CY24B_PIG
ID CY24B_PIG Reviewed; 484 AA.
AC P52649;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cytochrome b-245 heavy chain;
DE EC=1.-.-.-;
DE AltName: Full=CGD91-phox;
DE AltName: Full=Cytochrome b(558) subunit beta;
DE Short=Cytochrome b558 subunit beta;
DE AltName: Full=Heme-binding membrane glycoprotein gp91phox;
DE AltName: Full=Neutrophil cytochrome b 91 kDa polypeptide;
DE AltName: Full=gp91-1;
DE AltName: Full=gp91-phox;
DE AltName: Full=p22 phagocyte B-cytochrome;
DE Flags: Fragment;
GN Name=CYBB;
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=7857983; DOI=10.1016/0167-4889(94)00207-u;
RA Zhou Y., Lin G., Murtaugh M.P.;
RT "Interleukin-4 suppresses the expression of macrophage NADPH oxidase heavy
RT chain subunit (gp91-phox).";
RL Biochim. Biophys. Acta 1265:40-48(1995).
CC -!- FUNCTION: Critical component of the membrane-bound oxidase of
CC phagocytes that generates superoxide. It is the terminal component of a
CC respiratory chain that transfers single electrons from cytoplasmic
CC NADPH across the plasma membrane to molecular oxygen on the exterior.
CC Also functions as a voltage-gated proton channel that mediates the H(+)
CC currents of resting phagocytes.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
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. Interacts with calprotectin
CC (S100A8/9). Interacts with NRROS; the interaction is direct and impairs
CC formation of a stable NADPH oxidase complex. Interacts with CYBC1;
CC CYBC1 may act as a chaperone stabilizing Cytochrome b-245 heterodimer
CC (By similarity). Interacts with NCF2; the interaction is enhanced in
CC the presence of GBP7 (By similarity). The CYBA-CYBB complex interacts
CC with GBP7 (By similarity). {ECO:0000250|UniProtKB:P04839,
CC ECO:0000250|UniProtKB:Q61093}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04839};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P04839}. Note=As
CC unassembled monomer may localize to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P04839}.
CC -!- PTM: Phosphorylated on Ser and Thr residues. {ECO:0000250}.
CC -!- PTM: Undergoes 'Lys-48'-linked polyubiquitination, likely by RNF145,
CC triggering endoplasmic reticulum-associated degradation.
CC {ECO:0000250|UniProtKB:Q61093}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64634.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U02476; AAA64634.1; ALT_INIT; mRNA.
DR PIR; S52077; S52077.
DR RefSeq; NP_999208.1; NM_214043.2.
DR AlphaFoldDB; P52649; -.
DR SMR; P52649; -.
DR STRING; 9823.ENSSSCP00000029153; -.
DR PaxDb; P52649; -.
DR PeptideAtlas; P52649; -.
DR GeneID; 397108; -.
DR KEGG; ssc:397108; -.
DR CTD; 397108; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; P52649; -.
DR OrthoDB; 936110at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0043020; C:NADPH oxidase complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Electron transport; FAD; Flavoprotein; Glycoprotein; Heme;
KW Ion channel; Ion transport; Iron; Isopeptide bond; Membrane; Metal-binding;
KW NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN <1..484
FT /note="Cytochrome b-245 heavy chain"
FT /id="PRO_0000210147"
FT TOPO_DOM <1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..87
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 5..201
FT /note="Ferric oxidoreductase"
FT DOMAIN 201..311
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 15
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:0000305"
FT BINDING 29
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:0000305"
FT BINDING 123
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:0000305"
FT BINDING 136
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:0000305"
FT BINDING 252..258
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 75
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 169
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 242
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT NON_TER 1
SQ SEQUENCE 484 AA; 55830 MW; 065AB9B6920CFE02 CRC64;
STRVRRQLDR NLTFHKMVAW MIALHATIHT IAHLFNVEWC VNARVNNSDP YSIALSDIGD
KPNETYLNFV RQRIKNPEGG LYVAVTRLAG ITGVVITLCL ILIITSSTKT IRRSYFEVFW
YTHHLFVIFF IGLAIHGAER IVRRQTPKSL LVHDPKACAQ NISQWGKIKD CPIPEFAGNP
PMTWKWIVGP MFLYLCERLV RFWRSQQKVV ITKVVTHPFK TIELQMKKKG FRMEVGQYIF
VKRPAVSKLE WHPFTLTSAP EEDFFSIHIR IVGDWTEGLF KACGCDKQEF QDAWKLPKIA
VDGPFGTASE DVFSYQVVML VGAGIGVTPF ASILKSVWYK YCNNATNLRL KKIYFYWLCR
DTHAFEWFAD LLQLLETQMQ ERNNAGFLSY NIYLTGWDES QANHFAVHHD EEKDVITGLK
QKTLYGRPNW DNEFKTIASQ HPTTRIGVFL CGPEALAETL NKQCISNSDS SPRGVHFIFN
KENF
