UniProtKB - P52649 (CY24B_PIG)
Cytochrome b-245 heavy chain
CYBB
Functioni
Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H+ currents of resting phagocytes.
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 15 | Iron (heme axial ligand)Curated | 1 | |
Metal bindingi | 29 | Iron (heme axial ligand)Curated | 1 | |
Metal bindingi | 123 | Iron (heme axial ligand)Curated | 1 | |
Metal bindingi | 136 | Iron (heme axial ligand)Curated | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 252 – 258 | FADSequence analysis | 7 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- superoxide-generating NAD(P)H oxidase activity Source: GO_Central
- voltage-gated ion channel activity Source: UniProtKB-KW
GO - Biological processi
- defense response Source: GO_Central
- inflammatory response Source: UniProtKB
- innate immune response Source: UniProtKB
- regulation of ion transmembrane transport Source: UniProtKB-KW
- superoxide anion generation Source: GO_Central
- superoxide metabolic process Source: UniProtKB
Keywordsi
Molecular function | Ion channel, Oxidoreductase, Voltage-gated channel |
Biological process | Electron transport, Ion transport, Transport |
Ligand | FAD, Flavoprotein, Heme, Iron, Metal-binding, NADP |
Names & Taxonomyi
Protein namesi | Recommended name: Cytochrome b-245 heavy chain (EC:1.-.-.-)Alternative name(s): CGD91-phox Cytochrome b(558) subunit beta Short name: Cytochrome b558 subunit beta Heme-binding membrane glycoprotein gp91phox Neutrophil cytochrome b 91 kDa polypeptide gp91-1 gp91-phox p22 phagocyte B-cytochrome |
Gene namesi | Name:CYBB |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Multi-pass membrane protein By similarity
Note: As unassembled monomer may localize to the endoplasmic reticulum.By similarity
Plasma Membrane
- NADPH oxidase complex Source: UniProtKB
- plasma membrane Source: GO_Central
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | ‹1 – 16 | CytoplasmicSequence analysisAdd BLAST | ›16 | |
Transmembranei | 17 – 37 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 38 – 87 | ExtracellularSequence analysisAdd BLAST | 50 | |
Transmembranei | 88 – 108 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 109 – 114 | CytoplasmicSequence analysis | 6 | |
Transmembranei | 115 – 135 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 136 – 175 | ExtracellularSequence analysisAdd BLAST | 40 | |
Transmembranei | 176 – 196 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 197 – 484 | CytoplasmicSequence analysisAdd BLAST | 288 |
Keywords - Cellular componenti
Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000210147 | ‹1 – 484 | Cytochrome b-245 heavy chainAdd BLAST | ›484 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 46 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 63 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Cross-linki | 75 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Glycosylationi | 161 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Cross-linki | 169 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 208 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 213 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 220 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 242 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 248 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 295 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 420 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 481 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity |
Post-translational modificationi
Keywords - PTMi
Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | P52649 |
PeptideAtlasi | P52649 |
Interactioni
Subunit structurei
Composed of a heavy chain (beta) and a light chain (alpha).
Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4.
Interacts with NCF1.
Interacts with calprotectin (S100A8/9).
Interacts with NRROS; the interaction is direct and impairs formation of a stable NADPH oxidase complex.
Interacts with CYBC1; CYBC1 may act as a chaperone stabilizing Cytochrome b-245 heterodimer (By similarity).
Interacts with NCF2; the interaction is enhanced in the presence of GBP7 (By similarity). The CYBA-CYBB complex interacts with GBP7 (By similarity).
By similarityProtein-protein interaction databases
STRINGi | 9823.ENSSSCP00000029153 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 5 – 201 | Ferric oxidoreductaseAdd BLAST | 197 | |
Domaini | 201 – 311 | FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST | 111 |
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0039, Eukaryota |
InParanoidi | P52649 |
OrthoDBi | 936110at2759 |
Family and domain databases
Gene3Di | 3.40.50.80, 1 hit |
InterProi | View protein in InterPro IPR000778, Cyt_b245_heavy_chain IPR013112, FAD-bd_8 IPR017927, FAD-bd_FR_type IPR013130, Fe3_Rdtase_TM_dom IPR013121, Fe_red_NAD-bd_6 IPR039261, FNR_nucleotide-bd IPR017938, Riboflavin_synthase-like_b-brl |
Pfami | View protein in Pfam PF08022, FAD_binding_8, 1 hit PF01794, Ferric_reduct, 1 hit PF08030, NAD_binding_6, 1 hit |
PRINTSi | PR00466, GP91PHOX |
SUPFAMi | SSF52343, SSF52343, 1 hit SSF63380, SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS51384, FAD_FR, 1 hit |
i Sequence
Sequence statusi: Fragment.
10 20 30 40 50
STRVRRQLDR NLTFHKMVAW MIALHATIHT IAHLFNVEWC VNARVNNSDP
60 70 80 90 100
YSIALSDIGD KPNETYLNFV RQRIKNPEGG LYVAVTRLAG ITGVVITLCL
110 120 130 140 150
ILIITSSTKT IRRSYFEVFW YTHHLFVIFF IGLAIHGAER IVRRQTPKSL
160 170 180 190 200
LVHDPKACAQ NISQWGKIKD CPIPEFAGNP PMTWKWIVGP MFLYLCERLV
210 220 230 240 250
RFWRSQQKVV ITKVVTHPFK TIELQMKKKG FRMEVGQYIF VKRPAVSKLE
260 270 280 290 300
WHPFTLTSAP EEDFFSIHIR IVGDWTEGLF KACGCDKQEF QDAWKLPKIA
310 320 330 340 350
VDGPFGTASE DVFSYQVVML VGAGIGVTPF ASILKSVWYK YCNNATNLRL
360 370 380 390 400
KKIYFYWLCR DTHAFEWFAD LLQLLETQMQ ERNNAGFLSY NIYLTGWDES
410 420 430 440 450
QANHFAVHHD EEKDVITGLK QKTLYGRPNW DNEFKTIASQ HPTTRIGVFL
460 470 480
CGPEALAETL NKQCISNSDS SPRGVHFIFN KENF
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Non-terminal residuei | 1 | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U02476 mRNA Translation: AAA64634.1 Different initiation. |
PIRi | S52077 |
RefSeqi | NP_999208.1, NM_214043.2 |
Genome annotation databases
GeneIDi | 397108 |
KEGGi | ssc:397108 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U02476 mRNA Translation: AAA64634.1 Different initiation. |
PIRi | S52077 |
RefSeqi | NP_999208.1, NM_214043.2 |
3D structure databases
SMRi | P52649 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9823.ENSSSCP00000029153 |
Proteomic databases
PaxDbi | P52649 |
PeptideAtlasi | P52649 |
Genome annotation databases
GeneIDi | 397108 |
KEGGi | ssc:397108 |
Organism-specific databases
CTDi | 397108 |
Phylogenomic databases
eggNOGi | KOG0039, Eukaryota |
InParanoidi | P52649 |
OrthoDBi | 936110at2759 |
Family and domain databases
Gene3Di | 3.40.50.80, 1 hit |
InterProi | View protein in InterPro IPR000778, Cyt_b245_heavy_chain IPR013112, FAD-bd_8 IPR017927, FAD-bd_FR_type IPR013130, Fe3_Rdtase_TM_dom IPR013121, Fe_red_NAD-bd_6 IPR039261, FNR_nucleotide-bd IPR017938, Riboflavin_synthase-like_b-brl |
Pfami | View protein in Pfam PF08022, FAD_binding_8, 1 hit PF01794, Ferric_reduct, 1 hit PF08030, NAD_binding_6, 1 hit |
PRINTSi | PR00466, GP91PHOX |
SUPFAMi | SSF52343, SSF52343, 1 hit SSF63380, SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS51384, FAD_FR, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CY24B_PIG | |
Accessioni | P52649Primary (citable) accession number: P52649 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | May 30, 2000 | |
Last modified: | February 23, 2022 | |
This is version 120 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |