CY24A_HUMAN
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 03-AUG-2022, entry version 212.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-26, AND VARIANTS HIS-72
RP 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 chain
RT 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 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., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., 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., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-123, AND VARIANT CGD4 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., Keijer J.,
RA Weening R.S., Roos D.;
RT "Characterization of two monoclonal antibodies against cytochrome b558 of
RT 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 activation of
RT 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 probes
RT of flavocytochrome b: characterization of six monoclonal antibodies to the
RT 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-related
RT 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 p22phox-
RT dependent manner: its regulation by oxidase organizers and 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., Knaus U.G.;
RT "Functional analysis of Nox4 reveals unique characteristics compared to
RT 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., 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 BY
RP 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 p47phox
RT complexed with a p22phox-derived proline-rich peptide.";
RL J. Biol. Chem. 281:3660-3668(2006).
RN [16]
RP INVOLVEMENT IN CGD4, AND VARIANTS CGD4 GLN-90 AND ARG-94.
RX PubMed=1415254;
RA de Boer M., de Klein A., Hossle J.-P., Seger R., Corbeel L., Weening R.S.,
RA Roos D.;
RT "Cytochrome b558-negative, autosomal recessive chronic granulomatous
RT disease: two new mutations in the cytochrome b558 light chain of the NADPH
RT oxidase (p22-phox).";
RL Am. J. Hum. Genet. 51:1127-1135(1992).
RN [17]
RP VARIANT CGD4 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 and
RT chronic granulomatous disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11231-11235(1991).
RN [18]
RP VARIANT CGD4 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 PCR and
RT restriction enzyme analysis.";
RL Hum. Genet. 93:437-442(1994).
RN [19]
RP CHARACTERIZATION OF VARIANT CGD4 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., Kaulfersch W.,
RA Seger R.A., Roos D., Verhoeven A.J.;
RT "156Pro-->Gln substitution in the light chain of cytochrome b558 of the
RT human NADPH oxidase (p22-phox) leads to defective translocation of the
RT cytosolic proteins p47-phox and p67-phox.";
RL J. Exp. Med. 180:2329-2334(1994).
RN [20]
RP VARIANTS CGD4 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., Cross A.R.;
RT "Molecular analysis of 9 new families with chronic granulomatous disease
RT caused by mutations in CYBA, the gene encoding p22(phox).";
RL Blood 96:1106-1112(2000).
RN [21]
RP VARIANT CGD4 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., Ohshika E.,
RA Tatsuzawa O., Kobayashi K., Sakiyama Y.;
RT "Genetic studies of three Japanese patients with p22-phox-deficient chronic
RT granulomatous disease: detection of a possible common mutant CYBA allele in
RT Japan and a genotype-phenotype correlation in these patients.";
RL Br. J. Haematol. 108:511-517(2000).
RN [22]
RP VARIANTS CGD4 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 in
RT Japan with special reference to gp91-phox and p22-phox deficiency.";
RL Hum. Genet. 106:473-481(2000).
RN [23]
RP VARIANT CGD4 THR-125.
RX PubMed=18422995; DOI=10.1111/j.1365-2141.2008.07148.x;
RA Teimourian S., Zomorodian E., Badalzadeh M., Pouya A., Kannengiesser C.,
RA 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 associated
RT with decreased ROS generation.";
RL Hum. Mutat. 30:1123-1133(2009).
RN [25]
RP VARIANTS CGD4 ARG-24; ASP-25; VAL-124 AND THR-125.
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).
CC -!- FUNCTION: Critical component of the membrane-bound oxidase of
CC phagocytes that generates superoxide. Associates with NOX3 to form a
CC functional NADPH oxidase constitutively generating superoxide.
CC {ECO:0000269|PubMed:15824103}.
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 (via SH3 domain). Interacts with
CC SH3PXD2A (By similarity). Interacts with DUOX1, DUOX2 and TPO.
CC Interacts with NOX3 and NOX4. Interacts with calprotectin (S100A8/9)
CC (PubMed:22808130). Interacts with GBP7 (By similarity).
CC {ECO:0000250|UniProtKB:Q61462, ECO:0000269|PubMed:12716910,
CC ECO:0000269|PubMed:15561711, ECO:0000269|PubMed:15927447,
CC ECO:0000269|PubMed:16326715, ECO:0000269|PubMed:22808130}.
CC -!- INTERACTION:
CC P13498; P14598: NCF1; NbExp=7; IntAct=EBI-986058, EBI-395044;
CC P13498; Q8NFA2: NOXO1; NbExp=3; IntAct=EBI-986058, EBI-7130806;
CC P13498; 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 localize
CC to the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q61462}.
CC -!- PTM: The heme prosthetic group could be coordinated with residues of
CC the light chain, the heavy chain, or both, and it is possible that more
CC 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, autosomal recessive, 4 (CGD4)
CC [MIM:233690]: A form of chronic granulomatous disease, a primary
CC immunodeficiency characterized by severe recurrent bacterial and fungal
CC infections, along with manifestations of chronic granulomatous
CC inflammation. It results from an impaired ability of phagocytes to
CC mount a burst of reactive oxygen species in response to pathogens.
CC {ECO:0000269|PubMed:10759707, ECO:0000269|PubMed:10910929,
CC ECO:0000269|PubMed:10914676, ECO:0000269|PubMed:1415254,
CC ECO:0000269|PubMed:1763037, ECO:0000269|PubMed:18422995,
CC ECO:0000269|PubMed:2243141, ECO:0000269|PubMed:23910690,
CC ECO:0000269|PubMed:7964505, ECO:0000269|PubMed:8168815}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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/";
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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 PDB; 1WLP; NMR; -; A=149-168.
DR PDB; 7YXW; X-ray; 2.50 A; D=151-168.
DR PDBsum; 1WLP; -.
DR PDBsum; 7YXW; -.
DR AlphaFoldDB; P13498; -.
DR SMR; P13498; -.
DR BioGRID; 107915; 74.
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-37650N; -.
DR IntAct; P13498; 12.
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 jPOST; P13498; -.
DR MassIVE; P13498; -.
DR MaxQB; P13498; -.
DR PaxDb; P13498; -.
DR PeptideAtlas; P13498; -.
DR PRIDE; P13498; -.
DR ProteomicsDB; 52920; -.
DR ABCD; P13498; 2 sequenced antibodies.
DR Antibodypedia; 4009; 277 antibodies from 27 providers.
DR DNASU; 1535; -.
DR Ensembl; ENST00000261623.8; ENSP00000261623.3; ENSG00000051523.11.
DR GeneID; 1535; -.
DR KEGG; hsa:1535; -.
DR MANE-Select; ENST00000261623.8; ENSP00000261623.3; NM_000101.4; NP_000092.2.
DR UCSC; uc002flb.5; human.
DR CTD; 1535; -.
DR DisGeNET; 1535; -.
DR GeneCards; CYBA; -.
DR GeneReviews; CYBA; -.
DR HGNC; HGNC:2577; CYBA.
DR HPA; ENSG00000051523; Tissue enhanced (bone marrow, lymphoid tissue).
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 VEuPathDB; HostDB:ENSG00000051523; -.
DR eggNOG; ENOG502QVK1; Eukaryota.
DR GeneTree; ENSGT00390000002290; -.
DR HOGENOM; CLU_125024_0_0_1; -.
DR InParanoid; P13498; -.
DR OMA; AYDNPIS; -.
DR PhylomeDB; P13498; -.
DR TreeFam; TF328901; -.
DR PathwayCommons; P13498; -.
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 Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping.
DR SignaLink; P13498; -.
DR SIGNOR; P13498; -.
DR BioGRID-ORCS; 1535; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; CYBA; human.
DR EvolutionaryTrace; P13498; -.
DR GenomeRNAi; 1535; -.
DR Pharos; P13498; Tbio.
DR PRO; PR:P13498; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P13498; protein.
DR Bgee; ENSG00000051523; Expressed in granulocyte and 181 other tissues.
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 NAD(P)H oxidase activity; IEA:Ensembl.
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:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0017004; P:cytochrome complex assembly; IDA:BHF-UCL.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
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:0070254; P:mucus secretion; IEA:Ensembl.
DR GO; GO:0003106; P:negative regulation of glomerular filtration by angiotensin; IEA:Ensembl.
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:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; 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 IDEAL; IID00596; -.
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 Direct protein sequencing; Disease variant; Electron transport; Heme; Iron;
KW Isopeptide bond; Membrane; Metal-binding; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3368442"
FT CHAIN 2..195
FT /note="Cytochrome b-245 light chain"
FT /id="PRO_0000144907"
FT INTRAMEM 91..127
FT REGION 134..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
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:0000255"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19948736,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61462"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61462"
FT VARIANT 24
FT /note="G -> R (in CGD4; dbSNP:rs28941476)"
FT /evidence="ECO:0000269|PubMed:10759707,
FT ECO:0000269|PubMed:10910929, ECO:0000269|PubMed:10914676,
FT ECO:0000269|PubMed:23910690"
FT /id="VAR_012755"
FT VARIANT 25
FT /note="G -> D (in CGD4; dbSNP:rs179363891)"
FT /evidence="ECO:0000269|PubMed:23910690"
FT /id="VAR_071860"
FT VARIANT 25
FT /note="G -> V (in CGD4; dbSNP:rs179363891)"
FT /evidence="ECO:0000269|PubMed:10910929"
FT /id="VAR_060576"
FT VARIANT 52
FT /note="L -> P (in CGD4; dbSNP:rs179363890)"
FT /evidence="ECO:0000269|PubMed:10910929"
FT /id="VAR_060577"
FT VARIANT 53
FT /note="E -> V (in CGD4; dbSNP:rs179363893)"
FT /evidence="ECO:0000269|PubMed:8168815"
FT /id="VAR_060578"
FT VARIANT 72
FT /note="Y -> H (in dbSNP:rs4673)"
FT /evidence="ECO:0000269|PubMed:19388116,
FT ECO:0000269|PubMed:2469497, ECO:0000269|PubMed:3368442"
FT /id="VAR_005122"
FT VARIANT 90
FT /note="R -> Q (in CGD4; dbSNP:rs104894513)"
FT /evidence="ECO:0000269|PubMed:1415254"
FT /id="VAR_005123"
FT VARIANT 90
FT /note="R -> W (in CGD4; dbSNP:rs179363892)"
FT /evidence="ECO:0000269|PubMed:10910929"
FT /id="VAR_060579"
FT VARIANT 94
FT /note="H -> R (in CGD4; dbSNP:rs104894510)"
FT /evidence="ECO:0000269|PubMed:1415254"
FT /id="VAR_005124"
FT VARIANT 118
FT /note="S -> R (in CGD4; dbSNP:rs104894514)"
FT /evidence="ECO:0000269|PubMed:10910929,
FT ECO:0000269|PubMed:2243141"
FT /id="VAR_005125"
FT VARIANT 124
FT /note="A -> V (in CGD4; dbSNP:rs179363894)"
FT /evidence="ECO:0000269|PubMed:10914676,
FT ECO:0000269|PubMed:23910690"
FT /id="VAR_060580"
FT VARIANT 125
FT /note="A -> T (in CGD4; dbSNP:rs119103269)"
FT /evidence="ECO:0000269|PubMed:18422995,
FT ECO:0000269|PubMed:23910690"
FT /id="VAR_060581"
FT VARIANT 156
FT /note="P -> Q (in CGD4; dbSNP:rs104894515)"
FT /evidence="ECO:0000269|PubMed:1763037,
FT ECO:0000269|PubMed:7964505"
FT /id="VAR_005126"
FT VARIANT 171
FT /note="E -> G (in dbSNP:rs72667005)"
FT /evidence="ECO:0000269|PubMed:19388116"
FT /id="VAR_060582"
FT VARIANT 174
FT /note="V -> A (in dbSNP:rs1049254)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:19388116, ECO:0000269|PubMed:2469497,
FT ECO:0000269|PubMed:3368442, ECO:0000269|Ref.2"
FT /id="VAR_054801"
FT VARIANT 193
FT /note="E -> D (in dbSNP:rs72667006)"
FT /evidence="ECO:0000269|PubMed:19388116"
FT /id="VAR_060583"
FT MUTAGEN 157
FT /note="P->Q: Loss of interaction with NOXO1."
FT /evidence="ECO:0000269|PubMed:12716910"
FT HELIX 161..165
FT /evidence="ECO:0007829|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
