Reviewed, UniProtKB/Swiss-Prot P14598 (NCF1_HUMAN)

Names and origin

Protein names

Recommended name:
    Neutrophil cytosol factor 1
      Short name=NCF-1
Alternative name(s):
    Neutrophil NADPH oxidase factor 1
    47 kDa neutrophil oxidase factor
    p47-phox
    NCF-47K
    47 kDa autosomal chronic granulomatous disease protein
    Nox-organizing protein 2
    Nox organizer 2
    SH3 and PX domain-containing protein 1A

Gene names

Name:	NCF1
Synonyms:	NOXO2, SH3PXD1A

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).
Subunit structure	Interacts with NOXA1. Ref.16
Subcellular location	Cytoplasm.
Involvement in disease	Defects in NCF1 are the cause of chronic granulomatous disease autosomal recessive cytochrome-b-positive type 1 (CGD1) [MIM:233700]. Chronic granulomatous disease is a genetically heterogeneous disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections. Ref.13 Ref.18
Sequence similarities	Contains 1 PX (phox homology) domain. Contains 2 SH3 domains.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Chronic granulomatous disease Disease mutation
Domain	Repeat SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell communication Inferred from electronic annotation. Source: InterPro cellular defense response Traceable author statement. Source: ProtInc innate immune response Traceable author statement. Source: UniProtKB respiratory burst Traceable author statement. Source: UniProtKB superoxide release Traceable author statement. Source: UniProtKB
Cellular component	NADPH oxidase complex Traceable author statement. Source: UniProtKB cytosol Traceable author statement. Source: ProtInc soluble fraction Traceable author statement. Source: ProtInc
Molecular function	GTP binding Traceable author statement. Source: ProtInc GTPase activity Ref.3 Traceable author statement. Source: ProtInc SH3 domain binding Inferred from physical interaction. Source: UniProtKB electron carrier activity Traceable author statement. Source: UniProtKB phosphoinositide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABI1	Q8IZP0	4	EBI-395044,EBI-375446
CYBA	P13498	4	EBI-395044,EBI-986058

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P14598-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P14598-2)

The sequence of this isoform differs from the canonical sequence as follows:
     193-193: W → QTSHLTGLLP...LDGYGTVCSL
     194-390: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 390

390

Neutrophil cytosol factor 1

PRO_0000096762

Regions

Domain

4 – 125

122

PX

Domain

156 – 215

60

SH3 1

Domain

226 – 285

60

SH3 2

Compositional bias

211 – 254

44

Asp/Glu-rich (highly acidic)

Compositional bias

292 – 390

99

Arg/Lys-rich (highly basic)

Amino acid modifications

Modified residue

303

1

Phosphoserine Ref.15

Modified residue

304

1

Phosphoserine Ref.15

Modified residue

320

1

Phosphoserine Ref.15

Modified residue

328

1

Phosphoserine Ref.15

Modified residue

345

1

Phosphoserine Ref.15

Modified residue

348

1

Phosphoserine Ref.15

Natural variations

Alternative sequence

193

1

W → QTSHLTGLLPLVLRNPQPQA PCQGSGSLAPGRTPALLGAL NVLPTLWVAFCLSVHPVVAV GICAWQAGAGHVCVFCLDGY GTVCSL in isoform 2.

VSP_035032

Alternative sequence

194 – 390

197

Missing in isoform 2.

VSP_035033

Natural variant

42

1

R → Q in CGD1. Ref.18

VAR_012476

Natural variant

90

1

R → H: dbSNP rs13447. Ref.10

VAR_014735

Natural variant

99

1

S → G Ref.10 Ref.11

VAR_018479

Natural variant

160

1

T → S

VAR_012477

Natural variant

166

1

D → N: dbSNP rs4868. Ref.10 Ref.11 Ref.8 Ref.9

VAR_012478

Natural variant

258

1

K → E Ref.7

VAR_018476

Natural variant

262

1

G → S Ref.18

VAR_012479

Natural variant

308

1

A → V: dbSNP rs13739.

VAR_012480

Experimental info

Sequence conflict

200

1

A → T in AAK19516. Ref.7

Secondary structure

1

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390

Helix Strand Turn

Details...

Beta strand

6 – 17

12

Beta strand

19 – 21

3

Beta strand

23 – 32

10

Beta strand

37 – 42

6

Helix

44 – 57

14

Turn

59 – 63

5

Helix

67 – 69

3

Helix

84 – 101

18

Helix

106 – 109

4

Helix

112 – 118

7

Helix

122 – 125

4

Beta strand

137 – 140

4

Beta strand

159 – 165

7

Beta strand

182 – 187

6

Beta strand

192 – 198

7

Beta strand

202 – 206

5

Helix

207 – 209

3

Beta strand

210 – 214

5

Beta strand

229 – 235

7

Beta strand

252 – 257

6

Beta strand

262 – 268

7

Beta strand

271 – 276

6

Helix

277 – 279

3

Beta strand

280 – 282

3

Helix

287 – 292

6

Helix

302 – 304

3

Helix

321 – 328

8

Helix

373 – 376

4

Helix

380 – 385

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1992. Version 2. Checksum: B11B256516F3AA9B	FASTA	390	44,683
	10 20 30 40 50 60 MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI 70 80 90 100 110 120 EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV 130 140 150 160 170 180 RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIADYEKT SGSEMALSTG 190 200 210 220 230 240 DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV 250 260 270 280 290 300 EGDEVSLLEG EAVEVIHKLL DGWWVIRKDD VTGYFPSMYL QKSGQDVSQA QRQIKRGAPP 310 320 330 340 350 360 RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK 370 380 390 PQPAVPPRPS ADLILNRCSE STKRKLASAV
	Isoform 2. Checksum: B8B940F5F5373E7B	FASTA	278	30,812
	10 20 30 40 50 60 MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI 70 80 90 100 110 120 EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV 130 140 150 160 170 180 RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIADYEKT SGSEMALSTG 190 200 210 220 230 240 DVVEVVEKSE SGQTSHLTGL LPLVLRNPQP QAPCQGSGSL APGRTPALLG ALNVLPTLWV 250 260 270 AFCLSVHPVV AVGICAWQAG AGHVCVFCLD GYGTVCSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase." Volpp B.D., Nauseef W.M., Clark R.A. Proc. Natl. Acad. Sci. U.S.A. 86:7195-7199(1989) [PubMed: 2550933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	Erratum Volpp B.D., Nauseef W.M., Clark R.A. Proc. Natl. Acad. Sci. U.S.A. 86:9563-9563(1989) Cited for: SEQUENCE REVISION.
[3]	"Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in chronic granulomatous disease." Lomax K.J., Leto T.L., Nunoi H., Gallin J.I., Malech H.L. Science 245:409-412(1989) [PubMed: 2547247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Characterization of the 47-kilodalton autosomal chronic granulomatous disease protein: tissue-specific expression and transcriptional control by retinoic acid." Rodaway A.R.F., Teahan C.G., Casimir C.M., Segal A.W., Bentley D.L. Mol. Cell. Biol. 10:5388-5396(1990) [PubMed: 2398896] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"A p47-phox pseudogene carries the most common mutation causing p47-phox-deficient chronic granulomatous disease." Gorlach A., Lee P.L., Roesler J., Hopkins P.J., Christensen B., Green E.D., Chanock S.J., Curnutte J.T. J. Clin. Invest. 100:1907-1918(1997) [PubMed: 9329953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Genomic structure of the human p47-phox (NCF1) gene." Chanock S.J., Roesler J., Zhan S., Hopkins P., Lee P., Barrett D.T., Christensen B.L., Curnutte J.T., Goerlach A. Blood Cells Mol. Dis. 26:37-46(2000) [PubMed: 10772875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"TNFalpha activates c-jun amino terminal kinase through p47(phox)." Gu Y., Xu Y.C., Wu R.F., Souza R.F., Nwariaku F.E., Terada L.S. Exp. Cell Res. 272:62-74(2002) [PubMed: 11740866] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-258. Tissue: Umbilical vein.
[8]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ASN-166. Tissue: Spleen and Synovium.
[9]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-166. Tissue: Spleen.
[10]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS HIS-90; GLY-99 AND ASN-166.
[11]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLY-99 AND ASN-166. Tissue: Lymph.
[12]	"Comparison of the positional cloning methods used to isolate the BRCA1 gene." Harshman K., Bell R., Rosenthal J., Katcher H., Miki Y., Swenson J., Gholami Z., Frye C., Ding W., Dayananth P., Eddington K., Norris F.H., Bristow P.K., Phelps R., Hattier T., Stone S., Shaffer D., Bayer S. , Hussey C., Tran T., Lai M., Rosteck P.R. Jr., Skolnick M.H., Shattuck-Eidens D., Kamb A. Hum. Mol. Genet. 4:1259-1266(1995) [PubMed: 7581362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-31 (ISOFORM 1). Tissue: Ovary.
[13]	"Autosomal recessive chronic granulomatous disease caused by deletion at a dinucleotide repeat." Casimir C.M., Bu-Ghanim H.N., Rodaway A.R., Bentley D.L., Rowe P., Segal A.W. Proc. Natl. Acad. Sci. U.S.A. 88:2753-2757(1991) [PubMed: 2011585] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-24, INVOLVEMENT IN CHRONIC GRANULOMATOUS DISEASE.
[14]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-390.
[15]	"The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases." el Benna J., Faust L.P., Babior B.M. J. Biol. Chem. 269:23431-23436(1994) [PubMed: 8089108] [Abstract] Cited for: PHOSPHORYLATION AT SER-303; SER-304; SER-320; SER-328; SER-345 AND SER-348.
[16]	"Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases." Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H., Sumimoto H. J. Biol. Chem. 278:25234-25246(2003) [PubMed: 12716910] [Abstract] Cited for: INTERACTION WITH NOXA1.
[17]	"Solution structure of the PX domain, a target of the SH3 domain." Hiroaki H., Ago T., Ito T., Sumimoto H., Kohda D. Nat. Struct. Biol. 8:526-530(2001) [PubMed: 11373621] [Abstract] Cited for: STRUCTURE BY NMR OF 1-128.
[18]	"Autosomal recessive chronic granulomatous disease caused by defects in NCF1, the gene encoding the phagocyte p47-phox: mutations not arising in the NCF1 pseudogenes." Noack D., Rae J., Cross A.R., Ellis B.A., Newburger P.E., Curnutte J.T., Heyworth P.G. Blood 97:305-311(2001) [PubMed: 11133775] [Abstract] Cited for: VARIANT CGD1 GLN-42, VARIANT SER-262.
+	Additional computationally mapped references.

Web resources

NCF1base

NCF1 deficiency database

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

M25665 mRNA. Translation: AAA57209.1.
M55067 mRNA. Translation: AAA59901.1.
U57835, U57833, U57834 Genomic DNA. Translation: AAB95193.1.
AF184614 Genomic DNA. Translation: AAF34737.1.
AF330625 mRNA. Translation: AAK19516.1.
AF330626 mRNA. Translation: AAK19517.1.
AF330627 mRNA. Translation: AAK19518.1.
AC004883 Genomic DNA. No translation available.
AC083884 Genomic DNA. Translation: AAS07465.1.
AK127905 mRNA. Translation: BAG54596.1. Different initiation.
AK292094 mRNA. Translation: BAF84783.1. Different initiation.
AK223217 mRNA. Translation: BAD96937.1.
AC124781 Genomic DNA. No translation available.
BC002816 mRNA. Translation: AAH02816.1.
BC065731 mRNA. Translation: AAH65731.1.
U25793 mRNA. Translation: AAA93232.1.
DQ314878 Genomic DNA. Translation: ABC40737.1.

IPI

IPI00788186.
IPI00902858.

PIR

A39249. A35926.

RefSeq

NP_000256.3.

UniGene

Hs.647047
Hs.655201

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GD5	NMR	-	A	1-128	[»]
1K4U	NMR	-	P	359-390	[»]
1KQ6	X-ray	1.18	A	1-141	[»]
1NG2	X-ray	1.70	A	156-340	[»]
1O7K	X-ray	2.00	A/B/C	1-123	[»]
1OV3	X-ray	1.80	A/B	156-285	[»]
1UEC	X-ray	1.82	A	151-340	[»]
1W70	X-ray	1.46	C/D	360-372	[»]
1WLP	NMR	-	B	151-286	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:126N.

IntAct

P14598. 3 interactions.

PTM databases

PhosphoSite

P14598.

Proteomic databases

PRIDE

P14598.

Genome annotation databases

Ensembl

ENSG00000165178. Homo sapiens. [Contig view]

GeneID

653361.

KEGG

hsa:653361.

Organism-specific databases

GeneCards

GC07P073826.

H-InvDB

HIX0006771.
HIX0033553.

HGNC

HGNC:7660. NCF1.

MIM

233700. phenotype.
608512. gene.

Orphanet

379. Granulomatous disease, chronic.

PharmGKB

PA31463.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P14598.

Gene expression databases

GermOnline

ENSG00000158517. Homo sapiens.

Family and domain databases

InterPro

IPR015039. NADPH_oxidase_p47Phox_C.
IPR001655. P47PHOX.
IPR001683. PX.
IPR001452. SH3_domain.
[Graphical view]

Gene3D

G3DSA:3.30.1520.10. PX. 1 hit.

PANTHER

PTHR15706:SF3. P47PHOX. 1 hit.

Pfam

PF08944. p47_phox_C. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]

PRINTS

PR00498. P47PHOX.

ProDom

PD000066. SH3. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]

PROSITE

PS50195. PX. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

123127.

SOURCE

Search...

Entry information

Entry name

NCF1_HUMAN

Accession

Primary (citable) accession number: P14598
Secondary accession number(s): A6NEH2 , A8K7S9, O43842, Q2PP07, Q53FR5, Q9BU90, Q9BXI7, Q9BXI8, Q9UDV9, Q9UMU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	May 1, 1992
Last modified:	July 7, 2009
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)