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Cytochrome b-245 light chain (Cytochrome b(558) alpha chain) (Cytochrome b558 subunit alpha) (Neutrophil cytochrome b 22 kDa polypeptide) (Superoxide-generating NADPH oxidase light chain subunit) (p22 phagocyte B-cytochrome) (p22-phox) (p22phox)

 CY24A_HUMAN             Reviewed;         195 AA.
P13498; Q14090; Q9BR72;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
27-SEP-2017, entry version 180.
RecName: Full=Cytochrome b-245 light chain;
AltName: Full=Cytochrome b(558) alpha chain;
AltName: Full=Cytochrome b558 subunit alpha;
AltName: Full=Neutrophil cytochrome b 22 kDa polypeptide;
AltName: Full=Superoxide-generating NADPH oxidase light chain subunit;
AltName: Full=p22 phagocyte B-cytochrome;
AltName: Full=p22-phox;
Short=p22phox;
Name=CYBA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-26, AND VARIANTS
HIS-72 AND ALA-174.
PubMed=3368442; DOI=10.1073/pnas.85.10.3319;
Parkos C.A., Dinauer M.C., Walker L.E., Allen R.A., Jesaitis A.J.,
Orkin S.H.;
"Primary structure and unique expression of the 22-kilodalton light
chain of human neutrophil cytochrome b.";
Proc. Natl. Acad. Sci. U.S.A. 85:3319-3323(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-174.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-174.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-123, AND VARIANT ARCGD
ARG-118.
PubMed=2243141; DOI=10.1172/JCI114898;
Dinauer M.C., Pierce E.A., Bruns G.A.P., Curnutte J.T., Orkin S.H.;
"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. 86:1729-1737(1990).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 51-195, AND VARIANTS HIS-72 AND ALA-174.
PubMed=2469497;
Verhoeven A.J., Bolscher B.G., Meerhof L.J., van Zwieten R.,
Keijer J., Weening R.S., Roos D.;
"Characterization of two monoclonal antibodies against cytochrome b558
of human neutrophils.";
Blood 73:1686-1694(1989).
[7]
INTERACTION WITH NOXO1, AND MUTAGENESIS OF PRO-157.
PubMed=12716910; DOI=10.1074/jbc.M212856200;
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. 278:25234-25246(2003).
[8]
SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
PubMed=15585859; DOI=10.4049/jimmunol.173.12.7349;
Taylor R.M., Burritt J.B., Baniulis D., Foubert T.R., Lord C.I.,
Dinauer M.C., Parkos C.A., Jesaitis A.J.;
"Site-specific inhibitors of NADPH oxidase activity and structural
probes of flavocytochrome b: characterization of six monoclonal
antibodies to the p22phox subunit.";
J. Immunol. 173:7349-7357(2004).
[9]
INTERACTION WITH DUOX1; DUOX2 AND TPO.
PubMed=15561711; DOI=10.1074/jbc.M407709200;
Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E.,
Miot F.;
"Identification of a novel partner of duox: EFP1, a thioredoxin-
related protein.";
J. Biol. Chem. 280:3096-3103(2005).
[10]
FUNCTION.
PubMed=15824103; DOI=10.1074/jbc.M414548200;
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. 280:23328-23339(2005).
[11]
INTERACTION WITH NOX4.
PubMed=15927447; DOI=10.1016/j.cellsig.2005.03.023;
Martyn K.D., Frederick L.M., von Loehneysen K., Dinauer M.C.,
Knaus U.G.;
"Functional analysis of Nox4 reveals unique characteristics compared
to other NADPH oxidases.";
Cell. Signal. 18:69-82(2006).
[12]
PHOSPHORYLATION AT THR-147.
PubMed=19948736; DOI=10.1074/jbc.M109.030643;
Lewis E.M., Sergeant S., Ledford B., Stull N., Dinauer M.C.,
McPhail L.C.;
"Phosphorylation of p22phox on threonine 147 enhances NADPH oxidase
activity by promoting p47phox binding.";
J. Biol. Chem. 285:2959-2967(2010).
[13]
SUBCELLULAR LOCATION, AND INTERACTION WITH CALPROTECTIN.
PubMed=22808130; DOI=10.1371/journal.pone.0040277;
Berthier S., Nguyen M.V., Baillet A., Hograindleur M.A., Paclet M.H.,
Polack B., Morel F.;
"Molecular interface of S100A8 with cytochrome b and NADPH oxidase
activation.";
PLoS ONE 7:E40277-E40277(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
STRUCTURE BY NMR OF 149-167 IN COMPLEX WITH NCF1, AND INTERACTION WITH
NCF1.
PubMed=16326715; DOI=10.1074/jbc.M505193200;
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. 281:3660-3668(2006).
[16]
INVOLVEMENT IN ARCGD, AND VARIANTS ARCGD GLN-90 AND ARG-94.
PubMed=1415254;
de Boer M., de Klein A., Hossle J.-P., Seger R., Corbeel L.,
Weening R.S., 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. 51:1127-1135(1992).
[17]
VARIANT ARCGD GLN-156.
PubMed=1763037; DOI=10.1073/pnas.88.24.11231;
Dinauer M.C., Pierce E.A., Erickson R.W., Muhlebach T.J., Messner H.,
Orkin S.H., Seger R.A., Curnutte J.T.;
"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. 88:11231-11235(1991).
[18]
VARIANT ARCGD VAL-53.
PubMed=8168815; DOI=10.1007/BF00201671;
Hossle J.-P., de Boer M., Seger R.A., 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. 93:437-442(1994).
[19]
CHARACTERIZATION OF VARIANT ARCGD GLN-156.
PubMed=7964505; DOI=10.1084/jem.180.6.2329;
Leusen J.H., Bolscher B.G., Hilarius P.M., Weening R.S.,
Kaulfersch W., Seger R.A., Roos D., Verhoeven A.J.;
"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. 180:2329-2334(1994).
[20]
VARIANTS ARCGD ARG-24; VAL-25; PRO-52; TRP-90 AND ARG-118.
PubMed=10910929;
Rae J., Noack D., Heyworth P.G., Ellis B.A., Curnutte J.T.,
Cross A.R.;
"Molecular analysis of 9 new families with chronic granulomatous
disease caused by mutations in CYBA, the gene encoding p22(phox).";
Blood 96:1106-1112(2000).
[21]
VARIANT ARCGD ARG-24.
PubMed=10759707; DOI=10.1046/j.1365-2141.2000.01857.x;
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. 108:511-517(2000).
[22]
VARIANTS ARCGD ARG-24 AND VAL-124.
PubMed=10914676; DOI=10.1007/s004390000288;
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. 106:473-481(2000).
[23]
VARIANT ARCGD THR-125.
PubMed=18422995; DOI=10.1111/j.1365-2141.2008.07148.x;
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. 141:848-851(2008).
[24]
VARIANTS HIS-72; GLY-171; ALA-174 AND ASP-193.
PubMed=19388116; DOI=10.1002/humu.21029;
Bedard K., Attar H., Bonnefont J., Jaquet V., Borel C., Plastre O.,
Stasia M.-J., Antonarakis S.E., Krause K.-H.;
"Three common polymorphisms in the CYBA gene form a haplotype
associated with decreased ROS generation.";
Hum. Mutat. 30:1123-1133(2009).
[25]
VARIANTS ARCGD ARG-24; ASP-25; VAL-124 AND THR-125.
PubMed=23910690; DOI=10.1016/j.jaci.2013.05.039;
Koeker M.Y., Camcioglu Y., van Leeuwen K., Kilic S.S., 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. 132:1156-1163(2013).
-!- 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.
{ECO:0000269|PubMed:15824103}.
-!- SUBUNIT: Composed of a heavy chain (beta) and a light chain
(alpha). Component of an NADPH oxidase complex composed of a
heterodimer formed by the membrane proteins CYBA and CYBB and the
cytosolic subunits NCF1, NCF2 and NCF4. Interacts with NCF1 (via
SH3 domain). Interacts with SH3PXD2A (By similarity). Interacts
with DUOX1, DUOX2 and TPO. Interacts with NOX3 and NOX4. Interacts
with calprotectin (S100A8/9). {ECO:0000250,
ECO:0000269|PubMed:12716910, ECO:0000269|PubMed:15561711,
ECO:0000269|PubMed:15927447, ECO:0000269|PubMed:16326715,
ECO:0000269|PubMed:22808130}.
-!- INTERACTION:
P14598:NCF1; NbExp=7; IntAct=EBI-986058, EBI-395044;
Q8NFA2:NOXO1; NbExp=6; IntAct=EBI-986058, EBI-7130806;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15585859,
ECO:0000269|PubMed:22808130}.
-!- PTM: The heme prosthetic group could be coordinated with residues
of the light chain, the heavy chain, or both, and it is possible
that more than one heme is present per cytochrome b-245.
-!- PTM: Phosphorylation at Thr-147 enhances NADPH oxidase activity by
promoting p47phox binding. {ECO:0000250}.
-!- DISEASE: Granulomatous disease, chronic, cytochrome-b-negative,
autosomal recessive (ARCGD) [MIM:233690]: A disorder characterized
by the inability of neutrophils and phagocytes to kill microbes
that they have ingested. Patients suffer from life-threatening
bacterial/fungal infections. {ECO:0000269|PubMed:10759707,
ECO:0000269|PubMed:10910929, ECO:0000269|PubMed:10914676,
ECO:0000269|PubMed:1415254, ECO:0000269|PubMed:1763037,
ECO:0000269|PubMed:18422995, ECO:0000269|PubMed:2243141,
ECO:0000269|PubMed:23910690, ECO:0000269|PubMed:7964505,
ECO:0000269|PubMed:8168815}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the p22phox family. {ECO:0000305}.
-!- WEB RESOURCE: Name=CYBAbase; Note=CYBA mutation db;
URL="http://structure.bmc.lu.se/idbase/CYBAbase/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=C&genename=CYBB+%40+GP91-PHOX";
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EMBL; M21186; AAA90925.1; -; mRNA.
EMBL; BT006861; AAP35507.1; -; mRNA.
EMBL; AC116552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006465; AAH06465.1; -; mRNA.
EMBL; AH002664; AAA52134.1; -; Genomic_DNA.
CCDS; CCDS32504.1; -.
PIR; A28201; A28201.
RefSeq; NP_000092.2; NM_000101.3.
UniGene; Hs.513803; -.
PDB; 1WLP; NMR; -; A=149-168.
PDBsum; 1WLP; -.
ProteinModelPortal; P13498; -.
SMR; P13498; -.
BioGrid; 107915; 13.
DIP; DIP-37650N; -.
IntAct; P13498; 7.
MINT; MINT-5209680; -.
STRING; 9606.ENSP00000261623; -.
DrugBank; DB00514; Dextromethorphan.
TCDB; 5.B.1.1.1; the phagocyte (gp91(phox)) nadph oxidase family.
iPTMnet; P13498; -.
PhosphoSitePlus; P13498; -.
BioMuta; CYBA; -.
DMDM; 311033459; -.
EPD; P13498; -.
MaxQB; P13498; -.
PaxDb; P13498; -.
PeptideAtlas; P13498; -.
PRIDE; P13498; -.
DNASU; 1535; -.
Ensembl; ENST00000261623; ENSP00000261623; ENSG00000051523.
GeneID; 1535; -.
KEGG; hsa:1535; -.
UCSC; uc002flb.5; human.
CTD; 1535; -.
DisGeNET; 1535; -.
EuPathDB; HostDB:ENSG00000051523.10; -.
GeneCards; CYBA; -.
GeneReviews; CYBA; -.
H-InvDB; HIX0013335; -.
HGNC; HGNC:2577; CYBA.
HPA; CAB009492; -.
MalaCards; CYBA; -.
MIM; 233690; phenotype.
MIM; 608508; gene.
neXtProt; NX_P13498; -.
OpenTargets; ENSG00000051523; -.
Orphanet; 379; Chronic granulomatous disease.
PharmGKB; PA27075; -.
eggNOG; ENOG410IXYN; Eukaryota.
eggNOG; ENOG4111MI6; LUCA.
GeneTree; ENSGT00390000002290; -.
HOGENOM; HOG000001585; -.
HOVERGEN; HBG051278; -.
InParanoid; P13498; -.
KO; K08009; -.
OMA; EQWTPIE; -.
PhylomeDB; P13498; -.
TreeFam; TF328901; -.
Reactome; R-HSA-1222556; ROS, RNS production in phagocytes.
Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; CYBA; human.
EvolutionaryTrace; P13498; -.
GenomeRNAi; 1535; -.
PRO; PR:P13498; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000051523; -.
CleanEx; HS_CYBA; -.
ExpressionAtlas; P13498; baseline and differential.
Genevisible; P13498; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043020; C:NADPH oxidase complex; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:Ensembl.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030141; C:secretory granule; TAS:BHF-UCL.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0009055; F:electron carrier activity; IDA:BHF-UCL.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0045454; P:cell redox homeostasis; TAS:Reactome.
GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:1904845; P:cellular response to L-glutamine; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0017004; P:cytochrome complex assembly; IDA:BHF-UCL.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISS:BHF-UCL.
GO; GO:0006954; P:inflammatory response; IMP:BHF-UCL.
GO; GO:0045087; P:innate immune response; IMP:BHF-UCL.
GO; GO:0003106; P:negative regulation of glomerular filtration by angiotensin; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0055114; P:oxidation-reduction process; IMP:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:1900426; P:positive regulation of defense response to bacterium; IDA:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl.
GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; IEA:Ensembl.
GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IDA:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IDA:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0045730; P:respiratory burst; IMP:BHF-UCL.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:1904044; P:response to aldosterone; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0014895; P:smooth muscle hypertrophy; ISS:BHF-UCL.
GO; GO:0042554; P:superoxide anion generation; IMP:BHF-UCL.
GO; GO:0006801; P:superoxide metabolic process; IMP:BHF-UCL.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
InterPro; IPR007732; Cyt_b558_asu.
PANTHER; PTHR15168; PTHR15168; 1.
Pfam; PF05038; Cytochrom_B558a; 1.
PIRSF; PIRSF019635; Cytochr_b558a; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Chronic granulomatous disease;
Complete proteome; Direct protein sequencing; Disease mutation;
Electron transport; Heme; Iron; Membrane; Metal-binding; NADP;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome;
Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3368442}.
CHAIN 2 195 Cytochrome b-245 light chain.
/FTId=PRO_0000144907.
INTRAMEM 91 127
COMPBIAS 133 189 Pro-rich.
METAL 94 94 Iron (heme axial ligand). {ECO:0000255}.
MOD_RES 147 147 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19948736}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000250|UniProtKB:Q61462}.
VARIANT 24 24 G -> R (in ARCGD; dbSNP:rs28941476).
{ECO:0000269|PubMed:10759707,
ECO:0000269|PubMed:10910929,
ECO:0000269|PubMed:10914676,
ECO:0000269|PubMed:23910690}.
/FTId=VAR_012755.
VARIANT 25 25 G -> D (in ARCGD).
{ECO:0000269|PubMed:23910690}.
/FTId=VAR_071860.
VARIANT 25 25 G -> V (in ARCGD; dbSNP:rs179363891).
{ECO:0000269|PubMed:10910929}.
/FTId=VAR_060576.
VARIANT 52 52 L -> P (in ARCGD; dbSNP:rs179363890).
{ECO:0000269|PubMed:10910929}.
/FTId=VAR_060577.
VARIANT 53 53 E -> V (in ARCGD; dbSNP:rs179363893).
{ECO:0000269|PubMed:8168815}.
/FTId=VAR_060578.
VARIANT 72 72 Y -> H (in dbSNP:rs4673).
{ECO:0000269|PubMed:19388116,
ECO:0000269|PubMed:2469497,
ECO:0000269|PubMed:3368442}.
/FTId=VAR_005122.
VARIANT 90 90 R -> Q (in ARCGD; dbSNP:rs104894513).
{ECO:0000269|PubMed:1415254}.
/FTId=VAR_005123.
VARIANT 90 90 R -> W (in ARCGD; dbSNP:rs179363892).
{ECO:0000269|PubMed:10910929}.
/FTId=VAR_060579.
VARIANT 94 94 H -> R (in ARCGD; dbSNP:rs104894510).
{ECO:0000269|PubMed:1415254}.
/FTId=VAR_005124.
VARIANT 118 118 S -> R (in ARCGD; dbSNP:rs104894514).
{ECO:0000269|PubMed:10910929,
ECO:0000269|PubMed:2243141}.
/FTId=VAR_005125.
VARIANT 124 124 A -> V (in ARCGD; dbSNP:rs179363894).
{ECO:0000269|PubMed:10914676,
ECO:0000269|PubMed:23910690}.
/FTId=VAR_060580.
VARIANT 125 125 A -> T (in ARCGD; dbSNP:rs119103269).
{ECO:0000269|PubMed:18422995,
ECO:0000269|PubMed:23910690}.
/FTId=VAR_060581.
VARIANT 156 156 P -> Q (in ARCGD; dbSNP:rs104894515).
{ECO:0000269|PubMed:1763037,
ECO:0000269|PubMed:7964505}.
/FTId=VAR_005126.
VARIANT 171 171 E -> G (in dbSNP:rs72667005).
{ECO:0000269|PubMed:19388116}.
/FTId=VAR_060582.
VARIANT 174 174 V -> A (in dbSNP:rs1049254).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19388116,
ECO:0000269|PubMed:2469497,
ECO:0000269|PubMed:3368442,
ECO:0000269|Ref.2}.
/FTId=VAR_054801.
VARIANT 193 193 E -> D (in dbSNP:rs72667006).
{ECO:0000269|PubMed:19388116}.
/FTId=VAR_060583.
MUTAGEN 157 157 P->Q: Loss of interaction with NOXO1.
{ECO:0000269|PubMed:12716910}.
HELIX 161 165 {ECO:0000244|PDB:1WLP}.
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


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