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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_RAT               Reviewed;         192 AA.
Q62737; Q9ER27;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 123.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Vascular smooth muscle;
PubMed=7578211; DOI=10.1016/0005-2728(95)00098-4;
Fukui T., Lassegue B., Kai H., Alexander R.W., Griendling K.K.;
"Cytochrome b-558 alpha-subunit cloning and expression in rat aortic
smooth muscle cells.";
Biochim. Biophys. Acta 1231:215-219(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Coronary artery;
PubMed=10938010; DOI=10.1161/01.ATV.20.8.1903;
Bayraktutan U., Blayney L., Shah A.M.;
"Molecular characterization and localization of the NAD(P)H oxidase
components gp91-phox and p22-phox in endothelial cells.";
Arterioscler. Thromb. Vasc. Biol. 20:1903-1911(2000).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-176, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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.
-!- 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) (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed to a relatively high level in
kidney, spleen, thymus and lung, and to a lower level in aorta,
adrenals, and heart. Expression is not detected in liver or brain.
{ECO:0000269|PubMed:7578211}.
-!- 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.
{ECO:0000250}.
-!- PTM: Phosphorylation at Thr-147 enhances NADPH oxidase activity by
promoting p47phox binding. {ECO:0000250}.
-!- SIMILARITY: Belongs to the p22phox family. {ECO:0000305}.
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EMBL; U18729; AAA85865.1; -; mRNA.
EMBL; AJ295951; CAC09434.1; -; mRNA.
RefSeq; NP_077074.1; NM_024160.1.
UniGene; Rn.5856; -.
SMR; Q62737; -.
STRING; 10116.ENSRNOP00000017564; -.
iPTMnet; Q62737; -.
PhosphoSitePlus; Q62737; -.
PaxDb; Q62737; -.
PRIDE; Q62737; -.
Ensembl; ENSRNOT00000017564; ENSRNOP00000017564; ENSRNOG00000013014.
GeneID; 79129; -.
KEGG; rno:79129; -.
UCSC; RGD:620573; rat.
CTD; 1535; -.
RGD; 620573; Cyba.
eggNOG; ENOG410IXYN; Eukaryota.
eggNOG; ENOG4111MI6; LUCA.
GeneTree; ENSGT00390000002290; -.
HOGENOM; HOG000001585; -.
HOVERGEN; HBG051278; -.
InParanoid; Q62737; -.
KO; K08009; -.
OMA; EQWTPIE; -.
OrthoDB; EOG091G0NNC; -.
PhylomeDB; Q62737; -.
Reactome; R-RNO-1222556; ROS, RNS production in phagocytes.
Reactome; R-RNO-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:Q62737; -.
Proteomes; UP000002494; Chromosome 19.
Bgee; ENSRNOG00000013014; -.
Genevisible; Q62737; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043020; C:NADPH oxidase complex; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0001725; C:stress fiber; IDA:RGD.
GO; GO:0009055; F:electron carrier activity; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:RGD.
GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD.
GO; GO:0071480; P:cellular response to gamma radiation; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:1904845; P:cellular response to L-glutamine; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0071310; P:cellular response to organic substance; IDA:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0017004; P:cytochrome complex assembly; IEA:Ensembl.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:BHF-UCL.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:Ensembl.
GO; GO:0003106; P:negative regulation of glomerular filtration by angiotensin; IMP:RGD.
GO; GO:0055114; P:oxidation-reduction process; IMP:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
GO; GO:1900426; P:positive regulation of defense response to bacterium; IEA:Ensembl.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:RGD.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl.
GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; IMP:RGD.
GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:RGD.
GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0008217; P:regulation of blood pressure; IMP:RGD.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0045730; P:respiratory burst; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:1904044; P:response to aldosterone; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0014895; P:smooth muscle hypertrophy; IMP:BHF-UCL.
GO; GO:0042554; P:superoxide anion generation; IMP:BHF-UCL.
GO; GO:0006801; P:superoxide metabolic process; IDA:RGD.
InterPro; IPR007732; Cyt_b558_asu.
PANTHER; PTHR15168; PTHR15168; 1.
Pfam; PF05038; Cytochrom_B558a; 1.
PIRSF; PIRSF019635; Cytochr_b558a; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Electron transport; Heme; Iron;
Membrane; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
Reference proteome; Transport.
CHAIN 1 192 Cytochrome b-245 light chain.
/FTId=PRO_0000144911.
INTRAMEM 91 127 {ECO:0000250}.
METAL 94 94 Iron (heme axial ligand). {ECO:0000255}.
MOD_RES 147 147 Phosphothreonine.
{ECO:0000250|UniProtKB:P13498}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
SEQUENCE 192 AA; 20750 MW; EDFCB82C2D217AEA CRC64;
MGQIEWAMWA NEQALASGLI LITGGIVATA GRFTQWYFGA YSIVAGVLIC LLEYPRGKRK
KGSTMERCGQ KYLTAVVKLF GPLTRNYYVR AVLHLLLSVP AGFLLATILG TVCLAIASVI
YLLAAIRGEQ WTPIEPKPKE RPQVGGTIKQ PPTNPPPRPP AEVRKKPSEA EEEAASAGGP
QVNPIPVTDE VV


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