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Protein

Neutrophil cytosol factor 4

Gene

Ncf4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Lipid-binding

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-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5668599. RHO GTPases Activate NADPH Oxidases.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutrophil cytosol factor 4
Short name:
NCF-4
Alternative name(s):
Neutrophil NADPH oxidase factor 4
p40-phox
Short name:
p40phox
Gene namesi
Name:Ncf4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:109186. Ncf4.

Subcellular locationi

  • Cytoplasmcytosol By similarity
  • Endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • endosome membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • NADPH oxidase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339Neutrophil cytosol factor 4PRO_0000096765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541PhosphothreonineBy similarity
Modified residuei315 – 3151PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP97369.
MaxQBiP97369.
PaxDbiP97369.
PeptideAtlasiP97369.
PRIDEiP97369.

PTM databases

iPTMnetiP97369.
PhosphoSiteiP97369.

Expressioni

Gene expression databases

BgeeiP97369.
CleanExiMM_NCF4.
ExpressionAtlasiP97369. baseline and differential.
GenevisibleiP97369. MM.

Interactioni

Subunit structurei

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. NCF4 interacts primarily with NCF2 to form a complex with NCF1 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-2664N.
IntActiP97369. 1 interaction.
STRINGi10090.ENSMUSP00000094084.

Structurei

3D structure databases

ProteinModelPortaliP97369.
SMRiP97369. Positions 2-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 140122PXPROSITE-ProRule annotationAdd
BLAST
Domaini170 – 22960SH3PROSITE-ProRule annotationAdd
BLAST
Domaini237 – 32993PB1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 603Phosphatidylinositol 3-phosphate bindingBy similarity
Regioni92 – 943Phosphatidylinositol 3-phosphate bindingBy similarity

Domaini

The PB1 domain mediates the association with NCF2/p67-PHOX.By similarity
The PX domain mediates interaction with membranes enriched in phosphatidylnositol 3-phosphate.By similarity

Sequence similaritiesi

Contains 1 PB1 domain.PROSITE-ProRule annotation
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiENOG410IRR2. Eukaryota.
ENOG41101A3. LUCA.
GeneTreeiENSGT00510000048561.
HOGENOMiHOG000013076.
HOVERGENiHBG006452.
InParanoidiP97369.
KOiK08012.
OMAiLMRREFQ.
OrthoDBiEOG7H792H.
TreeFamiTF330850.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR000919. NCF_P40.
IPR000270. PB1_dom.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00564. PB1. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00497. P40PHOX.
PR00452. SH3DOMAIN.
SMARTiSM00666. PB1. 1 hit.
SM00312. PX. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEiPS51745. PB1. 1 hit.
PS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97369-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALAQQLRSE SDFEQLPDDV AVSANIADIE EKRGFTSHFV FVIEVKTKGG
60 70 80 90 100
SKYLIYRRYR QFYALQSKLE ERFGPESKNS PFTCSLPTLP AKVYMGAKQE
110 120 130 140 150
IAETRIPALN AYMKNLLSLP VCVLMDPDVR IFFYQSAYDA EQVPQALRRL
160 170 180 190 200
RPRTRKIKGV SPQGAIMDRM EAPRAEALFD FTGNSKLELS FKAGDVIFLL
210 220 230 240 250
SKINKDWLEG TSQGATGIFP GSFVKILKDF PEDEDTTNWL RCYFYEDTGK
260 270 280 290 300
TIKDIAVEED LSSTPLFKDL LALMRREFQR EDIALSYQDA EGDLVRLLSD
310 320 330
EDVGLMVKQA RGLPSQKRLF PWKLHVTQKD NYSVYNTVP
Length:339
Mass (Da):38,707
Last modified:July 27, 2011 - v2
Checksum:i62C4B8FC2D2C4CB1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851S → N in AAC53122 (PubMed:8995189).Curated
Sequence conflicti85 – 851S → N in BAA25651 (PubMed:9490028).Curated
Sequence conflicti85 – 851S → N in AAH25517 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59488 mRNA. Translation: AAC53122.1.
AB002665 mRNA. Translation: BAA25651.1.
AK150510 mRNA. Translation: BAE29623.1.
AK171315 mRNA. Translation: BAE42387.1.
AL589692 Genomic DNA. Translation: CAP19156.1.
CH466545 Genomic DNA. Translation: EDL29666.1.
BC025517 mRNA. Translation: AAH25517.1.
CCDSiCCDS27610.1.
RefSeqiNP_032703.2. NM_008677.2.
XP_006520627.1. XM_006520564.1.
XP_006520628.1. XM_006520565.2.
UniGeneiMm.2068.

Genome annotation databases

EnsembliENSMUST00000096357; ENSMUSP00000094084; ENSMUSG00000071715.
GeneIDi17972.
KEGGimmu:17972.
UCSCiuc007wow.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59488 mRNA. Translation: AAC53122.1.
AB002665 mRNA. Translation: BAA25651.1.
AK150510 mRNA. Translation: BAE29623.1.
AK171315 mRNA. Translation: BAE42387.1.
AL589692 Genomic DNA. Translation: CAP19156.1.
CH466545 Genomic DNA. Translation: EDL29666.1.
BC025517 mRNA. Translation: AAH25517.1.
CCDSiCCDS27610.1.
RefSeqiNP_032703.2. NM_008677.2.
XP_006520627.1. XM_006520564.1.
XP_006520628.1. XM_006520565.2.
UniGeneiMm.2068.

3D structure databases

ProteinModelPortaliP97369.
SMRiP97369. Positions 2-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-2664N.
IntActiP97369. 1 interaction.
STRINGi10090.ENSMUSP00000094084.

PTM databases

iPTMnetiP97369.
PhosphoSiteiP97369.

Proteomic databases

EPDiP97369.
MaxQBiP97369.
PaxDbiP97369.
PeptideAtlasiP97369.
PRIDEiP97369.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000096357; ENSMUSP00000094084; ENSMUSG00000071715.
GeneIDi17972.
KEGGimmu:17972.
UCSCiuc007wow.2. mouse.

Organism-specific databases

CTDi4689.
MGIiMGI:109186. Ncf4.

Phylogenomic databases

eggNOGiENOG410IRR2. Eukaryota.
ENOG41101A3. LUCA.
GeneTreeiENSGT00510000048561.
HOGENOMiHOG000013076.
HOVERGENiHBG006452.
InParanoidiP97369.
KOiK08012.
OMAiLMRREFQ.
OrthoDBiEOG7H792H.
TreeFamiTF330850.

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-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5668599. RHO GTPases Activate NADPH Oxidases.

Miscellaneous databases

PROiP97369.
SOURCEiSearch...

Gene expression databases

BgeeiP97369.
CleanExiMM_NCF4.
ExpressionAtlasiP97369. baseline and differential.
GenevisibleiP97369. MM.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR000919. NCF_P40.
IPR000270. PB1_dom.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00564. PB1. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00497. P40PHOX.
PR00452. SH3DOMAIN.
SMARTiSM00666. PB1. 1 hit.
SM00312. PX. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEiPS51745. PB1. 1 hit.
PS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and chromosomal localization of ncf4, the mouse homologue of p40-phox."
    Zhan S., Kozak C.A., Zhan S., Chanock S.J.
    Immunogenetics 45:217-219(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, FUNCTION.
  2. "Functional modules and expression of mouse p40(phox) and p67(phox), SH3-domain-containing proteins involved in the phagocyte NADPH oxidase complex."
    Mizuki K., Kadomatsu K., Hata K., Ito T., Fan Q.-W., Kage Y., Fukumaki Y., Sakaki Y., Takeshige K., Sumimoto H.
    Eur. J. Biochem. 251:573-582(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leukemia.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: FVB/N.
    Tissue: Mammary gland.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Spleen.

Entry informationi

Entry nameiNCF4_MOUSE
AccessioniPrimary (citable) accession number: P97369
Secondary accession number(s): Q3TBC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 138 of the entry and version 2 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.