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Protein

Cytochrome b-245 light chain

Gene

Cyba

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi94 – 941Iron (heme axial ligand)Sequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

ReactomeiR-MMU-1222556. ROS, RNS production in response to bacteria.
R-MMU-1236973. Cross-presentation of particulate exogenous antigens (phagosomes).
R-MMU-3299685. Detoxification of Reactive Oxygen Species.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5668599. RHO GTPases Activate NADPH Oxidases.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b-245 light chain
Alternative name(s):
Cytochrome b(558) alpha chain
Cytochrome b558 subunit alpha
Neutrophil cytochrome b 22 kDa polypeptide
Superoxide-generating NADPH oxidase light chain subunit
p22 phagocyte B-cytochrome
p22-phox
Short name:
p22phox
Gene namesi
Name:Cyba
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1316658. Cyba.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei91 – 12737By similarityAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • cytoplasm Source: MGI
  • dendrite Source: Ensembl
  • endosome Source: MGI
  • Golgi apparatus Source: Ensembl
  • membrane Source: MGI
  • mitochondrion Source: MGI
  • NADPH oxidase complex Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • perinuclear endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show defects in invadopodia biogenesis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 192191Cytochrome b-245 light chainPRO_0000144908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei147 – 1471PhosphothreonineBy similarity
Modified residuei168 – 1681PhosphoserineCombined sources
Modified residuei176 – 1761PhosphoserineCombined sources

Post-translational modificationi

The heme prosthetic group could be coordinated with residues of the light chain, the heavy chain, or both, and it is possible that more than one heme is present per cytochrome b-245.By similarity
Phosphorylation at Thr-147 enhances NADPH oxidase activity by promoting p47phox binding.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ61462.
MaxQBiQ61462.
PaxDbiQ61462.
PRIDEiQ61462.

PTM databases

iPTMnetiQ61462.
PhosphoSiteiQ61462.
SwissPalmiQ61462.

Expressioni

Tissue specificityi

The strongest level of expression is found in kidney, peritoneal neutrophils and peritoneal macrophages, and a lower level in spleen and small intestine. Very low level of expression can be noted in brain, liver, testis, and heart.1 Publication

Gene expression databases

BgeeiQ61462.
CleanExiMM_CYBA.
ExpressionAtlasiQ61462. baseline and differential.
GenevisibleiQ61462. MM.

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 (via SH3 domain). Interacts with DUOX1, DUOX2 and TPO. Interacts with NOX3 and NOX4. Interacts with calprotectin (S100A8/9) (By similarity). Interacts with SH3PXD2A.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198989. 1 interaction.
DIPiDIP-60456N.
STRINGi10090.ENSMUSP00000017604.

Family & Domainsi

Sequence similaritiesi

Belongs to the p22phox family.Curated

Phylogenomic databases

eggNOGiENOG410IXYN. Eukaryota.
ENOG4111MI6. LUCA.
GeneTreeiENSGT00390000002290.
HOGENOMiHOG000001585.
HOVERGENiHBG051278.
InParanoidiQ61462.
KOiK08009.
OMAiGQKYMTK.
OrthoDBiEOG7CZK79.
PhylomeDBiQ61462.
TreeFamiTF328901.

Family and domain databases

InterProiIPR007732. Cyt_b558_asu.
[Graphical view]
PANTHERiPTHR15168. PTHR15168. 1 hit.
PfamiPF05038. Cytochrom_B558a. 1 hit.
[Graphical view]
PIRSFiPIRSF019635. Cytochr_b558a. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q61462-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGQIEWAMWA NEQALASGLI LITGGIVATA GRFTQWYFGA YSIAAGVLIC
60 70 80 90 100
LLEYPRGKRK KGSTMERCGQ KYLTSVVKLF GPLTRNYYVR AALHFLLSVP
110 120 130 140 150
AGFLLATILG TVCLAIASVI YLLAAIRGEQ WTPIEPKPKE RPQVGGTIKQ
160 170 180 190
PPTNPPPRPP AEVRKKPSEG EEEAASAGGP QVNPMPVTDE VV
Length:192
Mass (Da):20,748
Last modified:January 23, 2007 - v3
Checksum:i10DA1F9A54F44E80
GO
Isoform 2 (identifier: Q61462-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-96: CGQKYLTSVVKLFGPLTRNYYVRAALHFL → W

Note: No experimental confirmation available.
Show »
Length:164
Mass (Da):17,593
Checksum:i8B7B5B5CCAC790B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751S → P in BAB32327 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei68 – 9629CGQKY…ALHFL → W in isoform 2. 1 PublicationVSP_001248Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31775 mRNA. Translation: AAA37513.1.
AK018713 mRNA. Translation: BAB31361.1.
AK021200 mRNA. Translation: BAB32327.1.
AK152414 mRNA. Translation: BAE31199.1.
BC026791 mRNA. Translation: AAH26791.1.
CCDSiCCDS22737.1. [Q61462-1]
PIRiA36747.
RefSeqiNP_001288213.1. NM_001301284.1. [Q61462-2]
NP_031832.2. NM_007806.3. [Q61462-1]
UniGeneiMm.271671.

Genome annotation databases

EnsembliENSMUST00000017604; ENSMUSP00000017604; ENSMUSG00000006519. [Q61462-1]
GeneIDi13057.
KEGGimmu:13057.
UCSCiuc009nsp.2. mouse. [Q61462-1]
uc009nsq.2. mouse. [Q61462-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31775 mRNA. Translation: AAA37513.1.
AK018713 mRNA. Translation: BAB31361.1.
AK021200 mRNA. Translation: BAB32327.1.
AK152414 mRNA. Translation: BAE31199.1.
BC026791 mRNA. Translation: AAH26791.1.
CCDSiCCDS22737.1. [Q61462-1]
PIRiA36747.
RefSeqiNP_001288213.1. NM_001301284.1. [Q61462-2]
NP_031832.2. NM_007806.3. [Q61462-1]
UniGeneiMm.271671.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198989. 1 interaction.
DIPiDIP-60456N.
STRINGi10090.ENSMUSP00000017604.

PTM databases

iPTMnetiQ61462.
PhosphoSiteiQ61462.
SwissPalmiQ61462.

Proteomic databases

EPDiQ61462.
MaxQBiQ61462.
PaxDbiQ61462.
PRIDEiQ61462.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017604; ENSMUSP00000017604; ENSMUSG00000006519. [Q61462-1]
GeneIDi13057.
KEGGimmu:13057.
UCSCiuc009nsp.2. mouse. [Q61462-1]
uc009nsq.2. mouse. [Q61462-2]

Organism-specific databases

CTDi1535.
MGIiMGI:1316658. Cyba.

Phylogenomic databases

eggNOGiENOG410IXYN. Eukaryota.
ENOG4111MI6. LUCA.
GeneTreeiENSGT00390000002290.
HOGENOMiHOG000001585.
HOVERGENiHBG051278.
InParanoidiQ61462.
KOiK08009.
OMAiGQKYMTK.
OrthoDBiEOG7CZK79.
PhylomeDBiQ61462.
TreeFamiTF328901.

Enzyme and pathway databases

ReactomeiR-MMU-1222556. ROS, RNS production in response to bacteria.
R-MMU-1236973. Cross-presentation of particulate exogenous antigens (phagosomes).
R-MMU-3299685. Detoxification of Reactive Oxygen Species.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5668599. RHO GTPases Activate NADPH Oxidases.

Miscellaneous databases

PROiQ61462.
SOURCEiSearch...

Gene expression databases

BgeeiQ61462.
CleanExiMM_CYBA.
ExpressionAtlasiQ61462. baseline and differential.
GenevisibleiQ61462. MM.

Family and domain databases

InterProiIPR007732. Cyt_b558_asu.
[Graphical view]
PANTHERiPTHR15168. PTHR15168. 1 hit.
PfamiPF05038. Cytochrom_B558a. 1 hit.
[Graphical view]
PIRSFiPIRSF019635. Cytochr_b558a. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complementary DNA for the mouse homolog of the small subunit of human cytochrome b558."
    Sumimoto H., Nozaki M., Sasaki H., Takeshige K., Sakaki Y., Minakami S.
    Biochem. Biophys. Res. Commun. 165:902-906(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-192 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Macrophage.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Embryonic stem cell and Kidney.
  3. "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] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Tks5-dependent, nox-mediated generation of reactive oxygen species is necessary for invadopodia formation."
    Diaz B., Shani G., Pass I., Anderson D., Quintavalle M., Courtneidge S.A.
    Sci. Signal. 2:RA53-RA53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SH3PXD2A.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung and Spleen.

Entry informationi

Entry nameiCY24A_MOUSE
AccessioniPrimary (citable) accession number: Q61462
Secondary accession number(s): Q3U820, Q9CWB9, Q9D2W2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.