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Protein

Neutrophil cytosol factor 1

Gene

Ncf1

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

Functioni

NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell proliferation Source: MGI
  • cellular defense response Source: MGI
  • defense response to bacterium Source: MGI
  • defense response to fungus Source: MGI
  • defense response to Gram-positive bacterium Source: MGI
  • hydrogen peroxide biosynthetic process Source: MGI
  • inflammatory response Source: MGI
  • leukocyte mediated cytotoxicity Source: MGI
  • leukotriene metabolic process Source: MGI
  • NADP catabolic process Source: MGI
  • negative regulation of smooth muscle contraction Source: MGI
  • neutrophil mediated killing of fungus Source: MGI
  • neutrophil mediated killing of gram-positive bacterium Source: MGI
  • oxidation-reduction process Source: MGI
  • protein targeting to membrane Source: UniProtKB
  • respiratory burst Source: MGI
  • respiratory burst involved in defense response Source: MGI
  • response to bacterium Source: MGI
  • response to yeast Source: MGI
  • superoxide anion generation Source: MGI
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_315885. VEGFA-VEGFR2 Pathway.
REACT_321869. Cross-presentation of particulate exogenous antigens (phagosomes).
REACT_358543. RHO GTPases Activate NADPH Oxidases.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ncf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:97283. Ncf1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extrinsic component of membrane Source: UniProtKB
  • NADPH oxidase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Neutrophil cytosol factor 1PRO_0000096763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei304 – 3041PhosphoserineBy similarity
Modified residuei321 – 3211PhosphoserineBy similarity
Modified residuei329 – 3291PhosphoserineBy similarity
Modified residuei346 – 3461PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ09014.
PaxDbiQ09014.
PRIDEiQ09014.

PTM databases

PhosphoSiteiQ09014.

Expressioni

Gene expression databases

BgeeiQ09014.
CleanExiMM_NCF1.
ExpressionAtlasiQ09014. baseline and differential.
GenevisibleiQ09014. 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. 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).By similarity

Protein-protein interaction databases

DIPiDIP-2665N.
IntActiQ09014. 2 interactions.
MINTiMINT-1649450.
STRINGi10090.ENSMUSP00000106906.

Structurei

3D structure databases

ProteinModelPortaliQ09014.
SMRiQ09014. Positions 1-128, 156-333, 360-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 125122PXPROSITE-ProRule annotationAdd
BLAST
Domaini162 – 21554SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini226 – 28560SH3 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi211 – 25444Asp/Glu-rich (highly acidic)Add
BLAST
Compositional biasi292 – 39099Arg/Lys-rich (highly basic)Add
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
Contains 2 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG326975.
GeneTreeiENSGT00530000063010.
HOGENOMiHOG000232124.
HOVERGENiHBG002055.
InParanoidiQ09014.
KOiK08011.
OrthoDBiEOG7P02J1.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR015039. NADPH_oxidase_p47Phox_C.
IPR001655. P47PHOX.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF08944. p47_phox_C. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSiPR00498. P47PHOX.
PR00452. SH3DOMAIN.
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09014-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDTFIRHIA LLGFEKRFIP SQHYVYMFLV KWQDLSEKVV YRKFTEIYEF
60 70 80 90 100
HKMLKEMFPI EAGEIHTENR VIPHLPAPRW FDGQRAAESR QGTLTEYFNG
110 120 130 140 150
LMGLPVKISR CPHLLDFFKV RPDDLKLPTD SQAKKPETYL VPKDGKNNVA
160 170 180 190 200
DITGPIILQT YRAIADYEKS SGTEMTVATG DVVDVVEKSE SGWWFCQMKT
210 220 230 240 250
KRGWVPASYL EPLDSPDEAE DPDPNYAGEP YVTIKAYAAV EEDEMSLSEG
260 270 280 290 300
EAIEVIHKLL DGWWVVRKGD ITGYFPSMYL QKAGEEITQA QRQIRGRGAP
310 320 330 340 350
PRRSTIRNAQ SIHQRSRKRL SQDTYRRNSV RFLQQRRRPG RPGPLSTDGT
360 370 380 390
KDNPSTPRVK PQPAVPPRPS SDLILHRCTE STKRKLTSAV
Length:390
Mass (Da):44,667
Last modified:July 27, 2011 - v3
Checksum:iC8EFAB953839CE9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611Y → H in AAA50469 (PubMed:8119734).Curated
Sequence conflicti343 – 3453GPL → RAA in AAA50469 (PubMed:8119734).Curated
Sequence conflicti344 – 3441P → Q in BAA25649 (PubMed:9490028).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39298.1.
RefSeqiNP_001272966.1. NM_001286037.1.
NP_035006.3. NM_010876.4.
UniGeneiMm.425296.

Genome annotation databases

EnsembliENSMUST00000111275; ENSMUSP00000106906; ENSMUSG00000015950.
ENSMUST00000146354; ENSMUSP00000138121; ENSMUSG00000015950.
GeneIDi17969.
KEGGimmu:17969.
UCSCiuc008zvh.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39298.1.
RefSeqiNP_001272966.1. NM_001286037.1.
NP_035006.3. NM_010876.4.
UniGeneiMm.425296.

3D structure databases

ProteinModelPortaliQ09014.
SMRiQ09014. Positions 1-128, 156-333, 360-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-2665N.
IntActiQ09014. 2 interactions.
MINTiMINT-1649450.
STRINGi10090.ENSMUSP00000106906.

PTM databases

PhosphoSiteiQ09014.

Proteomic databases

MaxQBiQ09014.
PaxDbiQ09014.
PRIDEiQ09014.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000111275; ENSMUSP00000106906; ENSMUSG00000015950.
ENSMUST00000146354; ENSMUSP00000138121; ENSMUSG00000015950.
GeneIDi17969.
KEGGimmu:17969.
UCSCiuc008zvh.3. mouse.

Organism-specific databases

CTDi653361.
MGIiMGI:97283. Ncf1.

Phylogenomic databases

eggNOGiNOG326975.
GeneTreeiENSGT00530000063010.
HOGENOMiHOG000232124.
HOVERGENiHBG002055.
InParanoidiQ09014.
KOiK08011.
OrthoDBiEOG7P02J1.

Enzyme and pathway databases

ReactomeiREACT_315885. VEGFA-VEGFR2 Pathway.
REACT_321869. Cross-presentation of particulate exogenous antigens (phagosomes).
REACT_358543. RHO GTPases Activate NADPH Oxidases.

Miscellaneous databases

NextBioi292913.
PROiQ09014.
SOURCEiSearch...

Gene expression databases

BgeeiQ09014.
CleanExiMM_NCF1.
ExpressionAtlasiQ09014. baseline and differential.
GenevisibleiQ09014. MM.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR015039. NADPH_oxidase_p47Phox_C.
IPR001655. P47PHOX.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF08944. p47_phox_C. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSiPR00498. P47PHOX.
PR00452. SH3DOMAIN.
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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].

Entry informationi

Entry nameiNCF1_MOUSE
AccessioniPrimary (citable) accession number: Q09014
Secondary accession number(s): O70144, Q3UE58, Q9JI34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 130 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

External Data

Dasty 3

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 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.