CY24A_PIG
ID CY24A_PIG Reviewed; 192 AA.
AC P52650;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 86.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=7958970; DOI=10.1016/0378-1119(94)90714-5;
RA Zhou Y., Murtaugh M.P.;
RT "Cloning and expression of the gene encoding the porcine NADPH oxidase
RT light-chain subunit (p22-phox).";
RL Gene 148:363-367(1994).
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; U02477; AAA64635.1; -; mRNA.
DR RefSeq; NP_999432.1; NM_214267.1.
DR AlphaFoldDB; P52650; -.
DR PRIDE; P52650; -.
DR GeneID; 397507; -.
DR KEGG; ssc:397507; -.
DR CTD; 1535; -.
DR InParanoid; P52650; -.
DR OrthoDB; 1604124at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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 GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
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_0000144909"
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 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; 20745 MW; 9D516AC867385560 CRC64;
MGQIEWAMWA NEQALASGLI LMTGGIVATA GQFTQWYLGT YSIAAGVLVC LLEYPRGRRT
KGSTMERCEQ KYMTKVVKAF GPLSRNYYIR AFLHLGLSVP AGFLLATILG TACLAIASGI
YLLAAIRGEQ WTPIEPKPKE RPQVGGTIKQ PPSNPPPRPP PEARKKPGEE AVAGVPRGAP
RKTPCPVTDE VV
