GENTAUR Molecular Products.

 NCF4_HUMAN              Reviewed;         339 AA.
 Q15080; A8K4F9; O60808; Q86U56; Q9BU98; Q9NP45;
 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
 30-MAY-2006, sequence version 2.
 13-FEB-2019, entry version 192.
 RecName: Full=Neutrophil cytosol factor 4;
          Short=NCF-4;
 AltName: Full=Neutrophil NADPH oxidase factor 4;
 AltName: Full=SH3 and PX domain-containing protein 4;
 AltName: Full=p40-phox;
          Short=p40phox;
 Name=NCF4; Synonyms=SH3PXD4;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
 LOCATION, VARIANT ILE-147, AND PARTIAL PROTEIN SEQUENCE.
 PubMed=8280052; DOI=10.1042/bj2960557;
 Wientjes F.B., Hsuan J.J., Totty N.F., Segal A.W.;
 "p40phox, a third cytosolic component of the activation complex of the
 NADPH oxidase to contain src homology 3 domains.";
 Biochem. J. 296:557-561(1993).
 [2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-147.
 PubMed=8839867;
 Zhan S., Vazquez N., Zhan S., Wientjes F.B., Budarf M.L., Schrock E.,
 Ried T., Green E.D., Chanock S.J.;
 "Genomic structure, chromosomal localization, start of transcription,
 and tissue expression of the human p40-phox, a new component of the
 nicotinamide adenine dinucleotide phosphate-oxidase complex.";
 Blood 88:2714-2721(1996).
 [3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
 PubMed=10437784; DOI=10.1016/S0014-5793(99)00905-9;
 Hasebe T., Someya A., Nagaoka I.;
 "Identification of a splice variant mRNA of p40phox, an NADPH oxidase
 component of phagocytes.";
 FEBS Lett. 455:257-261(1999).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
 PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
 Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
 Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
 Beare D.M., Dunham I.;
 "A genome annotation-driven approach to cloning the human ORFeome.";
 Genome Biol. 5:R84.1-R84.11(2004).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
 Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
 Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
 Phelan M., Farmer A.;
 "Cloning of human full-length CDSs in BD Creator(TM) system donor
 vector.";
 Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
 PubMed=14702039; DOI=10.1038/ng1285;
 Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
 Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
 Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
 Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
 Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
 Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
 Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
 Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
 Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
 Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
 Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
 Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
 Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
 Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
 Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
 Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
 Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
 Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
 Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
 Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
 Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
 Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
 Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
 Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
 Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
 Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
 Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
 Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
 "Complete sequencing and characterization of 21,243 full-length human
 cDNAs.";
 Nat. Genet. 36:40-45(2004).
 [7]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 NHLBI resequencing and genotyping service (RS&G);
 Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
 [8]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=10591208; DOI=10.1038/990031;
 Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
 Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
 Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
 Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
 Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
 Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
 Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
 Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
 Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
 Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
 Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
 Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
 Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
 Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
 Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
 Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
 Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
 Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
 Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
 Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
 Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
 Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
 Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
 Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
 Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
 Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
 Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
 Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
 Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
 Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
 Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
 Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
 Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
 Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
 Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
 Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
 Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
 Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
 Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
 O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
 Khan A.S., Lane L., Tilahun Y., Wright H.;
 "The DNA sequence of human chromosome 22.";
 Nature 402:489-495(1999).
 [9]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
 TISSUE=Lymph;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [10]
 PHOSPHORYLATION AT THR-154 AND SER-315, AND MUTAGENESIS OF THR-154;
 THR-211; THR-251; THR-274; SER-315 AND THR-327.
 PubMed=9804763; DOI=10.1074/jbc.273.46.30097;
 Bouin A.-P., Grandvaux N., Vignais P.V., Fuchs A.;
 "p40(phox) is phosphorylated on threonine 154 and serine 315 during
 activation of the phagocyte NADPH oxidase. Implication of a protein
 kinase c-type kinase in the phosphorylation process.";
 J. Biol. Chem. 273:30097-30103(1998).
 [11]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-144 IN COMPLEX WITH
 PHOSPHATIDYLINOSITOL 3-PHOSPHATE, SUBCELLULAR LOCATION, DOMAIN,
 MUTAGENESIS OF ARG-58; ARG-60; LYS-92; TYR-94 AND ARG-105, AND
 LIPID-BINDING.
 PubMed=11684018; DOI=10.1016/S1097-2765(01)00372-0;
 Bravo J., Karathanassis D., Pacold C.M., Pacold M.E., Ellson C.D.,
 Anderson K.E., Butler P.J.G., Lavenir I., Perisic O., Hawkins P.T.,
 Stephens L., Williams R.L.;
 "The crystal structure of the PX domain from p40(phox) bound to
 phosphatidylinositol 3-phosphate.";
 Mol. Cell 8:829-839(2001).
 [12]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 237-339 IN COMPLEX WITH NCF2,
 AND INTERACTION WITH NCF2.
 PubMed=12887891; DOI=10.1016/S1097-2765(03)00246-6;
 Wilson M.I., Gill D.J., Perisic O., Quinn M.T., Williams R.L.;
 "PB1 domain-mediated heterodimerization in NADPH oxidase and signaling
 complexes of atypical protein kinase C with Par6 and p62.";
 Mol. Cell 12:39-50(2003).
 [13]
 X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 174-228 IN COMPLEX WITH
 NCF1, AND INTERACTION WITH NCF1.
 PubMed=15657040; DOI=10.1074/jbc.M412897200;
 Massenet C., Chenavas S., Cohen-Addad C., Dagher M.-C., Brandolin G.,
 Pebay-Peyroula E., Fieschi F.;
 "Effects of p47phox C terminus phosphorylations on binding
 interactions with p40phox and p67phox. Structural and functional
 comparison of p40phox and p67phox SH3 domains.";
 J. Biol. Chem. 280:13752-13761(2005).
 [14]
 X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS), AND DOMAIN OPR/PB1.
 PubMed=17290225; DOI=10.1038/sj.emboj.7601561;
 Honbou K., Minakami R., Yuzawa S., Takeya R., Suzuki N.N.,
 Kamakura S., Sumimoto H., Inagaki F.;
 "Full-length p40phox structure suggests a basis for regulation
 mechanism of its membrane binding.";
 EMBO J. 26:1176-1186(2007).
 [15]
 VARIANT CGD3 GLN-105, AND CHARACTERIZATION OF VARIANT CGD3 GLN-105.
 PubMed=19692703; DOI=10.1182/blood-2009-07-231498;
 Matute J.D., Arias A.A., Wright N.A., Wrobel I., Waterhouse C.C.,
 Li X.J., Marchal C.C., Stull N.D., Lewis D.B., Steele M.,
 Kellner J.D., Yu W., Meroueh S.O., Nauseef W.M., Dinauer M.C.;
 "A new genetic subgroup of chronic granulomatous disease with
 autosomal recessive mutations in p40 phox and selective defects in
 neutrophil NADPH oxidase activity.";
 Blood 114:3309-3315(2009).
 -!- FUNCTION: Component of the NADPH-oxidase, a multicomponent enzyme
     system responsible for the oxidative burst in which electrons are
     transported from NADPH to molecular oxygen, generating reactive
     oxidant intermediates. It may be important for the assembly and/or
     activation of the NADPH-oxidase complex.
     {ECO:0000269|PubMed:8280052}.
 -!- SUBUNIT: 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. NCF4 interacts primarily
     with NCF2 to form a complex with NCF1.
     {ECO:0000269|PubMed:11684018, ECO:0000269|PubMed:12887891,
     ECO:0000269|PubMed:15657040, ECO:0000269|PubMed:8280052}.
 -!- INTERACTION:
     P14598:NCF1; NbExp=2; IntAct=EBI-1036870, EBI-395044;
     P19878:NCF2; NbExp=5; IntAct=EBI-1036870, EBI-489611;
 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
     {ECO:0000269|PubMed:8280052}. Endosome membrane
     {ECO:0000269|PubMed:11684018}; Peripheral membrane protein
     {ECO:0000269|PubMed:11684018}; Cytoplasmic side
     {ECO:0000269|PubMed:11684018}. Membrane
     {ECO:0000269|PubMed:11684018}; Peripheral membrane protein
     {ECO:0000269|PubMed:11684018}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=2;
     Name=1;
       IsoId=Q15080-1; Sequence=Displayed;
     Name=3;
       IsoId=Q15080-3; Sequence=VSP_042681;
       Note=Variant in position: 272:L->P (in dbSNP:rs2075939).;
 -!- TISSUE SPECIFICITY: Expression is restricted to hematopoietic
     cells.
 -!- DOMAIN: The PB1 domain mediates the association with NCF2/p67-
     PHOX.
 -!- DOMAIN: The PX domain mediates interaction with membranes enriched
     in phosphatidylnositol 3-phosphate.
 -!- DISEASE: Granulomatous disease, chronic, cytochrome-b-positive 3,
     autosomal recessive (CGD3) [MIM:613960]: A disorder characterized
     by the inability of neutrophils and phagocytes to kill microbes
     that they have ingested. Patients suffer from life-threatening
     bacterial/fungal infections. {ECO:0000269|PubMed:19692703}.
     Note=The disease is caused by mutations affecting the gene
     represented in this entry.
 -----------------------------------------------------------------------
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 EMBL; X77094; CAA54372.1; -; mRNA.
 EMBL; U50729; AAB39970.1; -; Genomic_DNA.
 EMBL; U50720; AAB39970.1; JOINED; Genomic_DNA.
 EMBL; U50721; AAB39970.1; JOINED; Genomic_DNA.
 EMBL; U50722; AAB39970.1; JOINED; Genomic_DNA.
 EMBL; U50723; AAB39970.1; JOINED; Genomic_DNA.
 EMBL; U50724; AAB39970.1; JOINED; Genomic_DNA.
 EMBL; U50725; AAB39970.1; JOINED; Genomic_DNA.
 EMBL; U50726; AAB39970.1; JOINED; Genomic_DNA.
 EMBL; U50727; AAB39970.1; JOINED; Genomic_DNA.
 EMBL; U50728; AAB39970.1; JOINED; Genomic_DNA.
 EMBL; AB025220; BAA89792.1; -; mRNA.
 EMBL; AB025219; BAA89791.1; -; mRNA.
 EMBL; CR456528; CAG30414.1; -; mRNA.
 EMBL; BT007346; AAP36010.1; -; mRNA.
 EMBL; AK290924; BAF83613.1; -; mRNA.
 EMBL; DQ314880; ABC40739.1; -; Genomic_DNA.
 EMBL; AL008637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; BC002798; AAH02798.1; -; mRNA.
 CCDS; CCDS13934.1; -. [Q15080-1]
 CCDS; CCDS13935.1; -. [Q15080-3]
 PIR; S39768; S39768.
 RefSeq; NP_000622.2; NM_000631.4. [Q15080-1]
 RefSeq; NP_038202.2; NM_013416.3. [Q15080-3]
 UniGene; Hs.474781; -.
 PDB; 1H6H; X-ray; 1.70 A; A=2-144.
 PDB; 1OEY; X-ray; 2.00 A; J/K/L/M=237-339.
 PDB; 1W6X; X-ray; 2.00 A; A/B=174-228.
 PDB; 1W70; X-ray; 1.46 A; A/B=174-228.
 PDB; 1Z9Q; NMR; -; A=168-233.
 PDB; 2DYB; X-ray; 3.15 A; A/B=1-339.
 PDBsum; 1H6H; -.
 PDBsum; 1OEY; -.
 PDBsum; 1W6X; -.
 PDBsum; 1W70; -.
 PDBsum; 1Z9Q; -.
 PDBsum; 2DYB; -.
 ProteinModelPortal; Q15080; -.
 SMR; Q15080; -.
 BioGrid; 110769; 6.
 DIP; DIP-17019N; -.
 IntAct; Q15080; 5.
 MINT; Q15080; -.
 STRING; 9606.ENSP00000380334; -.
 DrugBank; DB00514; Dextromethorphan.
 iPTMnet; Q15080; -.
 PhosphoSitePlus; Q15080; -.
 BioMuta; NCF4; -.
 DMDM; 108884815; -.
 jPOST; Q15080; -.
 MaxQB; Q15080; -.
 PaxDb; Q15080; -.
 PeptideAtlas; Q15080; -.
 PRIDE; Q15080; -.
 ProteomicsDB; 60430; -.
 ProteomicsDB; 60432; -. [Q15080-3]
 DNASU; 4689; -.
 Ensembl; ENST00000248899; ENSP00000248899; ENSG00000100365. [Q15080-1]
 Ensembl; ENST00000397147; ENSP00000380334; ENSG00000100365. [Q15080-3]
 GeneID; 4689; -.
 KEGG; hsa:4689; -.
 UCSC; uc003apy.5; human. [Q15080-1]
 CTD; 4689; -.
 DisGeNET; 4689; -.
 EuPathDB; HostDB:ENSG00000100365.14; -.
 GeneCards; NCF4; -.
 GeneReviews; NCF4; -.
 HGNC; HGNC:7662; NCF4.
 HPA; CAB010146; -.
 HPA; HPA036156; -.
 HPA; HPA057975; -.
 MalaCards; NCF4; -.
 MIM; 601488; gene.
 MIM; 613960; phenotype.
 neXtProt; NX_Q15080; -.
 OpenTargets; ENSG00000100365; -.
 Orphanet; 379; Chronic granulomatous disease.
 Orphanet; 206; NON RARE IN EUROPE: Crohn disease.
 PharmGKB; PA31465; -.
 eggNOG; KOG4773; Eukaryota.
 eggNOG; ENOG410YBFF; LUCA.
 GeneTree; ENSGT00510000048561; -.
 HOGENOM; HOG000013076; -.
 HOVERGEN; HBG006452; -.
 InParanoid; Q15080; -.
 KO; K08012; -.
 OMA; FPWKLHV; -.
 OrthoDB; 824942at2759; -.
 PhylomeDB; Q15080; -.
 Reactome; R-HSA-1222556; ROS, RNS production in phagocytes.
 Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
 Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
 Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
 Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
 SIGNOR; Q15080; -.
 ChiTaRS; NCF4; human.
 EvolutionaryTrace; Q15080; -.
 GenomeRNAi; 4689; -.
 PRO; PR:Q15080; -.
 Proteomes; UP000005640; Chromosome 22.
 Bgee; ENSG00000100365; Expressed in 162 organ(s), highest expression level in blood.
 ExpressionAtlas; Q15080; baseline and differential.
 Genevisible; Q15080; HS.
 GO; GO:0005829; C:cytosol; IDA:UniProtKB.
 GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
 GO; GO:0016020; C:membrane; IDA:UniProtKB.
 GO; GO:0043020; C:NADPH oxidase complex; IDA:UniProtKB.
 GO; GO:0032010; C:phagolysosome; TAS:Reactome.
 GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
 GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
 GO; GO:0046983; F:protein dimerization activity; TAS:UniProtKB.
 GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IMP:UniProtKB.
 GO; GO:0006955; P:immune response; TAS:UniProtKB.
 GO; GO:0055114; P:oxidation-reduction process; TAS:UniProtKB.
 GO; GO:0006909; P:phagocytosis; IEA:InterPro.
 GO; GO:0045730; P:respiratory burst; IEA:InterPro.
 GO; GO:0006801; P:superoxide metabolic process; IBA:GO_Central.
 GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
 CDD; cd06399; PB1_P40; 1.
 CDD; cd06882; PX_p40phox; 1.
 CDD; cd11869; SH3_p40phox; 1.
 Gene3D; 3.30.1520.10; -; 1.
 InterPro; IPR000919; p40phox.
 InterPro; IPR035541; p40phox_SH3.
 InterPro; IPR000270; PB1_dom.
 InterPro; IPR034853; PB1_P40.
 InterPro; IPR001683; Phox.
 InterPro; IPR036871; PX_dom_sf.
 InterPro; IPR034912; PX_p40phox.
 InterPro; IPR036028; SH3-like_dom_sf.
 InterPro; IPR001452; SH3_domain.
 PANTHER; PTHR44898; PTHR44898; 1.
 Pfam; PF00564; PB1; 1.
 Pfam; PF00787; PX; 1.
 Pfam; PF00018; SH3_1; 1.
 PRINTS; PR00497; P40PHOX.
 SMART; SM00666; PB1; 1.
 SMART; SM00312; PX; 1.
 SMART; SM00326; SH3; 1.
 SUPFAM; SSF50044; SSF50044; 1.
 SUPFAM; SSF64268; SSF64268; 1.
 PROSITE; PS51745; PB1; 1.
 PROSITE; PS50195; PX; 1.
 PROSITE; PS50002; SH3; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Chronic granulomatous disease;
 Complete proteome; Cytoplasm; Direct protein sequencing;
 Disease mutation; Endosome; Lipid-binding; Membrane; Phosphoprotein;
 Polymorphism; Reference proteome; SH3 domain.
 CHAIN         1    339       Neutrophil cytosol factor 4.
                              /FTId=PRO_0000096764.
 DOMAIN       19    140       PX. {ECO:0000255|PROSITE-
                              ProRule:PRU00147}.
 DOMAIN      170    229       SH3. {ECO:0000255|PROSITE-
                              ProRule:PRU00192}.
 DOMAIN      237    329       PB1. {ECO:0000255|PROSITE-
                              ProRule:PRU01081}.
 REGION       58     60       Phosphatidylinositol 3-phosphate binding.
 REGION       92     94       Phosphatidylinositol 3-phosphate binding.
 MOD_RES     154    154       Phosphothreonine.
                              {ECO:0000269|PubMed:9804763}.
 MOD_RES     315    315       Phosphoserine.
                              {ECO:0000269|PubMed:9804763}.
 VAR_SEQ     254    339       DIAVEEDLSSTPLLKDLLELTRREFQREDIALNYRDAEGDL
                              VRLLSDEDVALMVRQARGLPSQKRLFPWKLHITQKDNYRVY
                              NTMP -> SVAWEGGACPAFLPSLRPLPLTSPSHGSLSHSK
                              APSGSQMSHNAVTSHQRPGWPGQPHSPFPHPTPHFQPDASL
                              LQPVTPLGTSRWRKISAALPY (in isoform 3).
                              {ECO:0000303|PubMed:10437784,
                              ECO:0000303|PubMed:14702039,
                              ECO:0000303|PubMed:15489334,
                              ECO:0000303|Ref.5}.
                              /FTId=VSP_042681.
 VARIANT     105    105       R -> Q (in CGD3; the protein remains
                              cytosolic, does not localize to
                              phagosomes or endosomes and is unable to
                              bind phosphatidylinositol 3-phosphate
                              (PtdIns(3)P) in a lipid-binding assay;
                              unable to rescue the NADPH-oxidase defect
                              of NCF4 functionally null cells;
                              dbSNP:rs387906808).
                              {ECO:0000269|PubMed:19692703}.
                              /FTId=VAR_065949.
 VARIANT     147    147       L -> I. {ECO:0000269|PubMed:8280052,
                              ECO:0000269|PubMed:8839867}.
                              /FTId=VAR_009314.
 VARIANT     153    153       R -> H (in dbSNP:rs35160112).
                              /FTId=VAR_034136.
 MUTAGEN      58     58       R->Q: Abolishes interaction with
                              membranes enriched in
                              phosphatidylinositol 3-phosphate.
                              {ECO:0000269|PubMed:11684018}.
 MUTAGEN      60     60       R->A: Strongly reduces interaction with
                              membranes enriched in
                              phosphatidylinositol 3-phosphate.
                              {ECO:0000269|PubMed:11684018}.
 MUTAGEN      92     92       K->A: Abolishes interaction with
                              membranes enriched in
                              phosphatidylinositol 3-phosphate.
                              {ECO:0000269|PubMed:11684018}.
 MUTAGEN      94     94       Y->A: Slightly reduces interaction with
                              membranes enriched in
                              phosphatidylinositol 3-phosphate.
                              {ECO:0000269|PubMed:11684018}.
 MUTAGEN     105    105       R->A: Abolishes interaction with
                              membranes enriched in
                              phosphatidylinositol 3-phosphate.
                              {ECO:0000269|PubMed:11684018}.
 MUTAGEN     154    154       T->A: Reduces phosphorylation.
                              {ECO:0000269|PubMed:9804763}.
 MUTAGEN     211    211       T->A: No effect on phosphorylation.
                              {ECO:0000269|PubMed:9804763}.
 MUTAGEN     251    251       T->A: No effect on phosphorylation.
                              {ECO:0000269|PubMed:9804763}.
 MUTAGEN     274    274       T->A: No effect on phosphorylation.
                              {ECO:0000269|PubMed:9804763}.
 MUTAGEN     315    315       S->A: Reduces phosphorylation.
                              {ECO:0000269|PubMed:9804763}.
 MUTAGEN     327    327       T->A: No effect on phosphorylation.
                              {ECO:0000269|PubMed:9804763}.
 HELIX         3     15       {ECO:0000244|PDB:1H6H}.
 STRAND       21     32       {ECO:0000244|PDB:1H6H}.
 STRAND       34     36       {ECO:0000244|PDB:1H6H}.
 STRAND       38     47       {ECO:0000244|PDB:1H6H}.
 STRAND       52     58       {ECO:0000244|PDB:1H6H}.
 HELIX        59     73       {ECO:0000244|PDB:1H6H}.
 HELIX        80     82       {ECO:0000244|PDB:1H6H}.
 HELIX        98    116       {ECO:0000244|PDB:1H6H}.
 HELIX       121    124       {ECO:0000244|PDB:1H6H}.
 HELIX       127    133       {ECO:0000244|PDB:1H6H}.
 HELIX       137    140       {ECO:0000244|PDB:1H6H}.
 STRAND      174    179       {ECO:0000244|PDB:1W70}.
 STRAND      184    188       {ECO:0000244|PDB:2DYB}.
 STRAND      196    202       {ECO:0000244|PDB:1W70}.
 STRAND      204    212       {ECO:0000244|PDB:1W70}.
 STRAND      215    220       {ECO:0000244|PDB:1W70}.
 HELIX       221    223       {ECO:0000244|PDB:1W70}.
 STRAND      224    226       {ECO:0000244|PDB:1W70}.
 STRAND      238    246       {ECO:0000244|PDB:1OEY}.
 STRAND      249    257       {ECO:0000244|PDB:1OEY}.
 HELIX       267    278       {ECO:0000244|PDB:1OEY}.
 STRAND      281    288       {ECO:0000244|PDB:1OEY}.
 STRAND      290    292       {ECO:0000244|PDB:2DYB}.
 STRAND      294    296       {ECO:0000244|PDB:1OEY}.
 HELIX       300    309       {ECO:0000244|PDB:1OEY}.
 STRAND      324    328       {ECO:0000244|PDB:1OEY}.
 SEQUENCE   339 AA;  39032 MW;  D82FE9E5BA12890B CRC64;
 MAVAQQLRAE SDFEQLPDDV AISANIADIE EKRGFTSHFV FVIEVKTKGG SKYLIYRRYR
 QFHALQSKLE ERFGPDSKSS ALACTLPTLP AKVYVGVKQE IAEMRIPALN AYMKSLLSLP
 VWVLMDEDVR IFFYQSPYDS EQVPQALRRL RPRTRKVKSV SPQGNSVDRM AAPRAEALFD
 FTGNSKLELN FKAGDVIFLL SRINKDWLEG TVRGATGIFP LSFVKILKDF PEEDDPTNWL
 RCYYYEDTIS TIKDIAVEED LSSTPLLKDL LELTRREFQR EDIALNYRDA EGDLVRLLSD
 EDVALMVRQA RGLPSQKRLF PWKLHITQKD NYRVYNTMP

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