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Q61093 (CY24B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Cybb
Synonyms:Cgd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Cofactor

FAD Probable.

Subunit structure

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) By similarity. Interacts with NRROS; the interaction is direct and impairs formation of a stable NADPH oxidase complex. Ref.3

Subcellular location

Cell membrane; Multi-pass membrane protein.

Post-translational modification

Glycosylated.

Phosphorylated on Ser and Thr residues By similarity.

Sequence similarities

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Ontologies

Keywords
   Biological processElectron transport
Ion transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
Heme
Iron
Metal-binding
NADP
   Molecular functionIon channel
Oxidoreductase
Voltage-gated channel
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhydrogen peroxide biosynthetic process

Inferred from mutant phenotype PubMed 15258578. Source: MGI

inflammatory response

Inferred from mutant phenotype Ref.3. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

superoxide anion generation

Inferred from electronic annotation. Source: Ensembl

superoxide metabolic process

Inferred from mutant phenotype Ref.3. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

NADPH oxidase complex

Inferred from direct assay Ref.3. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 15499027PubMed 15850784. Source: MGI

dendrite

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 15499027. Source: MGI

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionelectron carrier activity

Inferred from electronic annotation. Source: Ensembl

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: Ensembl

heme binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.3. Source: UniProtKB

superoxide-generating NADPH oxidase activity

Inferred from direct assay PubMed 22493499. Source: MGI

voltage-gated ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 570569Cytochrome b-245 heavy chain
PRO_0000210146

Regions

Topological domain2 – 87Cytoplasmic Potential
Transmembrane9 – 2921Helical; Potential
Topological domain30 – 4819Extracellular Potential
Transmembrane49 – 6921Helical; Potential
Topological domain70 – 10233Cytoplasmic Potential
Transmembrane103 – 12321Helical; Potential
Topological domain124 – 16946Extracellular Potential
Transmembrane170 – 19021Helical; Potential
Topological domain191 – 20010Cytoplasmic Potential
Transmembrane201 – 22121Helical; Potential
Topological domain222 – 26140Extracellular Potential
Transmembrane262 – 28221Helical; Potential
Topological domain283 – 570288Cytoplasmic Potential
Domain54 – 286233Ferric oxidoreductase
Domain287 – 397111FAD-binding FR-type
Nucleotide binding338 – 3447FAD Potential

Sites

Metal binding1011Iron (heme axial ligand) Probable
Metal binding1151Iron (heme axial ligand) Probable
Metal binding2091Iron (heme axial ligand) Probable
Metal binding2221Iron (heme axial ligand) Probable

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q61093 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8816274E3D253DFA

FASTA57065,305
        10         20         30         40         50         60 
MGNWAVNEGL SIFVILVWLG LNVFLFINYY KVYDDGPKYN YTRKLLGSAL ALARAPAACL 

        70         80         90        100        110        120 
NFNCMLILLP VCRNLLSFLR GSSACCSTRI RRQLDRNLTF HKMVAWMIAL HTAIHTIAHL 

       130        140        150        160        170        180 
FNVEWCVNAR VGISDRYSIA LSDIGDNENE EYLNFAREKI KNPEGGLYVA VTRLAGITGI 

       190        200        210        220        230        240 
VITLCLILII TSSTKTIRRS YFEVFWYTHH LFVIFFIGLA IHGAERIVRG QTAESLEEHN 

       250        260        270        280        290        300 
LDICADKIEE WGKIKECPVP KFAGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKV 

       310        320        330        340        350        360 
VTHPFKTIEL QMKKKGFKME VGQYIFVKCP KVSKLEWHPF TLTSAPEEDF FSIHIRIVGD 

       370        380        390        400        410        420 
WTEGLFNACG CDKQEFQDAW KLPKIAVDGP FGTASEDVFS YEVVMLVGAG IGVTPFASIL 

       430        440        450        460        470        480 
KSVWYKYCDN ATSLKLKKIY FYWLCRDTHA FEWFADLLQL LETQMQERNN ANFLSYNIYL 

       490        500        510        520        530        540 
TGWDESQANH FAVHHDEEKD VITGLKQKTL YGRPNWDNEF KTIASEHPNT TIGVFLCGPE 

       550        560        570 
ALAETLSKQS ISNSESGPRG VHFIFNKENF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of murine gp91phox cDNA and functional expression in a human X-linked chronic granulomatous disease cell line."
Bjorgvinsdottir H., Zhen L., Dinauer M.C.
Blood 87:2005-2010(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NMRI.
Tissue: Mammary gland.
[3]"NRROS negatively regulates reactive oxygen species during host defence and autoimmunity."
Noubade R., Wong K., Ota N., Rutz S., Eidenschenk C., Valdez P.A., Ding J., Peng I., Sebrell A., Caplazi P., Devoss J., Soriano R.H., Sai T., Lu R., Modrusan Z., Hackney J., Ouyang W.
Nature 509:235-239(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NRROS, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43384 mRNA. Translation: AAB05997.1.
BC071229 mRNA. Translation: AAH71229.1.
CCDSCCDS30010.1.
RefSeqNP_031833.3. NM_007807.5.
XP_006527628.1. XM_006527565.1.
UniGeneMm.200362.

3D structure databases

ProteinModelPortalQ61093.
SMRQ61093. Positions 385-570.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ61093. 3 interactions.

Protein family/group databases

PeroxiBase5957. MmNOx02.

PTM databases

PhosphoSiteQ61093.

Proteomic databases

MaxQBQ61093.
PaxDbQ61093.
PRIDEQ61093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015484; ENSMUSP00000015484; ENSMUSG00000015340.
GeneID13058.
KEGGmmu:13058.
UCSCuc009spv.2. mouse.

Organism-specific databases

CTD1536.
MGIMGI:88574. Cybb.

Phylogenomic databases

eggNOGNOG287712.
GeneTreeENSGT00550000074350.
HOGENOMHOG000216669.
HOVERGENHBG003760.
InParanoidQ61093.
KOK08008.
OMAERNNANF.
OrthoDBEOG71P299.
PhylomeDBQ61093.
TreeFamTF105354.

Gene expression databases

ArrayExpressQ61093.
BgeeQ61093.
CleanExMM_CYBB.
GenevestigatorQ61093.

Family and domain databases

InterProIPR000778. Cyt_b245_heavy_chain.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSPR00466. GP91PHOX.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCYBB. mouse.
NextBio282986.
PROQ61093.
SOURCESearch...

Entry information

Entry nameCY24B_MOUSE
AccessionPrimary (citable) accession number: Q61093
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot