ID CY24A_HUMAN Reviewed; 195 AA. AC P13498; Q14090; Q9BR72; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 3. DT 07-NOV-2018, entry version 190. DE RecName: Full=Cytochrome b-245 light chain; DE AltName: Full=Cytochrome b(558) alpha chain; DE AltName: Full=Cytochrome b558 subunit alpha; DE AltName: Full=Neutrophil cytochrome b 22 kDa polypeptide; DE AltName: Full=Superoxide-generating NADPH oxidase light chain subunit; DE AltName: Full=p22 phagocyte B-cytochrome; DE AltName: Full=p22-phox; DE Short=p22phox; GN Name=CYBA {ECO:0000312|HGNC:HGNC:2577}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-26, AND VARIANTS RP HIS-72 AND ALA-174. RX PubMed=3368442; DOI=10.1073/pnas.85.10.3319; RA Parkos C.A., Dinauer M.C., Walker L.E., Allen R.A., Jesaitis A.J., RA Orkin S.H.; RT "Primary structure and unique expression of the 22-kilodalton light RT chain of human neutrophil cytochrome b."; RL Proc. Natl. Acad. Sci. U.S.A. 85:3319-3323(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-174. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-174. RC TISSUE=Brain; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-123, AND VARIANT ARCGD RP ARG-118. RX PubMed=2243141; DOI=10.1172/JCI114898; RA Dinauer M.C., Pierce E.A., Bruns G.A.P., Curnutte J.T., Orkin S.H.; RT "Human neutrophil cytochrome b light chain (p22-phox). Gene structure, RT chromosomal location, and mutations in cytochrome-negative autosomal RT recessive chronic granulomatous disease."; RL J. Clin. Invest. 86:1729-1737(1990). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-195, AND VARIANTS HIS-72 AND ALA-174. RX PubMed=2469497; RA Verhoeven A.J., Bolscher B.G., Meerhof L.J., van Zwieten R., RA Keijer J., Weening R.S., Roos D.; RT "Characterization of two monoclonal antibodies against cytochrome b558 RT of human neutrophils."; RL Blood 73:1686-1694(1989). RN [7] RP INTERACTION WITH NOXO1, AND MUTAGENESIS OF PRO-157. RX PubMed=12716910; DOI=10.1074/jbc.M212856200; RA Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H., RA Sumimoto H.; RT "Novel human homologues of p47phox and p67phox participate in RT activation of superoxide-producing NADPH oxidases."; RL J. Biol. Chem. 278:25234-25246(2003). RN [8] RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY. RX PubMed=15585859; DOI=10.4049/jimmunol.173.12.7349; RA Taylor R.M., Burritt J.B., Baniulis D., Foubert T.R., Lord C.I., RA Dinauer M.C., Parkos C.A., Jesaitis A.J.; RT "Site-specific inhibitors of NADPH oxidase activity and structural RT probes of flavocytochrome b: characterization of six monoclonal RT antibodies to the p22phox subunit."; RL J. Immunol. 173:7349-7357(2004). RN [9] RP INTERACTION WITH DUOX1; DUOX2 AND TPO. RX PubMed=15561711; DOI=10.1074/jbc.M407709200; RA Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., RA Miot F.; RT "Identification of a novel partner of duox: EFP1, a thioredoxin- RT related protein."; RL J. Biol. Chem. 280:3096-3103(2005). RN [10] RP FUNCTION. RX PubMed=15824103; DOI=10.1074/jbc.M414548200; RA Ueno N., Takeya R., Miyano K., Kikuchi H., Sumimoto H.; RT "The NADPH oxidase Nox3 constitutively produces superoxide in a RT p22phox-dependent manner: its regulation by oxidase organizers and RT activators."; RL J. Biol. Chem. 280:23328-23339(2005). RN [11] RP INTERACTION WITH NOX4. RX PubMed=15927447; DOI=10.1016/j.cellsig.2005.03.023; RA Martyn K.D., Frederick L.M., von Loehneysen K., Dinauer M.C., RA Knaus U.G.; RT "Functional analysis of Nox4 reveals unique characteristics compared RT to other NADPH oxidases."; RL Cell. Signal. 18:69-82(2006). RN [12] RP PHOSPHORYLATION AT THR-147. RX PubMed=19948736; DOI=10.1074/jbc.M109.030643; RA Lewis E.M., Sergeant S., Ledford B., Stull N., Dinauer M.C., RA McPhail L.C.; RT "Phosphorylation of p22phox on threonine 147 enhances NADPH oxidase RT activity by promoting p47phox binding."; RL J. Biol. Chem. 285:2959-2967(2010). RN [13] RP SUBCELLULAR LOCATION, AND INTERACTION WITH CALPROTECTIN. RX PubMed=22808130; DOI=10.1371/journal.pone.0040277; RA Berthier S., Nguyen M.V., Baillet A., Hograindleur M.A., Paclet M.H., RA Polack B., Morel F.; RT "Molecular interface of S100A8 with cytochrome b and NADPH oxidase RT activation."; RL PLoS ONE 7:E40277-E40277(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP STRUCTURE BY NMR OF 149-167 IN COMPLEX WITH NCF1, AND INTERACTION WITH RP NCF1. RX PubMed=16326715; DOI=10.1074/jbc.M505193200; RA Ogura K., Nobuhisa I., Yuzawa S., Takeya R., Torikai S., Saikawa K., RA Sumimoto H., Inagaki F.; RT "NMR solution structure of the tandem Src homology 3 domains of RT p47phox complexed with a p22phox-derived proline-rich peptide."; RL J. Biol. Chem. 281:3660-3668(2006). RN [16] RP INVOLVEMENT IN ARCGD, AND VARIANTS ARCGD GLN-90 AND ARG-94. RX PubMed=1415254; RA de Boer M., de Klein A., Hossle J.-P., Seger R., Corbeel L., RA Weening R.S., Roos D.; RT "Cytochrome b558-negative, autosomal recessive chronic granulomatous RT disease: two new mutations in the cytochrome b558 light chain of the RT NADPH oxidase (p22-phox)."; RL Am. J. Hum. Genet. 51:1127-1135(1992). RN [17] RP VARIANT ARCGD GLN-156. RX PubMed=1763037; DOI=10.1073/pnas.88.24.11231; RA Dinauer M.C., Pierce E.A., Erickson R.W., Muhlebach T.J., Messner H., RA Orkin S.H., Seger R.A., Curnutte J.T.; RT "Point mutation in the cytoplasmic domain of the neutrophil p22-phox RT cytochrome b subunit is associated with a nonfunctional NADPH oxidase RT and chronic granulomatous disease."; RL Proc. Natl. Acad. Sci. U.S.A. 88:11231-11235(1991). RN [18] RP VARIANT ARCGD VAL-53. RX PubMed=8168815; DOI=10.1007/BF00201671; RA Hossle J.-P., de Boer M., Seger R.A., Roos D.; RT "Identification of allele-specific p22-phox mutations in a compound RT heterozygous patient with chronic granulomatous disease by mismatch RT PCR and restriction enzyme analysis."; RL Hum. Genet. 93:437-442(1994). RN [19] RP CHARACTERIZATION OF VARIANT ARCGD GLN-156. RX PubMed=7964505; DOI=10.1084/jem.180.6.2329; RA Leusen J.H., Bolscher B.G., Hilarius P.M., Weening R.S., RA Kaulfersch W., Seger R.A., Roos D., Verhoeven A.J.; RT "156Pro-->Gln substitution in the light chain of cytochrome b558 of RT the human NADPH oxidase (p22-phox) leads to defective translocation of RT the cytosolic proteins p47-phox and p67-phox."; RL J. Exp. Med. 180:2329-2334(1994). RN [20] RP VARIANTS ARCGD ARG-24; VAL-25; PRO-52; TRP-90 AND ARG-118. RX PubMed=10910929; RA Rae J., Noack D., Heyworth P.G., Ellis B.A., Curnutte J.T., RA Cross A.R.; RT "Molecular analysis of 9 new families with chronic granulomatous RT disease caused by mutations in CYBA, the gene encoding p22(phox)."; RL Blood 96:1106-1112(2000). RN [21] RP VARIANT ARCGD ARG-24. RX PubMed=10759707; DOI=10.1046/j.1365-2141.2000.01857.x; RA Yamada M., Ariga T., Kawamura N., Ohtsu M., Imajoh-Ohmi S., RA Ohshika E., Tatsuzawa O., Kobayashi K., Sakiyama Y.; RT "Genetic studies of three Japanese patients with p22-phox-deficient RT chronic granulomatous disease: detection of a possible common mutant RT CYBA allele in Japan and a genotype-phenotype correlation in these RT patients."; RL Br. J. Haematol. 108:511-517(2000). RN [22] RP VARIANTS ARCGD ARG-24 AND VAL-124. 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 RT in Japan with special reference to gp91-phox and p22-phox RT deficiency."; RL Hum. Genet. 106:473-481(2000). RN [23] RP VARIANT ARCGD THR-125. RX PubMed=18422995; DOI=10.1111/j.1365-2141.2008.07148.x; RA Teimourian S., Zomorodian E., Badalzadeh M., Pouya A., RA Kannengiesser C., Mansouri D., Cheraghi T., Parvaneh N.; RT "Characterization of six novel mutations in CYBA: the gene causing RT autosomal recessive chronic granulomatous disease."; RL Br. J. Haematol. 141:848-851(2008). RN [24] RP VARIANTS HIS-72; GLY-171; ALA-174 AND ASP-193. RX PubMed=19388116; DOI=10.1002/humu.21029; RA Bedard K., Attar H., Bonnefont J., Jaquet V., Borel C., Plastre O., RA Stasia M.-J., Antonarakis S.E., Krause K.-H.; RT "Three common polymorphisms in the CYBA gene form a haplotype RT associated with decreased ROS generation."; RL Hum. Mutat. 30:1123-1133(2009). RN [25] RP VARIANTS ARCGD ARG-24; ASP-25; VAL-124 AND THR-125. RX PubMed=23910690; DOI=10.1016/j.jaci.2013.05.039; RA Koeker M.Y., Camcioglu Y., van Leeuwen K., Kilic S.S., Barlan I., RA Yilmaz M., Metin A., de Boer M., Avcilar H., Patiroglu T., RA Yildiran A., Yegin O., 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). CC -!- FUNCTION: Critical component of the membrane-bound oxidase of CC phagocytes that generates superoxide. Associates with NOX3 to form CC a functional NADPH oxidase constitutively generating superoxide. CC {ECO:0000269|PubMed:15824103}. CC -!- SUBUNIT: Composed of a heavy chain (beta) and a light chain CC (alpha). Component of an NADPH oxidase complex composed of a CC heterodimer formed by the membrane proteins CYBA and CYBB and the CC cytosolic subunits NCF1, NCF2 and NCF4. Interacts with NCF1 (via CC SH3 domain). Interacts with SH3PXD2A (By similarity). Interacts CC with DUOX1, DUOX2 and TPO. Interacts with NOX3 and NOX4. Interacts CC with calprotectin (S100A8/9). {ECO:0000250, CC ECO:0000269|PubMed:12716910, ECO:0000269|PubMed:15561711, CC ECO:0000269|PubMed:15927447, ECO:0000269|PubMed:16326715, CC ECO:0000269|PubMed:22808130}. CC -!- INTERACTION: CC P14598:NCF1; NbExp=7; IntAct=EBI-986058, EBI-395044; CC Q8NFA2:NOXO1; NbExp=3; IntAct=EBI-986058, EBI-7130806; CC Q8NFA2-3:NOXO1; NbExp=3; IntAct=EBI-986058, EBI-20557410; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15585859, CC ECO:0000269|PubMed:22808130}. Note=As unassembled monomer may CC localize to the endoplasmic reticulum. CC {ECO:0000250|UniProtKB:Q61462}. CC -!- PTM: The heme prosthetic group could be coordinated with residues CC of the light chain, the heavy chain, or both, and it is possible CC that more than one heme is present per cytochrome b-245. CC -!- PTM: Phosphorylation at Thr-147 enhances NADPH oxidase activity by CC promoting p47phox binding. {ECO:0000250}. CC -!- PTM: Ubiquitinated at Lys-149 likely by RNF145. CC {ECO:0000250|UniProtKB:Q61462}. CC -!- DISEASE: Granulomatous disease, chronic, cytochrome-b-negative, CC autosomal recessive (ARCGD) [MIM:233690]: A disorder characterized CC by the inability of neutrophils and phagocytes to kill microbes CC that they have ingested. Patients suffer from life-threatening CC bacterial/fungal infections. {ECO:0000269|PubMed:10759707, CC ECO:0000269|PubMed:10910929, ECO:0000269|PubMed:10914676, CC ECO:0000269|PubMed:1415254, ECO:0000269|PubMed:1763037, CC ECO:0000269|PubMed:18422995, ECO:0000269|PubMed:2243141, CC ECO:0000269|PubMed:23910690, ECO:0000269|PubMed:7964505, CC ECO:0000269|PubMed:8168815}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the p22phox family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=CYBAbase; Note=CYBA mutation db; CC URL="http://structure.bmc.lu.se/idbase/CYBAbase/"; CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and CC polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=C&genename=CYBB+%40+GP91-PHOX"; 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; M21186; AAA90925.1; -; mRNA. DR EMBL; BT006861; AAP35507.1; -; mRNA. DR EMBL; AC116552; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC006465; AAH06465.1; -; mRNA. DR EMBL; AH002664; AAA52134.1; -; Genomic_DNA. DR CCDS; CCDS32504.1; -. DR PIR; A28201; A28201. DR RefSeq; NP_000092.2; NM_000101.3. DR UniGene; Hs.513803; -. DR PDB; 1WLP; NMR; -; A=149-168. DR PDBsum; 1WLP; -. DR ProteinModelPortal; P13498; -. DR SMR; P13498; -. DR BioGrid; 107915; 13. DR DIP; DIP-37650N; -. DR IntAct; P13498; 10. DR MINT; P13498; -. DR STRING; 9606.ENSP00000261623; -. DR DrugBank; DB00514; Dextromethorphan. DR TCDB; 5.B.1.1.1; the phagocyte (gp91(phox)) nadph oxidase family. DR iPTMnet; P13498; -. DR PhosphoSitePlus; P13498; -. DR BioMuta; CYBA; -. DR DMDM; 311033459; -. DR EPD; P13498; -. DR MaxQB; P13498; -. DR PaxDb; P13498; -. DR PeptideAtlas; P13498; -. DR PRIDE; P13498; -. DR ProteomicsDB; 52920; -. DR DNASU; 1535; -. DR Ensembl; ENST00000261623; ENSP00000261623; ENSG00000051523. DR GeneID; 1535; -. DR KEGG; hsa:1535; -. DR UCSC; uc002flb.5; human. DR CTD; 1535; -. DR DisGeNET; 1535; -. DR EuPathDB; HostDB:ENSG00000051523.10; -. DR GeneCards; CYBA; -. DR GeneReviews; CYBA; -. DR H-InvDB; HIX0013335; -. DR HGNC; HGNC:2577; CYBA. DR HPA; CAB009492; -. DR MalaCards; CYBA; -. DR MIM; 233690; phenotype. DR MIM; 608508; gene. DR neXtProt; NX_P13498; -. DR OpenTargets; ENSG00000051523; -. DR Orphanet; 379; Chronic granulomatous disease. DR PharmGKB; PA27075; -. DR eggNOG; ENOG410IXYN; Eukaryota. DR eggNOG; ENOG4111MI6; LUCA. DR GeneTree; ENSGT00390000002290; -. DR HOGENOM; HOG000001585; -. DR HOVERGEN; HBG051278; -. DR InParanoid; P13498; -. DR KO; K08009; -. DR OMA; KIEWAMW; -. DR PhylomeDB; P13498; -. DR TreeFam; TF328901; -. DR Reactome; R-HSA-1222556; ROS, 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 ChiTaRS; CYBA; human. DR EvolutionaryTrace; P13498; -. DR GenomeRNAi; 1535; -. DR PRO; PR:P13498; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000051523; Expressed in 205 organ(s), highest expression level in blood. DR CleanEx; HS_CYBA; -. DR ExpressionAtlas; P13498; baseline and differential. DR Genevisible; P13498; HS. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005768; C:endosome; IEA:Ensembl. DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0016020; C:membrane; HDA: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:0005634; C:nucleus; 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; TAS:Reactome. DR GO; GO:0030141; C:secretory granule; TAS:BHF-UCL. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0001725; C:stress fiber; IEA:Ensembl. DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome. DR GO; GO:0009055; F:electron transfer activity; IDA:BHF-UCL. DR GO; GO:0020037; F:heme binding; IEA:InterPro. 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:0017124; F:SH3 domain binding; IPI:BHF-UCL. DR GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; IBA:GO_Central. DR GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl. DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:1904845; P:cellular response to L-glutamine; IEA:Ensembl. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0017004; P:cytochrome complex assembly; IDA:BHF-UCL. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISS:BHF-UCL. DR GO; GO:0006954; P:inflammatory response; IMP:BHF-UCL. DR GO; GO:0045087; P:innate immune response; IMP:BHF-UCL. DR GO; GO:0003106; P:negative regulation of glomerular filtration by angiotensin; IEA:Ensembl. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0055114; P:oxidation-reduction process; IMP:BHF-UCL. DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl. DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IDA:UniProtKB. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB. DR GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl. DR GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; IEA:Ensembl. DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB. DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IDA:UniProtKB. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl. DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl. DR GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IDA:UniProtKB. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB. DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl. DR GO; GO:0045730; P:respiratory burst; IMP:BHF-UCL. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:1904044; P:response to aldosterone; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl. DR GO; GO:0014895; P:smooth muscle hypertrophy; ISS:BHF-UCL. DR GO; GO:0042554; P:superoxide anion generation; IMP:BHF-UCL. DR GO; GO:0006801; P:superoxide metabolic process; IMP:BHF-UCL. DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome. DR InterPro; IPR007732; Cyt_b558_asu. DR PANTHER; PTHR15168; PTHR15168; 1. DR Pfam; PF05038; Cytochrom_B558a; 1. DR PIRSF; PIRSF019635; Cytochr_b558a; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Chronic granulomatous disease; KW Complete proteome; Direct protein sequencing; Disease mutation; KW Electron transport; Heme; Iron; Isopeptide bond; Membrane; KW Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Polymorphism; KW Reference proteome; Transport; Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3368442}. FT CHAIN 2 195 Cytochrome b-245 light chain. FT /FTId=PRO_0000144907. FT INTRAMEM 91 127 FT COMPBIAS 133 189 Pro-rich. FT METAL 94 94 Iron (heme axial ligand). {ECO:0000255}. FT MOD_RES 147 147 Phosphothreonine. FT {ECO:0000244|PubMed:23186163, FT ECO:0000269|PubMed:19948736}. FT MOD_RES 168 168 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61462}. FT CROSSLNK 149 149 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:Q61462}. FT VARIANT 24 24 G -> R (in ARCGD; dbSNP:rs28941476). FT {ECO:0000269|PubMed:10759707, FT ECO:0000269|PubMed:10910929, FT ECO:0000269|PubMed:10914676, FT ECO:0000269|PubMed:23910690}. FT /FTId=VAR_012755. FT VARIANT 25 25 G -> D (in ARCGD). FT {ECO:0000269|PubMed:23910690}. FT /FTId=VAR_071860. FT VARIANT 25 25 G -> V (in ARCGD; dbSNP:rs179363891). FT {ECO:0000269|PubMed:10910929}. FT /FTId=VAR_060576. FT VARIANT 52 52 L -> P (in ARCGD; dbSNP:rs179363890). FT {ECO:0000269|PubMed:10910929}. FT /FTId=VAR_060577. FT VARIANT 53 53 E -> V (in ARCGD; dbSNP:rs179363893). FT {ECO:0000269|PubMed:8168815}. FT /FTId=VAR_060578. FT VARIANT 72 72 Y -> H (in dbSNP:rs4673). FT {ECO:0000269|PubMed:19388116, FT ECO:0000269|PubMed:2469497, FT ECO:0000269|PubMed:3368442}. FT /FTId=VAR_005122. FT VARIANT 90 90 R -> Q (in ARCGD; dbSNP:rs104894513). FT {ECO:0000269|PubMed:1415254}. FT /FTId=VAR_005123. FT VARIANT 90 90 R -> W (in ARCGD; dbSNP:rs179363892). FT {ECO:0000269|PubMed:10910929}. FT /FTId=VAR_060579. FT VARIANT 94 94 H -> R (in ARCGD; dbSNP:rs104894510). FT {ECO:0000269|PubMed:1415254}. FT /FTId=VAR_005124. FT VARIANT 118 118 S -> R (in ARCGD; dbSNP:rs104894514). FT {ECO:0000269|PubMed:10910929, FT ECO:0000269|PubMed:2243141}. FT /FTId=VAR_005125. FT VARIANT 124 124 A -> V (in ARCGD; dbSNP:rs179363894). FT {ECO:0000269|PubMed:10914676, FT ECO:0000269|PubMed:23910690}. FT /FTId=VAR_060580. FT VARIANT 125 125 A -> T (in ARCGD; dbSNP:rs119103269). FT {ECO:0000269|PubMed:18422995, FT ECO:0000269|PubMed:23910690}. FT /FTId=VAR_060581. FT VARIANT 156 156 P -> Q (in ARCGD; dbSNP:rs104894515). FT {ECO:0000269|PubMed:1763037, FT ECO:0000269|PubMed:7964505}. FT /FTId=VAR_005126. FT VARIANT 171 171 E -> G (in dbSNP:rs72667005). FT {ECO:0000269|PubMed:19388116}. FT /FTId=VAR_060582. FT VARIANT 174 174 V -> A (in dbSNP:rs1049254). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:19388116, FT ECO:0000269|PubMed:2469497, FT ECO:0000269|PubMed:3368442, FT ECO:0000269|Ref.2}. FT /FTId=VAR_054801. FT VARIANT 193 193 E -> D (in dbSNP:rs72667006). FT {ECO:0000269|PubMed:19388116}. FT /FTId=VAR_060583. FT MUTAGEN 157 157 P->Q: Loss of interaction with NOXO1. FT {ECO:0000269|PubMed:12716910}. FT HELIX 161 165 {ECO:0000244|PDB:1WLP}. SQ SEQUENCE 195 AA; 21013 MW; 428427AD19398240 CRC64; MGQIEWAMWA NEQALASGLI LITGGIVATA GRFTQWYFGA YSIVAGVFVC LLEYPRGKRK KGSTMERWGQ KYMTAVVKLF GPFTRNYYVR AVLHLLLSVP AGFLLATILG TACLAIASGI YLLAAVRGEQ WTPIEPKPRE RPQIGGTIKQ PPSNPPPRPP AEARKKPSEE EAAVAAGGPP GGPQVNPIPV TDEVV //