CY24A_TURTR
ID CY24A_TURTR Reviewed; 192 AA.
AC Q9N2H0;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
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 Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Inoue Y., Ito T., Sakai T.;
RT "Molecular cloning and identification of bottle-nosed dolphin
RT flavocytochrome b558.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; AB034193; BAA95155.1; -; mRNA.
DR RefSeq; NP_001267539.1; NM_001280610.1.
DR AlphaFoldDB; Q9N2H0; -.
DR Ensembl; ENSTTRT00000006248; ENSTTRP00000005912; ENSTTRG00000006256.
DR GeneID; 101328418; -.
DR HOGENOM; CLU_125024_0_0_1; -.
DR OMA; AYDNPIS; -.
DR OrthoDB; 1604124at2759; -.
DR TreeFam; TF328901; -.
DR Proteomes; UP000245320; Chromosome 19.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0043020; C:NADPH oxidase complex; ISS:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IEA:Ensembl.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0045730; P:respiratory burst; IEA:Ensembl.
DR GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
DR InterPro; IPR007732; Cyt_b558_asu.
DR PANTHER; PTHR15168; PTHR15168; 1.
DR Pfam; PF05038; Cytochrom_B558a; 1.
DR PIRSF; PIRSF019635; Cytochr_b558a; 1.
PE 2: Evidence at transcript 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_0000144912"
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: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"
SQ SEQUENCE 192 AA; 20509 MW; DDEEE8EF54518B21 CRC64;
MGQIEWAMWA NEQALASGLI LITGGIVATA GQFAQWYLGA YSIAAGVLIC LLEYPRGKRS
KGSTMERCGQ KYLTRAVKVF GPLTSNYYIR AFLHLGLSVP AGFLLATILG TACLAIASSI
YLLAAIHGEH WTPIETKPKE RPQVGGTIKQ PPSNPPPRPP AEARKKPSEE EVAGVPGGGP
QENPMPVTDE VV
