NCF4_MOUSE
ID NCF4_MOUSE Reviewed; 339 AA.
AC P97369; Q3TBC6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Neutrophil cytosol factor 4;
DE Short=NCF-4;
DE AltName: Full=Neutrophil NADPH oxidase factor 4;
DE AltName: Full=p40-phox;
DE Short=p40phox;
GN Name=Ncf4;
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], SUBUNIT, AND FUNCTION.
RX PubMed=8995189; DOI=10.1007/s002510050192;
RA Zhan S., Kozak C.A., Zhan S., Chanock S.J.;
RT "Cloning and chromosomal localization of ncf4, the mouse homologue of p40-
RT phox.";
RL Immunogenetics 45:217-219(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and 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 [8]
RP INTERACTION WITH NCF2 AND GBP7.
RX PubMed=21551061; DOI=10.1126/science.1201711;
RA Kim B.H., Shenoy A.R., Kumar P., Das R., Tiwari S., MacMicking J.D.;
RT "A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial
RT infection.";
RL Science 332:717-721(2011).
CC -!- FUNCTION: Component of the NADPH-oxidase, a multicomponent enzyme
CC system responsible for the oxidative burst in which electrons are
CC transported from NADPH to molecular oxygen, generating reactive oxidant
CC intermediates. It may be important for the assembly and/or activation
CC of the NADPH-oxidase complex. {ECO:0000269|PubMed:8995189}.
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 (By similarity). Interacts with
CC NCF2 (PubMed:21551061). Interacts wirh NCF1 (By similarity). The NCF2-
CC NCF4 complex interacts with GBP7 (via GB1/RHD3-type G domain)
CC (PubMed:21551061). {ECO:0000250|UniProtKB:Q15080,
CC ECO:0000269|PubMed:21551061}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q15080}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q15080}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15080}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15080}. Membrane
CC {ECO:0000250|UniProtKB:Q15080}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15080}.
CC -!- DOMAIN: The PB1 domain mediates the association with NCF2/p67-PHOX.
CC {ECO:0000250}.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylnositol 3-phosphate. {ECO:0000250}.
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DR EMBL; U59488; AAC53122.1; -; mRNA.
DR EMBL; AB002665; BAA25651.1; -; mRNA.
DR EMBL; AK150510; BAE29623.1; -; mRNA.
DR EMBL; AK171315; BAE42387.1; -; mRNA.
DR EMBL; AL589692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466545; EDL29666.1; -; Genomic_DNA.
DR EMBL; BC025517; AAH25517.1; -; mRNA.
DR CCDS; CCDS27610.1; -.
DR RefSeq; NP_032703.2; NM_008677.2.
DR RefSeq; XP_006520627.1; XM_006520564.1.
DR RefSeq; XP_006520628.1; XM_006520565.2.
DR AlphaFoldDB; P97369; -.
DR SMR; P97369; -.
DR BioGRID; 201703; 10.
DR DIP; DIP-2664N; -.
DR IntAct; P97369; 1.
DR STRING; 10090.ENSMUSP00000094084; -.
DR iPTMnet; P97369; -.
DR PhosphoSitePlus; P97369; -.
DR EPD; P97369; -.
DR MaxQB; P97369; -.
DR PaxDb; P97369; -.
DR PeptideAtlas; P97369; -.
DR PRIDE; P97369; -.
DR ProteomicsDB; 286158; -.
DR Antibodypedia; 11797; 543 antibodies from 39 providers.
DR DNASU; 17972; -.
DR Ensembl; ENSMUST00000096357; ENSMUSP00000094084; ENSMUSG00000071715.
DR GeneID; 17972; -.
DR KEGG; mmu:17972; -.
DR UCSC; uc007wow.2; mouse.
DR CTD; 4689; -.
DR MGI; MGI:109186; Ncf4.
DR VEuPathDB; HostDB:ENSMUSG00000071715; -.
DR eggNOG; KOG4773; Eukaryota.
DR GeneTree; ENSGT00510000048561; -.
DR HOGENOM; CLU_068185_0_0_1; -.
DR InParanoid; P97369; -.
DR OMA; KLHVTQQ; -.
DR OrthoDB; 1045726at2759; -.
DR PhylomeDB; P97369; -.
DR TreeFam; TF330850; -.
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; 17972; 4 hits in 72 CRISPR screens.
DR PRO; PR:P97369; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P97369; protein.
DR Bgee; ENSMUSG00000071715; Expressed in granulocyte and 109 other tissues.
DR ExpressionAtlas; P97369; baseline and differential.
DR Genevisible; P97369; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043020; C:NADPH oxidase complex; ISO:MGI.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; ISS:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEA:InterPro.
DR GO; GO:0045730; P:respiratory burst; IEA:InterPro.
DR GO; GO:0042554; P:superoxide anion generation; ISO:MGI.
DR CDD; cd06399; PB1_P40; 1.
DR CDD; cd06882; PX_p40phox; 1.
DR CDD; cd11869; SH3_p40phox; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR000919; p40phox.
DR InterPro; IPR035541; p40phox_SH3.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034853; PB1_P40.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR034912; PX_p40phox.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15706:SF20; PTHR15706:SF20; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00497; P40PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endosome; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..339
FT /note="Neutrophil cytosol factor 4"
FT /id="PRO_0000096765"
FT DOMAIN 19..140
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 170..229
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 237..329
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT BINDING 58..60
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 92..94
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15080"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15080"
FT CONFLICT 85
FT /note="S -> N (in Ref. 1; AAC53122, 2; BAA25651 and 6;
FT AAH25517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 38707 MW; 62C4B8FC2D2C4CB1 CRC64;
MALAQQLRSE SDFEQLPDDV AVSANIADIE EKRGFTSHFV FVIEVKTKGG SKYLIYRRYR
QFYALQSKLE ERFGPESKNS PFTCSLPTLP AKVYMGAKQE IAETRIPALN AYMKNLLSLP
VCVLMDPDVR IFFYQSAYDA EQVPQALRRL RPRTRKIKGV SPQGAIMDRM EAPRAEALFD
FTGNSKLELS FKAGDVIFLL SKINKDWLEG TSQGATGIFP GSFVKILKDF PEDEDTTNWL
RCYFYEDTGK TIKDIAVEED LSSTPLFKDL LALMRREFQR EDIALSYQDA EGDLVRLLSD
EDVGLMVKQA RGLPSQKRLF PWKLHVTQKD NYSVYNTVP
