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Q09014

- NCF1_MOUSE

UniProt

Q09014 - NCF1_MOUSE

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Protein
Neutrophil cytosol factor 1
Gene
Ncf1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. phosphatidylinositol binding Source: UniProtKB
  2. phosphatidylinositol-3,4-bisphosphate binding Source: UniProtKB
  3. protein binding Source: MGI
  4. superoxide-generating NADPH oxidase activity Source: MGI

GO - Biological processi

  1. NADP catabolic process Source: MGI
  2. apoptotic process Source: Ensembl
  3. cell proliferation Source: MGI
  4. cellular defense response Source: MGI
  5. defense response to Gram-positive bacterium Source: MGI
  6. defense response to bacterium Source: MGI
  7. defense response to fungus Source: MGI
  8. hydrogen peroxide biosynthetic process Source: MGI
  9. inflammatory response Source: MGI
  10. leukocyte mediated cytotoxicity Source: MGI
  11. leukotriene metabolic process Source: MGI
  12. negative regulation of smooth muscle contraction Source: MGI
  13. neutrophil mediated killing of fungus Source: MGI
  14. neutrophil mediated killing of gram-positive bacterium Source: MGI
  15. oxidation-reduction process Source: GOC
  16. protein targeting to membrane Source: UniProtKB
  17. respiratory burst Source: MGI
  18. respiratory burst involved in defense response Source: MGI
  19. response to bacterium Source: MGI
  20. response to yeast Source: MGI
  21. superoxide anion generation Source: MGI
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_199093. Cross-presentation of particulate exogenous antigens (phagosomes).

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: Chromosome 5

Organism-specific databases

MGIiMGI:97283. Ncf1.

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. NADPH oxidase complex Source: UniProtKB
  3. cytoplasm Source: MGI
  4. cytosol Source: MGI
  5. dendrite Source: Ensembl
  6. extrinsic component of membrane Source: UniProtKB
  7. neuronal cell body Source: Ensembl
  8. rough endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei304 – 3041Phosphoserine By similarity
Modified residuei321 – 3211Phosphoserine By similarity
Modified residuei329 – 3291Phosphoserine By similarity
Modified residuei346 – 3461Phosphoserine By 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.
GenevestigatoriQ09014.

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.

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 125122PX
Add
BLAST
Domaini162 – 21554SH3 1
Add
BLAST
Domaini226 – 28560SH3 2
Add
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.

Sequence similaritiesi

Contains 2 SH3 domains.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG326975.
GeneTreeiENSGT00530000063010.
HOGENOMiHOG000232124.
HOVERGENiHBG002055.
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

MGDTFIRHIA LLGFEKRFIP SQHYVYMFLV KWQDLSEKVV YRKFTEIYEF    50
HKMLKEMFPI EAGEIHTENR VIPHLPAPRW FDGQRAAESR QGTLTEYFNG 100
LMGLPVKISR CPHLLDFFKV RPDDLKLPTD SQAKKPETYL VPKDGKNNVA 150
DITGPIILQT YRAIADYEKS SGTEMTVATG DVVDVVEKSE SGWWFCQMKT 200
KRGWVPASYL EPLDSPDEAE DPDPNYAGEP YVTIKAYAAV EEDEMSLSEG 250
EAIEVIHKLL DGWWVVRKGD ITGYFPSMYL QKAGEEITQA QRQIRGRGAP 300
PRRSTIRNAQ SIHQRSRKRL SQDTYRRNSV RFLQQRRRPG RPGPLSTDGT 350
KDNPSTPRVK PQPAVPPRPS SDLILHRCTE STKRKLTSAV 390
Length:390
Mass (Da):44,667
Last modified:July 27, 2011 - v3
Checksum:iC8EFAB953839CE9A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611Y → H in AAA50469. 1 Publication
Sequence conflicti343 – 3453GPL → RAA in AAA50469. 1 Publication
Sequence conflicti344 – 3441P → Q in BAA25649. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS39298.1.
RefSeqi NP_001272966.1. NM_001286037.1.
NP_035006.3. NM_010876.4.
UniGenei Mm.425296.

3D structure databases

ProteinModelPortali Q09014.
SMRi Q09014. Positions 1-128, 156-333, 360-390.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-2665N.
IntActi Q09014. 2 interactions.
MINTi MINT-1649450.

PTM databases

PhosphoSitei Q09014.

Proteomic databases

MaxQBi Q09014.
PaxDbi Q09014.
PRIDEi Q09014.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000111275 ; ENSMUSP00000106906 ; ENSMUSG00000015950 .
ENSMUST00000146354 ; ENSMUSP00000138121 ; ENSMUSG00000015950 .
GeneIDi 17969.
KEGGi mmu:17969.
UCSCi uc008zvh.2. mouse.

Organism-specific databases

CTDi 653361.
MGIi MGI:97283. Ncf1.

Phylogenomic databases

eggNOGi NOG326975.
GeneTreei ENSGT00530000063010.
HOGENOMi HOG000232124.
HOVERGENi HBG002055.
KOi K08011.
OrthoDBi EOG7P02J1.

Enzyme and pathway databases

Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).
REACT_199093. Cross-presentation of particulate exogenous antigens (phagosomes).

Miscellaneous databases

NextBioi 292913.
PROi Q09014.
SOURCEi Search...

Gene expression databases

Bgeei Q09014.
CleanExi MM_NCF1.
Genevestigatori Q09014.

Family and domain databases

Gene3Di 3.30.1520.10. 1 hit.
InterProi IPR015039. NADPH_oxidase_p47Phox_C.
IPR001655. P47PHOX.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF08944. p47_phox_C. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view ]
PRINTSi PR00498. P47PHOX.
PR00452. SH3DOMAIN.
SMARTi SM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEi PS50195. PX. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 120 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