CY24B_BISBI
ID CY24B_BISBI Reviewed; 570 AA.
AC Q95L74;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 73.
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;
GN Name=CYBB;
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. 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}.
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DR EMBL; AF411135; AAL11885.1; -; mRNA.
DR AlphaFoldDB; Q95L74; -.
DR SMR; Q95L74; -.
DR GO; GO:0043020; C:NADPH oxidase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
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: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; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..570
FT /note="Cytochrome b-245 heavy chain"
FT /id="PRO_0000210143"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..286
FT /note="Ferric oxidoreductase"
FT DOMAIN 287..397
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 101
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 115
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 209
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 222
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 338..344
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 506
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
FT CROSSLNK 567
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q61093"
SQ SEQUENCE 570 AA; 65600 MW; 94F9D1E833E19848 CRC64;
MGNWVVNEGI SIFVILVWLG MNVFLFVWYY RVYDIPDKFF YTRKLLGSAL ALARAPAACL
NFNCMLILLP VCRNLLSFLR GSSACCSTRI RRQLDRNLTF HKMVAWMIAL HTAIHTIAHL
FNVEWCVNAR VNNSDPYSIA LSDIGDKPNE TYLNFVRQRI KNPEGGLYVA VTLLAGITGV
VITLCLILII TSSTKTIRRS YFEVFWYTHH LFVIFFIGLA IHGAQRIVRG QTAESLLKHQ
PRNCYQNISQ WGKIKDCPIP EFSGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKV
VTHPFKTIEL QMKKKGFKME VGQYIFVKCP VVSKLEWHPF TLTSAPEEDF FSIHIRIVGD
WTEGLFKACG CDKQEFQDAW KLPKIAVDGP FGTASEDVFS YEVVMLVGAG IGVTPFASIL
KSVWYKYCNK APNLRLKKIY FYWLCRDTHA FEWFADLLQL LETQMQEKNN TDFLSYNICL
TGWDESQASH FAMHHDEEKD VITGLKQKTL YGRPNWDNEF KTIGSQHPNT RIGVFLCGPE
ALADTLNKQC ISNSDSGPRG VHFIFNKENF
