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Q09014 (NCF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. 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:
Neutrophil cytosol factor 1

Short name=NCF-1
Alternative name(s):
47 kDa neutrophil oxidase factor
NCF-47K
Neutrophil NADPH oxidase factor 1
p47-phox
Gene names
Name:Ncf1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). Ref.2

Subunit structure

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 (via C-terminus) with NCF2 (via the C-terminal SH3 domain). Interacts with NCF4. Interacts with CYBB. Interacts (via the second SH3 domain) with CYBA. Interacts with NOXA1. Interacts with ADAM15. Interacts with TRAF4. Interacts with FASLG By similarity.

Subcellular location

Cytoplasmcytosol By similarity. Membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

Domain

The PX domain mediates interaction with phosphatidylinositol 3,4-bisphosphate and other anionic phospholipids. In the autoinhibited, unphosphorylated state an intramolecular interaction with the C-terminal SH3 domain precludes phospholipid binding and interaction with CYBA. Phosphorylation disrupts the autoinhibited state By similarity.

Post-translational modification

Phosphorylated by PRKCD; phosphorylation induces activation of NCF1 and NADPH oxidase activity By similarity.

Sequence similarities

Contains 1 PX (phox homology) domain.

Contains 2 SH3 domains.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   DomainRepeat
SH3 domain
   LigandLipid-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNADP catabolic process

Inferred from sequence alignment PubMed 10647999. Source: MGI

apoptotic process

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from mutant phenotype PubMed 10987289. Source: MGI

cellular defense response

Inferred from mutant phenotype PubMed 7650482. Source: MGI

defense response to Gram-positive bacterium

Inferred from mutant phenotype PubMed 11907569. Source: MGI

defense response to bacterium

Inferred from mutant phenotype PubMed 17526748PubMed 9116268. Source: MGI

defense response to fungus

Inferred from mutant phenotype PubMed 10714686PubMed 16041040. Source: MGI

hydrogen peroxide biosynthetic process

Inferred from mutant phenotype PubMed 15258578. Source: MGI

inflammatory response

Inferred from mutant phenotype PubMed 11867678. Source: MGI

leukocyte mediated cytotoxicity

Inferred from mutant phenotype PubMed 17526748. Source: MGI

leukotriene metabolic process

Inferred from mutant phenotype PubMed 11867678. Source: MGI

negative regulation of smooth muscle contraction

Inferred from mutant phenotype PubMed 17993584. Source: MGI

neutrophil mediated killing of fungus

Inferred from mutant phenotype PubMed 11907569. Source: MGI

neutrophil mediated killing of gram-positive bacterium

Inferred from mutant phenotype PubMed 11907569. Source: MGI

oxidation-reduction process

Inferred from direct assay Ref.1. Source: GOC

protein targeting to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

respiratory burst

Inferred from mutant phenotype PubMed 15626477. Source: MGI

respiratory burst involved in defense response

Inferred from mutant phenotype PubMed 10714686. Source: MGI

response to bacterium

Inferred from mutant phenotype PubMed 10678931. Source: MGI

response to yeast

Inferred from mutant phenotype PubMed 10714686PubMed 11907569. Source: MGI

superoxide anion generation

Inferred from mutant phenotype PubMed 10725280PubMed 11156938. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

NADPH oxidase complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 11156938PubMed 15850784. Source: MGI

cytosol

Inferred from sequence alignment PubMed 10647999. Source: MGI

dendrite

Inferred from electronic annotation. Source: Ensembl

extrinsic component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionphosphatidylinositol binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3,4-bisphosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

superoxide-generating NADPH oxidase activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Neutrophil cytosol factor 1
PRO_0000096763

Regions

Domain4 – 125122PX
Domain162 – 21554SH3 1
Domain226 – 28560SH3 2
Compositional bias211 – 25444Asp/Glu-rich (highly acidic)
Compositional bias292 – 39099Arg/Lys-rich (highly basic)

Amino acid modifications

Modified residue3041Phosphoserine By similarity
Modified residue3211Phosphoserine By similarity
Modified residue3291Phosphoserine By similarity
Modified residue3461Phosphoserine By similarity

Experimental info

Sequence conflict1611Y → H in AAA50469. Ref.1
Sequence conflict343 – 3453GPL → RAA in AAA50469. Ref.1
Sequence conflict3441P → Q in BAA25649. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q09014 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: C8EFAB953839CE9A

FASTA39044,667
        10         20         30         40         50         60 
MGDTFIRHIA LLGFEKRFIP SQHYVYMFLV KWQDLSEKVV YRKFTEIYEF HKMLKEMFPI 

        70         80         90        100        110        120 
EAGEIHTENR VIPHLPAPRW FDGQRAAESR QGTLTEYFNG LMGLPVKISR CPHLLDFFKV 

       130        140        150        160        170        180 
RPDDLKLPTD SQAKKPETYL VPKDGKNNVA DITGPIILQT YRAIADYEKS SGTEMTVATG 

       190        200        210        220        230        240 
DVVDVVEKSE SGWWFCQMKT KRGWVPASYL EPLDSPDEAE DPDPNYAGEP YVTIKAYAAV 

       250        260        270        280        290        300 
EEDEMSLSEG EAIEVIHKLL DGWWVVRKGD ITGYFPSMYL QKAGEEITQA QRQIRGRGAP 

       310        320        330        340        350        360 
PRRSTIRNAQ SIHQRSRKRL SQDTYRRNSV RFLQQRRRPG RPGPLSTDGT KDNPSTPRVK 

       370        380        390 
PQPAVPPRPS SDLILHRCTE STKRKLTSAV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and functional expression of the mouse homologue of p47phox."
Jackson S.H., Malech H.L., Kozak C.A., Lomax K.J., Gallin J.I., Holland S.M.
Immunogenetics 39:272-275(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Macrophage.
[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], FUNCTION.
Tissue: Leukemia.
[3]Green E.D.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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. expand/collapse author list , 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 and NOD.
Tissue: Bone marrow and Colon.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11455 mRNA. Translation: AAA50469.1.
AB002663 mRNA. Translation: BAA25649.1.
AF267747 Genomic DNA. Translation: AAF90134.1.
AK149668 mRNA. Translation: BAE29014.1.
AK149732 mRNA. Translation: BAE29053.1.
AK152386 mRNA. Translation: BAE31174.1.
AK162308 mRNA. Translation: BAE36845.1.
AK170462 mRNA. Translation: BAE41812.1.
AK171559 mRNA. Translation: BAE42526.1.
CH466529 Genomic DNA. Translation: EDL19452.1.
RefSeqNP_001272966.1. NM_001286037.1.
NP_035006.3. NM_010876.4.
UniGeneMm.425296.

3D structure databases

ProteinModelPortalQ09014.
SMRQ09014. Positions 1-128, 156-333, 360-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-2665N.
IntActQ09014. 2 interactions.
MINTMINT-1649450.

PTM databases

PhosphoSiteQ09014.

Proteomic databases

PaxDbQ09014.
PRIDEQ09014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000111275; ENSMUSP00000106906; ENSMUSG00000015950.
ENSMUST00000146354; ENSMUSP00000138121; ENSMUSG00000015950.
GeneID17969.
KEGGmmu:17969.
UCSCuc008zvh.2. mouse.

Organism-specific databases

CTD653361.
MGIMGI:97283. Ncf1.

Phylogenomic databases

eggNOGNOG326975.
GeneTreeENSGT00530000063010.
HOGENOMHOG000232124.
HOVERGENHBG002055.
KOK08011.
OrthoDBEOG7P02J1.

Gene expression databases

BgeeQ09014.
CleanExMM_NCF1.
GenevestigatorQ09014.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR015039. NADPH_oxidase_p47Phox_C.
IPR001655. P47PHOX.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR15706:SF3. PTHR15706:SF3. 1 hit.
PfamPF08944. p47_phox_C. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSPR00498. P47PHOX.
PR00452. SH3DOMAIN.
SMARTSM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEPS50195. PX. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio292913.
PROQ09014.
SOURCESearch...

Entry information

Entry nameNCF1_MOUSE
AccessionPrimary (citable) accession number: Q09014
Secondary accession number(s): O70144, Q3UE58, Q9JI34
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 116 of the entry and version 3 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