CY24A_RAT
ID CY24A_RAT Reviewed; 192 AA.
AC Q62737; Q9ER27;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 149.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Vascular smooth muscle;
RX PubMed=7578211; DOI=10.1016/0005-2728(95)00098-4;
RA Fukui T., Lassegue B., Kai H., Alexander R.W., Griendling K.K.;
RT "Cytochrome b-558 alpha-subunit cloning and expression in rat aortic smooth
RT muscle cells.";
RL Biochim. Biophys. Acta 1231:215-219(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Coronary artery;
RX PubMed=10938010; DOI=10.1161/01.atv.20.8.1903;
RA Bayraktutan U., Blayney L., Shah A.M.;
RT "Molecular characterization and localization of the NAD(P)H oxidase
RT components gp91-phox and p22-phox in endothelial cells.";
RL Arterioscler. Thromb. Vasc. Biol. 20:1903-1911(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- 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 (By similarity). Interacts with GBP7 (By similarity).
CC {ECO:0000250|UniProtKB:P13498, ECO:0000250|UniProtKB:Q61462}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13498}.
CC Note=As unassembled monomer may localize to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q61462}.
CC -!- TISSUE SPECIFICITY: Expressed to a relatively high level in kidney,
CC spleen, thymus and lung, and to a lower level in aorta, adrenals, and
CC heart. Expression is not detected in liver or brain.
CC {ECO:0000269|PubMed:7578211}.
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. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the p22phox family. {ECO:0000305}.
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DR EMBL; U18729; AAA85865.1; -; mRNA.
DR EMBL; AJ295951; CAC09434.1; -; mRNA.
DR RefSeq; NP_077074.1; NM_024160.1.
DR AlphaFoldDB; Q62737; -.
DR STRING; 10116.ENSRNOP00000017564; -.
DR iPTMnet; Q62737; -.
DR PhosphoSitePlus; Q62737; -.
DR PaxDb; Q62737; -.
DR GeneID; 79129; -.
DR KEGG; rno:79129; -.
DR UCSC; RGD:620573; rat.
DR CTD; 1535; -.
DR RGD; 620573; Cyba.
DR VEuPathDB; HostDB:ENSRNOG00000013014; -.
DR eggNOG; ENOG502QVK1; Eukaryota.
DR HOGENOM; CLU_125024_0_0_1; -.
DR InParanoid; Q62737; -.
DR OMA; AYDNPIS; -.
DR OrthoDB; 1604124at2759; -.
DR PhylomeDB; Q62737; -.
DR Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-RNO-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q62737; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000013014; Expressed in spleen and 18 other tissues.
DR Genevisible; Q62737; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0043020; C:NADPH oxidase complex; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0001725; C:stress fiber; IDA:RGD.
DR GO; GO:0009055; F:electron transfer activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:RGD.
DR GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:1904845; P:cellular response to L-glutamine; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0017004; P:cytochrome complex assembly; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR GO; GO:0003106; P:negative regulation of glomerular filtration by angiotensin; IMP:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; ISO:RGD.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0070257; P:positive regulation of mucus secretion; ISO:RGD.
DR GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; IMP:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:RGD.
DR GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0045730; P:respiratory burst; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:1904044; P:response to aldosterone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0014895; P:smooth muscle hypertrophy; IMP:BHF-UCL.
DR GO; GO:0042554; P:superoxide anion generation; IMP:BHF-UCL.
DR GO; GO:0006801; P:superoxide metabolic process; IDA:RGD.
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 Cell membrane; Electron transport; Heme; Iron; Isopeptide bond; Membrane;
KW Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transport; Ubl conjugation.
FT CHAIN 1..192
FT /note="Cytochrome b-245 light chain"
FT /id="PRO_0000144911"
FT INTRAMEM 91..127
FT /evidence="ECO:0000250"
FT REGION 134..192
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:0000250|UniProtKB:P13498"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61462"
SQ 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
