD; 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 CGD; dbSNP:rs151344460)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007882" FT VARIANT 223 FT /note="G -> L (in CGD; requires 2 nucleotide substitutions; FT dbSNP:rs151344463 and dbSNP:rs151344464)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007883" FT VARIANT 224 FT /note="A -> G (in CGD; dbSNP:rs151344483)" FT /evidence="ECO:0000269|PubMed:10914676" FT /id="VAR_025617" FT VARIANT 225 FT /note="E -> V (in CGD; 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 CGD; dbSNP:rs151344465)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007884" FT VARIANT 244 FT /note="C -> S (in CGD; dbSNP:rs137854589)" FT /evidence="ECO:0000269|PubMed:1710153" FT /id="VAR_002436" FT VARIANT 244 FT /note="C -> Y (in CGD; dbSNP:rs137854589)" FT /evidence="ECO:0000269|PubMed:9888386" FT /id="VAR_002437" FT VARIANT 298..302 FT /note="Missing (in CGD)" FT /evidence="ECO:0000269|PubMed:9794433" FT /id="VAR_047270" FT VARIANT 299 FT /note="K -> N (in CGD)" FT /evidence="ECO:0000269|PubMed:23910690" FT /id="VAR_071861" FT VARIANT 303 FT /note="H -> N (in CGD; 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 CGD; reduces NADPH oxidase activity to 4% FT 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 CGD; dbSNP:rs151344489)" FT /evidence="ECO:0000269|PubMed:11462241" FT /id="VAR_047271" FT VARIANT 309 FT /note="E -> K (in CGD; dbSNP:rs151344466)" FT /evidence="ECO:0000269|PubMed:10914676, FT ECO:0000269|PubMed:9585602" FT /id="VAR_007885" FT VARIANT 315 FT /note="Missing (in CGD)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_047272" FT VARIANT 322 FT /note="G -> E (in CGD; dbSNP:rs151344467)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007886" FT VARIANT 325 FT /note="I -> F (in CGD; dbSNP:rs151344468)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007887" FT VARIANT 333 FT /note="S -> P (in CGD; dbSNP:rs151344469)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007888" FT VARIANT 338 FT /note="H -> D (in CGD)" FT /evidence="ECO:0000269|PubMed:23910690" FT /id="VAR_071862" FT VARIANT 338 FT /note="H -> Y (in CGD; 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 CGD; 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 CGD; dbSNP:rs151344495)" FT /evidence="ECO:0000269|PubMed:8916969" FT /id="VAR_047273" FT VARIANT 344 FT /note="S -> F (in CGD; 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 CGD; 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 CGD; dbSNP:rs137854586)" FT /evidence="ECO:0000269|PubMed:1710153" FT /id="VAR_002439" FT VARIANT 389 FT /note="G -> E (in CGD; dbSNP:rs137854586)" FT /evidence="ECO:0000269|PubMed:10914676" FT /id="VAR_025621" FT VARIANT 405 FT /note="M -> R (in CGD; dbSNP:rs151344472)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007890" FT VARIANT 408 FT /note="G -> E (in CGD; dbSNP:rs151344474)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007891" FT VARIANT 408 FT /note="G -> R (in CGD; 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 CGD)" FT /evidence="ECO:0000269|PubMed:27666509" FT /id="VAR_078386" FT VARIANT 412 FT /note="G -> E (in CGD)" FT /evidence="ECO:0000269|PubMed:23910690" FT /id="VAR_071863" FT VARIANT 415 FT /note="P -> H (in CGD; 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 CGD; dbSNP:rs137854585)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007893" FT VARIANT 420 FT /note="L -> P (in CGD; dbSNP:rs151344486)" FT /evidence="ECO:0000269|PubMed:10914676" FT /id="VAR_025622" FT VARIANT 422 FT /note="S -> P (in CGD; dbSNP:rs151344475)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007894" FT VARIANT 453 FT /note="W -> R (in CGD; 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 CGD)" FT /evidence="ECO:0000269|PubMed:22125116" FT /id="VAR_068012" FT VARIANT 500 FT /note="D -> E (in CGD)" FT /evidence="ECO:0000269|PubMed:22125116" FT /id="VAR_068013" FT VARIANT 500 FT /note="D -> G (in CGD; dbSNP:rs137854593)" FT /evidence="ECO:0000269|PubMed:8182143" FT /id="VAR_002441" FT VARIANT 505 FT /note="L -> R (in CGD; dbSNP:rs151344490)" FT /evidence="ECO:0000269|PubMed:11462241" FT /id="VAR_047275" FT VARIANT 516 FT /note="W -> C (in CGD; dbSNP:rs151344477)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007896" FT VARIANT 516 FT /note="W -> R (in CGD; 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 CGD; dbSNP:rs151344478)" FT /evidence="ECO:0000269|PubMed:9585602" FT /id="VAR_007897" FT VARIANT 537 FT /note="C -> R (in CGD; 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 CGD; 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 //