P97369 (NCF4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neutrophil cytosol factor 4
Short name=NCF-4

Alternative name(s):
Neutrophil NADPH oxidase factor 4
p40-phox
Short name=p40phox

Gene names

Name:

Ncf4

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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.
Subunit structure	p40-PHOX associates primarily with p67-PHOX to form a complex with p47-PHOX.
Subcellular location	Cytoplasm.
Domain	The OPR/PB1 domain mediates the association with NCF2/p67-PHOX By similarity.
Sequence similarities	Contains 1 OPR domain. Contains 1 PX (phox homology) domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	SH3 domain
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell communication Inferred from electronic annotation. Source: InterPro
Cellular_component	NADPH oxidase complex Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay PubMed 15850784. Source: MGI cytosol Inferred from electronic annotation. Source: Compara
Molecular_function	phosphatidylinositol binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 339	339	Neutrophil cytosol factor 4		PRO_0000096765
Regions
	Domain	19 – 140	122	PX
	Domain	170 – 229	60	SH3
	Domain	237 – 329	93	OPR
Amino acid modifications
	Modified residue	154	1	Phosphothreonine By similarity
	Modified residue	315	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	85	1	S → N in AAC53122. Ref.1
	Sequence conflict	85	1	S → N in BAA25651. Ref.2
	Sequence conflict	85	1	S → N in AAH25517. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P97369 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 62C4B8FC2D2C4CB1	FASTA	339	38,707
	10 20 30 40 50 60 MALAQQLRSE SDFEQLPDDV AVSANIADIE EKRGFTSHFV FVIEVKTKGG SKYLIYRRYR 70 80 90 100 110 120 QFYALQSKLE ERFGPESKNS PFTCSLPTLP AKVYMGAKQE IAETRIPALN AYMKNLLSLP 130 140 150 160 170 180 VCVLMDPDVR IFFYQSAYDA EQVPQALRRL RPRTRKIKGV SPQGAIMDRM EAPRAEALFD 190 200 210 220 230 240 FTGNSKLELS FKAGDVIFLL SKINKDWLEG TSQGATGIFP GSFVKILKDF PEDEDTTNWL 250 260 270 280 290 300 RCYFYEDTGK TIKDIAVEED LSSTPLFKDL LALMRREFQR EDIALSYQDA EGDLVRLLSD 310 320 330 EDVGLMVKQA RGLPSQKRLF PWKLHVTQKD NYSVYNTVP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and chromosomal localization of ncf4, the mouse homologue of p40-phox." Zhan S., Kozak C.A., Zhan S., Chanock S.J. Immunogenetics 45:217-219(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Functional modules and expression of mouse p40(phox) and p67(phox), SH3-domain-containing proteins involved in the phagocyte NADPH oxidase complex." Mizuki K., Kadomatsu K., Hata K., Ito T., Fan Q.-W., Kage Y., Fukumaki Y., Sakaki Y., Takeshige K., Sumimoto H. Eur. J. Biochem. 251:573-582(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leukemia.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U59488 mRNA. Translation: AAC53122.1. AB002665 mRNA. Translation: BAA25651.1. AK150510 mRNA. Translation: BAE29623.1. AK171315 mRNA. Translation: BAE42387.1. AL589692 Genomic DNA. Translation: CAP19156.1. CH466545 Genomic DNA. Translation: EDL29666.1. BC025517 mRNA. Translation: AAH25517.1.
IPI	IPI00124203.
RefSeq	NP_032703.2. NM_008677.2.
UniGene	Mm.2068.
3D structure databases
ProteinModelPortal	P97369.
SMR	P97369. Positions 2-339.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2664N.
IntAct	P97369. 1 interaction.
STRING	10090.ENSMUSP00000094084.
PTM databases
PhosphoSite	P97369.
Proteomic databases
PaxDb	P97369.
PRIDE	P97369.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000096357; ENSMUSP00000094084; ENSMUSG00000071715.
GeneID	17972.
KEGG	mmu:17972.
Organism-specific databases
CTD	4689.
MGI	MGI:109186. Ncf4.
Phylogenomic databases
eggNOG	NOG297760.
GeneTree	ENSGT00510000048561.
HOGENOM	HOG000013076.
HOVERGEN	HBG006452.
InParanoid	Q3TBC6.
KO	K08012.
OMA	LFPWKLH.
OrthoDB	EOG41RPVC.
Gene expression databases
ArrayExpress	P97369.
Bgee	P97369.
CleanEx	MM_NCF4.
Genevestigator	P97369.
GermOnline	ENSMUSG00000071715. Mus musculus.
Family and domain databases
Gene3D	3.30.1520.10. 1 hit.
InterPro	IPR000919. NCF_P40. IPR000270. OPR_PB1. IPR001683. Phox. IPR001452. SH3_domain. [Graphical view]
PANTHER	PTHR15552. PTHR15552. 1 hit.
Pfam	PF00564. PB1. 1 hit. PF00787. PX. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00497. P40PHOX. PR00452. SH3DOMAIN.
SMART	SM00666. PB1. 1 hit. SM00312. PX. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF64268. PX. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	PS50195. PX. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	292921.
SOURCE	Search...

Entry information

Entry name

NCF4_MOUSE

Accession

Primary (citable) accession number: P97369
Secondary accession number(s): Q3TBC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program