Cytochrome b-245 heavy chain - Bos taurus (Bovine)

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O46522 (CY24B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

CYBB

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Cofactor	FAD Probable.
Subunit structure	Composed of a heavy chain (beta) and a light chain (alpha). Interacts with calprotectin (S100A8/9) By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Contains 1 FAD-binding FR-type domain. Contains 1 ferric oxidoreductase domain.

Ontologies

Keywords
Biological process	Electron transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	FAD Heme Iron Metal-binding NADP
Molecular function	Ion channel Oxidoreductase Voltage-gated channel
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW hydrogen peroxide biosynthetic process Inferred from electronic annotation. Source: Compara superoxide anion generation Inferred from electronic annotation. Source: Compara
Cellular_component	integral to plasma membrane Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: Compara flavin adenine dinucleotide binding Inferred from electronic annotation. Source: Compara heme binding Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide-generating NADPH oxidase activity Inferred from electronic annotation. Source: Compara voltage-gated ion channel activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 570

569

Cytochrome b-245 heavy chain

PRO_0000210144

Regions

Topological domain

2 – 8

Cytoplasmic Potential

Transmembrane

9 – 29

Helical; Potential

Topological domain

30 – 48

Extracellular Potential

Transmembrane

49 – 69

Helical; Potential

Topological domain

70 – 102

Cytoplasmic Potential

Transmembrane

103 – 123

Helical; Potential

Topological domain

124 – 169

Extracellular Potential

Transmembrane

170 – 190

Helical; Potential

Topological domain

191 – 200

Cytoplasmic Potential

Transmembrane

201 – 221

Helical; Potential

Topological domain

222 – 261

Extracellular Potential

Transmembrane

262 – 282

Helical; Potential

Topological domain

283 – 570

288

Cytoplasmic Potential

Domain

54 – 286

233

Ferric oxidoreductase

Domain

287 – 397

111

FAD-binding FR-type

Nucleotide binding

338 – 344

FAD Potential

Sites

Metal binding

101

Iron (heme axial ligand) Probable

Metal binding

115

Iron (heme axial ligand) Probable

Metal binding

209

Iron (heme axial ligand) Probable

Metal binding

222

Iron (heme axial ligand) Probable

Amino acid modifications

Glycosylation

132

N-linked (GlcNAc...) Potential

Glycosylation

149

N-linked (GlcNAc...) Potential

Glycosylation

247

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

O46522 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 959236166089BCCC
Show »

FASTA

570

65,643

        10         20         30         40         50         60 
MGNWVVNEGI SIFVILVWLG MNVFLFVWYY RVYDIPDKFF YTRKLLGSAL ALARAPAACL 

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

       130        140        150        160        170        180 
FNVEWCVNAR VNNSDPYSIA LSDIGDKPNE TYLNFVRQRI KNPEGGLYVA VTRLAGITGV 

       190        200        210        220        230        240 
VITLCLILII TSSTKTIRRS YFEVFWYTHH LFVIFFIGLA IHGAQRIVRG QTAESLLKHQ 

       250        260        270        280        290        300 
PRNCYQNISQ WGKIENCPIP EFSGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKV 

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

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

       430        440        450        460        470        480 
KSVWYKYCNK APNLRLKKIY FYWLCRDTHA FEWFADLLQL LETQMQEKNN TDFLSYNICL 

       490        500        510        520        530        540 
TGWDESQASH FAMHHDEEKD VITGLKQKTL YGRPNWDNEF KTIGSQHPNT RIGVFLCGPE 

       550        560        570 
ALADTLNKQC ISNSDSGPRG VHFIFNKENF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of the bovine flavocytochrome b subunit proteins, gp91-phox and p22-phox: comparison with other known flavocytochrome b sequences." Davis A.R., Mascolo P.L., Bunger P.L., Sipes K.M., Quinn M.T. J. Leukoc. Biol. 64:114-123(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Thymus.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF036097 mRNA. Translation: AAC27247.1. BC134469 mRNA. Translation: AAI34470.1.
IPI	IPI00716709.
RefSeq	NP_776460.1. NM_174035.4.
UniGene	Bt.4558.
3D structure databases
ProteinModelPortal	O46522.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000026580; ENSBTAP00000026580; ENSBTAG00000019953.
GeneID	281112.
KEGG	bta:281112.
Organism-specific databases
CTD	1536.
Phylogenomic databases
eggNOG	NOG287712.
GeneTree	ENSGT00550000074350.
HOGENOM	HOG000216669.
HOVERGEN	HBG003760.
InParanoid	O46522.
KO	K08008.
OMA	QCCSRTA.
OrthoDB	EOG4J117S.
Family and domain databases
InterPro	IPR000778. 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]
Pfam	PF08022. FAD_binding_8. 1 hit. PF01794. Ferric_reduct. 1 hit. PF08030. NAD_binding_6. 1 hit. [Graphical view]
PRINTS	PR00466. GP91PHOX.
SUPFAM	SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20805183.

Entry information

Entry name

CY24B_BOVIN

Accession

Primary (citable) accession number: O46522
Secondary accession number(s): A4IF96

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents