Cytochrome b-245 light chain

Details

Name
Cytochrome b-245 light chain
Synonyms
  • Cytochrome b(558) alpha chain
  • Cytochrome b558 subunit alpha
  • Neutrophil cytochrome b 22 kDa polypeptide
  • p22 phagocyte B-cytochrome
  • p22-phox
  • p22phox
  • Superoxide-generating NADPH oxidase light chain subunit
Gene Name
CYBA
Organism
Humans
Amino acid sequence
>lcl|BSEQ0021711|Cytochrome b-245 light chain
MGQIEWAMWANEQALASGLILITGGIVATAGRFTQWYFGAYSIVAGVFVCLLEYPRGKRK
KGSTMERWGQKYMTAVVKLFGPFTRNYYVRAVLHLLLSVPAGFLLATILGTACLAIASGI
YLLAAVRGEQWTPIEPKPRERPQIGGTIKQPPSNPPPRPPAEARKKPSEEEAAVAAGGPP
GGPQVNPIPVTDEVV
Number of residues
195
Molecular Weight
21012.36
Theoretical pI
Not Available
GO Classification
Functions
electron carrier activity / heme binding / metal ion binding / protein heterodimerization activity / SH3 domain binding / superoxide-generating NADPH oxidase activity
Processes
antigen processing and presentation of exogenous peptide antigen via MHC class I / antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent / antigen processing and presentation of peptide antigen via MHC class I / cellular response to amino acid stimulus / cellular response to gamma radiation / cellular response to glucose stimulus / cellular response to mechanical stimulus / cellular response to organic cyclic compound / cellular response to tumor necrosis factor / cytochrome complex assembly / hydrogen peroxide biosynthetic process / inflammatory response / innate immune response / negative regulation of glomerular filtration by angiotensin / oxidation-reduction process / phagosome maturation / positive regulation of cell growth / positive regulation of defense response to bacterium / positive regulation of endothelial cell proliferation / positive regulation of interleukin-6 production / positive regulation of mucus secretion / positive regulation of phagocytosis / positive regulation of reactive oxygen species biosynthetic process / positive regulation of smooth muscle cell proliferation / positive regulation of superoxide anion generation / positive regulation of toll-like receptor 2 signaling pathway / positive regulation of tumor necrosis factor production / regulation of release of sequestered calcium ion into cytosol / respiratory burst / response to drug / response to interleukin-1 / response to nutrient levels / small GTPase mediated signal transduction / smooth muscle hypertrophy / superoxide anion generation / superoxide metabolic process / vascular endothelial growth factor receptor signaling pathway
Components
apical plasma membrane / dendrite / endosome / Golgi apparatus / membrane / mitochondrion / NADPH oxidase complex / neuronal cell body / perinuclear endoplasmic reticulum / phagocytic vesicle membrane / plasma membrane / secretory granule
General Function
Superoxide-generating nadph oxidase activity
Specific Function
Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0021712|Cytochrome b-245 light chain (CYBA)
ATGGGGCAGATCGAGTGGGCCATGTGGGCCAACGAGCAGGCGCTGGCGTCCGGCCTGATC
CTCATCACCGGGGGCATCGTGGCCACAGCTGGGCGCTTCACCCAGTGGTACTTTGGTGCC
TACTCCATTGTGGCGGGCGTGTTTGTGTGCCTGCTGGAGTACCCCCGGGGGAAGAGGAAG
AAGGGCTCCACCATGGAGCGCTGGGGACAGAAGTACATGACCGCCGTGGTGAAGCTGTTC
GGGCCCTTTACCAGGAATTACTATGTTCGGGCCGTCCTGCATCTCCTGCTCTCGGTGCCC
GCCGGCTTCCTGCTGGCCACCATCCTTGGGACCGCCTGCCTGGCCATTGCGAGCGGCATC
TACCTACTGGCGGCTGTGCGTGGCGAGCAGTGGACGCCCATCGAGCCCAAGCCCCGGGAG
CGGCCGCAGATCGGAGGCACCATCAAGCAGCCGCCCAGCAACCCCCCGCCGCGGCCCCCG
GCCGAGGCCCGCAAGAAGCCCAGCGAGGAGGAGGCTGCGGTGGCGGCGGGGGGACCCCCG
GGAGGTCCCCAGGTCAACCCCATCCCGGTGACCGACGAGGTCGTGTGA
Chromosome Location
16
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP13498
UniProtKB Entry NameCY24A_HUMAN
HGNC IDHGNC:2577
General References
  1. Parkos CA, Dinauer MC, Walker LE, Allen RA, Jesaitis AJ, Orkin SH: Primary structure and unique expression of the 22-kilodalton light chain of human neutrophil cytochrome b. Proc Natl Acad Sci U S A. 1988 May;85(10):3319-23. [Article]
  2. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [Article]
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  4. Dinauer MC, Pierce EA, Bruns GA, Curnutte JT, Orkin SH: Human neutrophil cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease. J Clin Invest. 1990 Nov;86(5):1729-37. [Article]
  5. Verhoeven AJ, Bolscher BG, Meerhof LJ, van Zwieten R, Keijer J, Weening RS, Roos D: Characterization of two monoclonal antibodies against cytochrome b558 of human neutrophils. Blood. 1989 May 1;73(6):1686-94. [Article]
  6. Takeya R, Ueno N, Kami K, Taura M, Kohjima M, Izaki T, Nunoi H, Sumimoto H: Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. J Biol Chem. 2003 Jul 4;278(27):25234-46. Epub 2003 Apr 25. [Article]
  7. Taylor RM, Burritt JB, Baniulis D, Foubert TR, Lord CI, Dinauer MC, Parkos CA, Jesaitis AJ: Site-specific inhibitors of NADPH oxidase activity and structural probes of flavocytochrome b: characterization of six monoclonal antibodies to the p22phox subunit. J Immunol. 2004 Dec 15;173(12):7349-57. [Article]
  8. Wang D, De Deken X, Milenkovic M, Song Y, Pirson I, Dumont JE, Miot F: Identification of a novel partner of duox: EFP1, a thioredoxin-related protein. J Biol Chem. 2005 Jan 28;280(4):3096-103. Epub 2004 Nov 22. [Article]
  9. Ueno N, Takeya R, Miyano K, Kikuchi H, Sumimoto H: The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators. J Biol Chem. 2005 Jun 17;280(24):23328-39. Epub 2005 Apr 11. [Article]
  10. Martyn KD, Frederick LM, von Loehneysen K, Dinauer MC, Knaus UG: Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases. Cell Signal. 2006 Jan;18(1):69-82. Epub 2005 May 31. [Article]
  11. Lewis EM, Sergeant S, Ledford B, Stull N, Dinauer MC, McPhail LC: Phosphorylation of p22phox on threonine 147 enhances NADPH oxidase activity by promoting p47phox binding. J Biol Chem. 2010 Jan 29;285(5):2959-67. doi: 10.1074/jbc.M109.030643. Epub 2009 Nov 30. [Article]
  12. Berthier S, Nguyen MV, Baillet A, Hograindleur MA, Paclet MH, Polack B, Morel F: Molecular interface of S100A8 with cytochrome b558 and NADPH oxidase activation. PLoS One. 2012;7(7):e40277. doi: 10.1371/journal.pone.0040277. Epub 2012 Jul 10. [Article]
  13. Ogura K, Nobuhisa I, Yuzawa S, Takeya R, Torikai S, Saikawa K, Sumimoto H, Inagaki F: NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide. J Biol Chem. 2006 Feb 10;281(6):3660-8. Epub 2005 Dec 2. [Article]
  14. de Boer M, de Klein A, Hossle JP, Seger R, Corbeel L, Weening RS, Roos D: Cytochrome b558-negative, autosomal recessive chronic granulomatous disease: two new mutations in the cytochrome b558 light chain of the NADPH oxidase (p22-phox). Am J Hum Genet. 1992 Nov;51(5):1127-35. [Article]
  15. Dinauer MC, Pierce EA, Erickson RW, Muhlebach TJ, Messner H, Orkin SH, Seger RA, Curnutte JT: Point mutation in the cytoplasmic domain of the neutrophil p22-phox cytochrome b subunit is associated with a nonfunctional NADPH oxidase and chronic granulomatous disease. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11231-5. [Article]
  16. Hossle JP, de Boer M, Seger RA, Roos D: Identification of allele-specific p22-phox mutations in a compound heterozygous patient with chronic granulomatous disease by mismatch PCR and restriction enzyme analysis. Hum Genet. 1994 Apr;93(4):437-42. [Article]
  17. Leusen JH, Bolscher BG, Hilarius PM, Weening RS, Kaulfersch W, Seger RA, Roos D, Verhoeven AJ: 156Pro-->Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox. J Exp Med. 1994 Dec 1;180(6):2329-34. [Article]
  18. Rae J, Noack D, Heyworth PG, Ellis BA, Curnutte JT, Cross AR: Molecular analysis of 9 new families with chronic granulomatous disease caused by mutations in CYBA, the gene encoding p22(phox). Blood. 2000 Aug 1;96(3):1106-12. [Article]
  19. Yamada M, Ariga T, Kawamura N, Ohtsu M, Imajoh-Ohmi S, Ohshika E, Tatsuzawa O, Kobayashi K, Sakiyama Y: Genetic studies of three Japanese patients with p22-phox-deficient chronic granulomatous disease: detection of a possible common mutant CYBA allele in Japan and a genotype-phenotype correlation in these patients. Br J Haematol. 2000 Mar;108(3):511-7. [Article]
  20. Ishibashi F, Nunoi H, Endo F, Matsuda I, Kanegasaki S: Statistical and mutational analysis of chronic granulomatous disease in Japan with special reference to gp91-phox and p22-phox deficiency. Hum Genet. 2000 May;106(5):473-81. [Article]
  21. Teimourian S, Zomorodian E, Badalzadeh M, Pouya A, Kannengiesser C, Mansouri D, Cheraghi T, Parvaneh N: Characterization of six novel mutations in CYBA: the gene causing autosomal recessive chronic granulomatous disease. Br J Haematol. 2008 Jun;141(6):848-51. doi: 10.1111/j.1365-2141.2008.07148.x. Epub 2008 Apr 18. [Article]
  22. Bedard K, Attar H, Bonnefont J, Jaquet V, Borel C, Plastre O, Stasia MJ, Antonarakis SE, Krause KH: Three common polymorphisms in the CYBA gene form a haplotype associated with decreased ROS generation. Hum Mutat. 2009 Jul;30(7):1123-33. doi: 10.1002/humu.21029. [Article]
  23. Koker MY, Camcioglu Y, van Leeuwen K, Kilic SS, Barlan I, Yilmaz M, Metin A, de Boer M, Avcilar H, Patiroglu T, Yildiran A, Yegin O, Tezcan I, Sanal O, Roos D: Clinical, functional, and genetic characterization of chronic granulomatous disease in 89 Turkish patients. J Allergy Clin Immunol. 2013 Nov;132(5):1156-1163.e5. doi: 10.1016/j.jaci.2013.05.039. Epub 2013 Jul 31. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00514DextromethorphanapprovedunknowninhibitorDetails