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Neutrophil cytosol factor 4 (NCF-4) (Neutrophil NADPH oxidase factor 4) (SH3 and PX domain-containing protein 4) (p40-phox) (p40phox)

 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.
22-NOV-2017, entry version 185.
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; MINT-206126; -.
STRING; 9606.ENSP00000380334; -.
DrugBank; DB00514; Dextromethorphan.
iPTMnet; Q15080; -.
PhosphoSitePlus; Q15080; -.
BioMuta; NCF4; -.
DMDM; 108884815; -.
MaxQB; Q15080; -.
PaxDb; Q15080; -.
PeptideAtlas; Q15080; -.
PRIDE; Q15080; -.
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; Crohn disease.
PharmGKB; PA31465; -.
eggNOG; KOG4773; Eukaryota.
eggNOG; ENOG410YBFF; LUCA.
GeneTree; ENSGT00510000048561; -.
HOGENOM; HOG000013076; -.
HOVERGEN; HBG006452; -.
InParanoid; Q15080; -.
KO; K08012; -.
OMA; LFPWKLH; -.
OrthoDB; EOG091G0CKP; -.
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; -.
CleanEx; HS_NCF4; -.
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:0005802; C:trans-Golgi network; IBA:GO_Central.
GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; 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:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0045454; P:cell redox homeostasis; TAS:Reactome.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
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:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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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