NCF1_MOUSE
ID NCF1_MOUSE Reviewed; 390 AA.
AC Q09014; O70144; Q3UE58; Q9JI34;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Neutrophil cytosol factor 1;
DE Short=NCF-1;
DE AltName: Full=47 kDa neutrophil oxidase factor;
DE AltName: Full=NCF-47K;
DE AltName: Full=Neutrophil NADPH oxidase factor 1;
DE AltName: Full=p47-phox;
GN Name=Ncf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Macrophage;
RX PubMed=8119734; DOI=10.1007/bf00188790;
RA Jackson S.H., Malech H.L., Kozak C.A., Lomax K.J., Gallin J.I.,
RA Holland S.M.;
RT "Cloning and functional expression of the mouse homologue of p47phox.";
RL Immunogenetics 39:272-275(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Leukemia;
RX PubMed=9490028; DOI=10.1046/j.1432-1327.1998.2510573.x;
RA Mizuki K., Kadomatsu K., Hata K., Ito T., Fan Q.-W., Kage Y., Fukumaki Y.,
RA Sakaki Y., Takeshige K., Sumimoto H.;
RT "Functional modules and expression of mouse p40(phox) and p67(phox), SH3-
RT domain-containing proteins involved in the phagocyte NADPH oxidase
RT complex.";
RL Eur. J. Biochem. 251:573-582(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Green E.D.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH PARK7, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=26021615; DOI=10.1038/cr.2015.63;
RA Liu W., Wu H., Chen L., Wen Y., Kong X., Gao W.Q.;
RT "Park7 interacts with p47(phox) to direct NADPH oxidase-dependent ROS
RT production and protect against sepsis.";
RL Cell Res. 25:691-706(2015).
CC -!- FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required
CC for activation of the latent NADPH oxidase (necessary for superoxide
CC production). {ECO:0000250|UniProtKB:P14598,
CC ECO:0000269|PubMed:9490028}.
CC -!- SUBUNIT: Component of an NADPH oxidase complex composed of a
CC heterodimer formed by the membrane proteins CYBA and CYBB and the
CC cytosolic subunits NCF1, NCF2 and NCF4. Interacts (via C-terminus) with
CC NCF2 (via the C-terminal SH3 domain). Interacts with NCF4. Interacts
CC with CYBB. Interacts (via the second SH3 domain) with CYBA. Interacts
CC with NOXA1. Interacts with ADAM15. Interacts with TRAF4. Interacts with
CC FASLG (By similarity). Interacts with PARK7 (via C-terminus); the
CC interaction is enhanced by LPS and modulates NCF1 phosphorylation and
CC membrane translocation (PubMed:26021615).
CC {ECO:0000250|UniProtKB:P14598, ECO:0000269|PubMed:26021615}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26021615}.
CC Membrane {ECO:0000269|PubMed:26021615}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14598}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P14598}.
CC -!- DOMAIN: The PX domain mediates interaction with phosphatidylinositol
CC 3,4-bisphosphate and other anionic phospholipids. In the autoinhibited,
CC unphosphorylated state an intramolecular interaction with the C-
CC terminal SH3 domain precludes phospholipid binding and interaction with
CC CYBA. Phosphorylation disrupts the autoinhibited state (By similarity).
CC {ECO:0000250|UniProtKB:P14598}.
CC -!- PTM: Phosphorylated by PRKCD; phosphorylation induces activation of
CC NCF1 and NADPH oxidase activity. {ECO:0000250|UniProtKB:P14598,
CC ECO:0000269|PubMed:26021615}.
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DR EMBL; L11455; AAA50469.1; -; mRNA.
DR EMBL; AB002663; BAA25649.1; -; mRNA.
DR EMBL; AF267747; AAF90134.1; -; Genomic_DNA.
DR EMBL; AK149668; BAE29014.1; -; mRNA.
DR EMBL; AK149732; BAE29053.1; -; mRNA.
DR EMBL; AK152386; BAE31174.1; -; mRNA.
DR EMBL; AK162308; BAE36845.1; -; mRNA.
DR EMBL; AK170462; BAE41812.1; -; mRNA.
DR EMBL; AK171559; BAE42526.1; -; mRNA.
DR EMBL; CH466529; EDL19452.1; -; Genomic_DNA.
DR CCDS; CCDS39298.1; -.
DR RefSeq; NP_001272966.1; NM_001286037.1.
DR RefSeq; NP_035006.3; NM_010876.4.
DR AlphaFoldDB; Q09014; -.
DR SMR; Q09014; -.
DR BioGRID; 201701; 2.
DR DIP; DIP-2665N; -.
DR IntAct; Q09014; 2.
DR STRING; 10090.ENSMUSP00000016094; -.
DR iPTMnet; Q09014; -.
DR PhosphoSitePlus; Q09014; -.
DR SwissPalm; Q09014; -.
DR EPD; Q09014; -.
DR MaxQB; Q09014; -.
DR PaxDb; Q09014; -.
DR PeptideAtlas; Q09014; -.
DR PRIDE; Q09014; -.
DR ProteomicsDB; 252649; -.
DR Antibodypedia; 3863; 954 antibodies from 39 providers.
DR DNASU; 17969; -.
DR Ensembl; ENSMUST00000111275; ENSMUSP00000106906; ENSMUSG00000015950.
DR Ensembl; ENSMUST00000146354; ENSMUSP00000138121; ENSMUSG00000015950.
DR GeneID; 17969; -.
DR KEGG; mmu:17969; -.
DR UCSC; uc008zvh.3; mouse.
DR CTD; 653361; -.
DR MGI; MGI:97283; Ncf1.
DR VEuPathDB; HostDB:ENSMUSG00000015950; -.
DR eggNOG; KOG4773; Eukaryota.
DR GeneTree; ENSGT00940000160014; -.
DR HOGENOM; CLU_030529_0_0_1; -.
DR InParanoid; Q09014; -.
DR OrthoDB; 1183210at2759; -.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 17969; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ncf1; mouse.
DR PRO; PR:Q09014; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q09014; protein.
DR Bgee; ENSMUSG00000015950; Expressed in granulocyte and 132 other tissues.
DR ExpressionAtlas; Q09014; baseline and differential.
DR Genevisible; Q09014; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0043020; C:NADPH oxidase complex; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; ISO:MGI.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0006968; P:cellular defense response; IMP:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0050832; P:defense response to fungus; IMP:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0001909; P:leukocyte mediated cytotoxicity; IMP:MGI.
DR GO; GO:0006691; P:leukotriene metabolic process; IMP:MGI.
DR GO; GO:0006742; P:NADP catabolic process; ISO:MGI.
DR GO; GO:0070947; P:neutrophil-mediated killing of fungus; IMP:MGI.
DR GO; GO:0070946; P:neutrophil-mediated killing of gram-positive bacterium; IMP:MGI.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:1903409; P:reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:0060264; P:regulation of respiratory burst involved in inflammatory response; ISO:MGI.
DR GO; GO:0045730; P:respiratory burst; IMP:MGI.
DR GO; GO:0002679; P:respiratory burst involved in defense response; IMP:MGI.
DR GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR GO; GO:0001878; P:response to yeast; IMP:MGI.
DR GO; GO:0042554; P:superoxide anion generation; IMP:MGI.
DR CDD; cd06887; PX_p47phox; 1.
DR CDD; cd12021; SH3_p47phox_1; 1.
DR CDD; cd12022; SH3_p47phox_2; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR015039; NADPH_oxidase_p47Phox_C.
DR InterPro; IPR035756; NCF1_SH3_1.
DR InterPro; IPR035757; NCF1_SH3_2.
DR InterPro; IPR032136; NECFESHC.
DR InterPro; IPR001655; P47PHOX.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR034909; PX_p47phox.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15706:SF6; PTHR15706:SF6; 1.
DR Pfam; PF16621; NECFESHC; 1.
DR Pfam; PF08944; p47_phox_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 2.
DR PRINTS; PR00498; P47PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid-binding; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain.
FT CHAIN 1..390
FT /note="Neutrophil cytosol factor 1"
FT /id="PRO_0000096763"
FT DOMAIN 4..125
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 156..215
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 226..285
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 291..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT CONFLICT 161
FT /note="Y -> H (in Ref. 1; AAA50469)"
FT /evidence="ECO:0000305"
FT CONFLICT 343..345
FT /note="GPL -> RAA (in Ref. 1; AAA50469)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="P -> Q (in Ref. 2; BAA25649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 44667 MW; C8EFAB953839CE9A CRC64;
MGDTFIRHIA LLGFEKRFIP SQHYVYMFLV KWQDLSEKVV YRKFTEIYEF HKMLKEMFPI
EAGEIHTENR VIPHLPAPRW FDGQRAAESR QGTLTEYFNG LMGLPVKISR CPHLLDFFKV
RPDDLKLPTD SQAKKPETYL VPKDGKNNVA DITGPIILQT YRAIADYEKS SGTEMTVATG
DVVDVVEKSE SGWWFCQMKT KRGWVPASYL EPLDSPDEAE DPDPNYAGEP YVTIKAYAAV
EEDEMSLSEG EAIEVIHKLL DGWWVVRKGD ITGYFPSMYL QKAGEEITQA QRQIRGRGAP
PRRSTIRNAQ SIHQRSRKRL SQDTYRRNSV RFLQQRRRPG RPGPLSTDGT KDNPSTPRVK
PQPAVPPRPS SDLILHRCTE STKRKLTSAV
