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Protein

Neutrophil cytosol factor 2

Gene

Ncf2

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

Functioni

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

GO - Molecular functioni

  1. protein C-terminus binding Source: MGI
  2. Rac GTPase binding Source: MGI

GO - Biological processi

  1. aging Source: Ensembl
  2. cellular response to hormone stimulus Source: Ensembl
  3. NADP catabolic process Source: MGI
  4. oxidation-reduction process Source: GOC
  5. positive regulation of blood pressure Source: Ensembl
  6. positive regulation of neuron apoptotic process Source: Ensembl
  7. response to activity Source: Ensembl
  8. response to drug Source: Ensembl
  9. response to glucose Source: Ensembl
  10. response to hyperoxia Source: Ensembl
  11. response to laminar fluid shear stress Source: Ensembl
  12. response to lipopolysaccharide Source: Ensembl
  13. response to progesterone Source: Ensembl
  14. superoxide anion generation Source: MGI
  15. superoxide metabolic process Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_199093. Cross-presentation of particulate exogenous antigens (phagosomes).
REACT_257088. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutrophil cytosol factor 2
Short name:
NCF-2
Alternative name(s):
67 kDa neutrophil oxidase factor
NADPH oxidase activator 2
Neutrophil NADPH oxidase factor 2
p67-phox
Gene namesi
Name:Ncf2Imported
Synonyms:Noxa2, P67phox
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:97284. Ncf2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. acrosomal vesicle Source: MGI
  2. cytoplasm Source: MGI
  3. cytosol Source: MGI
  4. membrane Source: Ensembl
  5. nucleolus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 525525Neutrophil cytosol factor 2PRO_0000312227Add
BLAST

Proteomic databases

MaxQBiO70145.
PaxDbiO70145.
PRIDEiO70145.

PTM databases

PhosphoSiteiO70145.

Expressioni

Gene expression databases

BgeeiO70145.
CleanExiMM_NCF2.
GenevestigatoriO70145.

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 with NCF4. Interacts (via the C-terminal SH3 domain) with NCF1 (via C-terminus). Interacts with SYTL1 and RAC1. May interact with NOXO1. Interacts with S100A8 and calprotectin (S100A8/9) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Prdx6O087093EBI-9550667,EBI-444895

Protein-protein interaction databases

IntActiO70145. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliO70145.
SMRiO70145. Positions 2-193, 242-297, 351-426, 454-514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati37 – 7034TPR 1Sequence AnalysisAdd
BLAST
Repeati71 – 10434TPR 2Sequence AnalysisAdd
BLAST
Repeati121 – 15434TPR 3Sequence AnalysisAdd
BLAST
Domaini240 – 29960SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini350 – 42879OPRSequence AnalysisAdd
BLAST
Domaini456 – 51560SH3 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The OPR/PB1 domain mediates the association with NCF4/p40-PHOX.By similarity

Sequence similaritiesi

Belongs to the NCF2/NOXA1 family.Curated
Contains 1 OPR domain.Sequence Analysis
Contains 2 SH3 domains.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain, TPR repeat

Phylogenomic databases

eggNOGiNOG248396.
GeneTreeiENSGT00530000063843.
HOGENOMiHOG000237312.
HOVERGENiHBG001521.
InParanoidiO70145.
KOiK08010.
OMAiYSQVRDM.
OrthoDBiEOG7G1V62.
PhylomeDBiO70145.
TreeFamiTF329087.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR000270. OPR_PB1.
IPR001452. SH3_domain.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00564. PB1. 1 hit.
PF00018. SH3_1. 2 hits.
PF00515. TPR_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00666. PB1. 1 hit.
SM00326. SH3. 2 hits.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
PROSITEiPS50002. SH3. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O70145-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLAEAIRLW NEGVLAADKK DWKGALEAFS EVQDPHSRIC FNIGCVNTIL
60 70 80 90 100
ENLQAAEQAF TKSINRDKHS AVAYFQRGML YYRMEKYDLA IKDLKEALTQ
110 120 130 140 150
LRGNQLIDYK ILGLQFKLFA CEVLYNIALM HAKKEEWKKA EEQLALATNM
160 170 180 190 200
KSEPRHSKID KAMESIWKQK LFEPVVIPVG RLFRPNERQV AQLAKKDYLG
210 220 230 240 250
KATVVASVVH QDNFSGFAPL QPQSAEPPPR PKTPEIFRAL EGEAHRVLFG
260 270 280 290 300
FVPETPEELQ VMPGNIVFVL KKGSDNWATV MFNGQKGLVP CNYLEPVELR
310 320 330 340 350
IHPQSQPQED TSPESDIPPP PNSSPPGRLQ LSPGHKQKEP KELKLSVPMP
360 370 380 390 400
YMLKVHYKYT VVMETRLGLP YSQLRNMVSK KLALSPEHTK LSYRRRDSHE
410 420 430 440 450
LLLLSEESMK DAWGQVKNYC LTLWCEHTVG DQGLIDEPIQ RENSDASKQT
460 470 480 490 500
TEPQPKEGTQ VVAIFSYEAA QPEDLEFVEG DVILVLSHVN EEWLEGECKG
510 520
KVGIFPKAFV EGCAAKNLEG IPREV
Length:525
Mass (Da):59,485
Last modified:August 1, 1998 - v1
Checksum:i663DB6B52D790F76
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311E → A in BAE42353 (PubMed:16141072).Curated
Sequence conflicti31 – 311E → A in BAE42218 (PubMed:16141072).Curated
Sequence conflicti31 – 311E → A in BAE42065 (PubMed:16141072).Curated
Sequence conflicti31 – 311E → A in BAE33191 (PubMed:16141072).Curated
Sequence conflicti324 – 3241S → N in BAE32002 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002664 mRNA. Translation: BAA25650.1.
AK036379 mRNA. Translation: BAC29404.1.
AK137152 mRNA. Translation: BAE23254.1.
AK153447 mRNA. Translation: BAE32002.1.
AK155324 mRNA. Translation: BAE33191.1.
AK170839 mRNA. Translation: BAE42065.1.
AK171059 mRNA. Translation: BAE42218.1.
AK171265 mRNA. Translation: BAE42353.1.
BC003730 mRNA. Translation: AAH03730.1.
CCDSiCCDS15367.1.
RefSeqiNP_035007.1. NM_010877.4.
XP_006529298.1. XM_006529235.1.
XP_006529299.1. XM_006529236.1.
UniGeneiMm.270307.

Genome annotation databases

EnsembliENSMUST00000027754; ENSMUSP00000027754; ENSMUSG00000026480.
ENSMUST00000186568; ENSMUSP00000140404; ENSMUSG00000026480.
GeneIDi17970.
KEGGimmu:17970.
UCSCiuc007czm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002664 mRNA. Translation: BAA25650.1.
AK036379 mRNA. Translation: BAC29404.1.
AK137152 mRNA. Translation: BAE23254.1.
AK153447 mRNA. Translation: BAE32002.1.
AK155324 mRNA. Translation: BAE33191.1.
AK170839 mRNA. Translation: BAE42065.1.
AK171059 mRNA. Translation: BAE42218.1.
AK171265 mRNA. Translation: BAE42353.1.
BC003730 mRNA. Translation: AAH03730.1.
CCDSiCCDS15367.1.
RefSeqiNP_035007.1. NM_010877.4.
XP_006529298.1. XM_006529235.1.
XP_006529299.1. XM_006529236.1.
UniGeneiMm.270307.

3D structure databases

ProteinModelPortaliO70145.
SMRiO70145. Positions 2-193, 242-297, 351-426, 454-514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO70145. 2 interactions.

PTM databases

PhosphoSiteiO70145.

Proteomic databases

MaxQBiO70145.
PaxDbiO70145.
PRIDEiO70145.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027754; ENSMUSP00000027754; ENSMUSG00000026480.
ENSMUST00000186568; ENSMUSP00000140404; ENSMUSG00000026480.
GeneIDi17970.
KEGGimmu:17970.
UCSCiuc007czm.1. mouse.

Organism-specific databases

CTDi4688.
MGIiMGI:97284. Ncf2.

Phylogenomic databases

eggNOGiNOG248396.
GeneTreeiENSGT00530000063843.
HOGENOMiHOG000237312.
HOVERGENiHBG001521.
InParanoidiO70145.
KOiK08010.
OMAiYSQVRDM.
OrthoDBiEOG7G1V62.
PhylomeDBiO70145.
TreeFamiTF329087.

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_199093. Cross-presentation of particulate exogenous antigens (phagosomes).
REACT_257088. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

NextBioi292917.
PROiO70145.
SOURCEiSearch...

Gene expression databases

BgeeiO70145.
CleanExiMM_NCF2.
GenevestigatoriO70145.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR000270. OPR_PB1.
IPR001452. SH3_domain.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00564. PB1. 1 hit.
PF00018. SH3_1. 2 hits.
PF00515. TPR_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00666. PB1. 1 hit.
SM00326. SH3. 2 hits.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
PROSITEiPS50002. SH3. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Myelomonocyte.
  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].
    Strain: C57BL/6JImported and NODImported.
    Tissue: BoneImported, Dendritic cell, Macrophage and Urinary bladderImported.
  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].
    Strain: FVB/NImported.
    Tissue: Mammary glandImported.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNCF2_MOUSE
AccessioniPrimary (citable) accession number: O70145
Secondary accession number(s): Q3TC92, Q3U5S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: August 1, 1998
Last modified: March 4, 2015
This is version 122 of the entry and version 1 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.