ID   CY24A_BISBI             Reviewed;         191 AA.
AC   Q95L73;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 72.
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   Bison bison (American bison) (Bos bison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bison.
OX   NCBI_TaxID=9901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12223206; DOI=10.1016/s1096-4959(02)00090-8;
RA   Gauss K.A., Bunger P.L., Siemsen D.W., Young C.J., Nelson-Overton L.,
RA   Prigge J.R., Swain S.D., Quinn M.T.;
RT   "Molecular analysis of the bison phagocyte NADPH oxidase: cloning and
RT   sequencing of five NADPH oxidase cDNAs.";
RL   Comp. Biochem. Physiol. 133B:1-12(2002).
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; AF411136; AAL11886.1; -; mRNA.
DR   AlphaFoldDB; Q95L73; -.
DR   GO; GO:0043020; C:NADPH oxidase complex; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
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; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..191
FT                   /note="Cytochrome b-245 light chain"
FT                   /id="PRO_0000144905"
FT   INTRAMEM        91..127
FT                   /evidence="ECO:0000250"
FT   REGION          134..191
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   191 AA;  20512 MW;  D3D7C8D50C1FBAC5 CRC64;
     MGQIEWAMWA NEQALASGLI LITGGIVATA GQFTQWYLGA YSIAAGVLVC LLEYPRGKRS
     KGSTMERCGQ KYLTRVVKLF GPLTRNYYIR AFLHLGLAVP AGFLLATILG TACLAIASGI
     YLLAAIRGEQ WSPIEPKPKE RPQIGGTIKQ PPSNPPPRPP AEARKKLSEE AAGVPTGGPQ
     ENPMPVNDEV V