NCF2_MOUSE
ID NCF2_MOUSE Reviewed; 525 AA.
AC O70145; Q3TC92; Q3U5S4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Neutrophil cytosol factor 2;
DE Short=NCF-2;
DE AltName: Full=67 kDa neutrophil oxidase factor;
DE AltName: Full=NADPH oxidase activator 2;
DE AltName: Full=Neutrophil NADPH oxidase factor 2;
DE AltName: Full=p67-phox;
GN Name=Ncf2 {ECO:0000312|MGI:MGI:97284}; Synonyms=Noxa2, P67phox;
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] {ECO:0000312|EMBL:BAA25650.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Myelomonocyte;
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 [2] {ECO:0000312|EMBL:BAC29404.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29404.1}, and
RC NOD {ECO:0000312|EMBL:BAE33191.1};
RC TISSUE=Bone {ECO:0000312|EMBL:BAC29404.1}, Dendritic cell, Macrophage, and
RC Urinary bladder {ECO:0000312|EMBL:BAE23254.1};
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 [3] {ECO:0000312|EMBL:AAH03730.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH03730.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH03730.1};
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233; SER-324 AND SER-398, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, 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 [6]
RP INTERACTION WITH GBP7; NCF4 AND CYBB.
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: NCF2, NCF1, and a membrane bound cytochrome b558 are required
CC for activation of the latent NADPH oxidase (necessary for superoxide
CC production). {ECO:0000250|UniProtKB:P19878}.
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 NCF4 (PubMed:21551061). Interacts (via the C-terminal SH3 domain) with
CC NCF1 (via C-terminus). Interacts with SYTL1 and RAC1. May interact with
CC NOXO1. Interacts with S100A8 and calprotectin (S100A8/9) (By
CC similarity). Interacts with GBP7 (via GB1/RHD3-type G domain)
CC (PubMed:21551061). Interacts with CYBB; the interaction is enhanced in
CC the presence of GBP7 (PubMed:21551061). {ECO:0000250|UniProtKB:P19878,
CC ECO:0000269|PubMed:21551061}.
CC -!- INTERACTION:
CC O70145; O08709: Prdx6; NbExp=3; IntAct=EBI-9550667, EBI-444895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19878}.
CC -!- DOMAIN: The OPR/PB1 domain mediates the association with NCF4/p40-PHOX.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NCF2/NOXA1 family. {ECO:0000305}.
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DR EMBL; AB002664; BAA25650.1; -; mRNA.
DR EMBL; AK036379; BAC29404.1; -; mRNA.
DR EMBL; AK137152; BAE23254.1; -; mRNA.
DR EMBL; AK153447; BAE32002.1; -; mRNA.
DR EMBL; AK155324; BAE33191.1; -; mRNA.
DR EMBL; AK170839; BAE42065.1; -; mRNA.
DR EMBL; AK171059; BAE42218.1; -; mRNA.
DR EMBL; AK171265; BAE42353.1; -; mRNA.
DR EMBL; BC003730; AAH03730.1; -; mRNA.
DR CCDS; CCDS15367.1; -.
DR RefSeq; NP_035007.1; NM_010877.5.
DR RefSeq; XP_006529299.1; XM_006529236.3.
DR AlphaFoldDB; O70145; -.
DR SMR; O70145; -.
DR BioGRID; 201702; 3.
DR IntAct; O70145; 2.
DR STRING; 10090.ENSMUSP00000140404; -.
DR iPTMnet; O70145; -.
DR PhosphoSitePlus; O70145; -.
DR SwissPalm; O70145; -.
DR EPD; O70145; -.
DR jPOST; O70145; -.
DR MaxQB; O70145; -.
DR PaxDb; O70145; -.
DR PeptideAtlas; O70145; -.
DR PRIDE; O70145; -.
DR ProteomicsDB; 252650; -.
DR Antibodypedia; 702; 291 antibodies from 30 providers.
DR DNASU; 17970; -.
DR Ensembl; ENSMUST00000027754; ENSMUSP00000027754; ENSMUSG00000026480.
DR Ensembl; ENSMUST00000186568; ENSMUSP00000140404; ENSMUSG00000026480.
DR GeneID; 17970; -.
DR KEGG; mmu:17970; -.
DR UCSC; uc007czm.1; mouse.
DR CTD; 4688; -.
DR MGI; MGI:97284; Ncf2.
DR VEuPathDB; HostDB:ENSMUSG00000026480; -.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00530000063843; -.
DR HOGENOM; CLU_041290_0_0_1; -.
DR InParanoid; O70145; -.
DR OMA; SKVNQDW; -.
DR OrthoDB; 431898at2759; -.
DR PhylomeDB; O70145; -.
DR TreeFam; TF329087; -.
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; 17970; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ncf2; mouse.
DR PRO; PR:O70145; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O70145; protein.
DR Bgee; ENSMUSG00000026480; Expressed in granulocyte and 64 other tissues.
DR ExpressionAtlas; O70145; baseline and differential.
DR Genevisible; O70145; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043020; C:NADPH oxidase complex; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IPI:MGI.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IDA:MGI.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; ISO:MGI.
DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:MGI.
DR GO; GO:0006742; P:NADP catabolic process; ISO:MGI.
DR GO; GO:0006909; P:phagocytosis; IEA:InterPro.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:0045730; P:respiratory burst; IEA:InterPro.
DR GO; GO:0009749; P:response to glucose; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0042554; P:superoxide anion generation; IDA:MGI.
DR GO; GO:0006801; P:superoxide metabolic process; ISO:MGI.
DR CDD; cd06406; PB1_P67; 1.
DR CDD; cd11871; SH3_p67phox_N; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR034889; P67-PHOX.
DR InterPro; IPR035546; p67phox_SH3_1.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034885; PB1_P67.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR15175:SF3; PTHR15175:SF3; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW TPR repeat.
FT CHAIN 1..525
FT /note="Neutrophil cytosol factor 2"
FT /id="PRO_0000312227"
FT REPEAT 37..70
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 71..104
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 121..154
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT DOMAIN 240..299
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 350..428
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 456..515
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 304..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 31
FT /note="E -> A (in Ref. 2; BAE42353/BAE42218/BAE42065/
FT BAE33191)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="S -> N (in Ref. 2; BAE32002)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 59485 MW; 663DB6B52D790F76 CRC64;
MSLAEAIRLW NEGVLAADKK DWKGALEAFS EVQDPHSRIC FNIGCVNTIL ENLQAAEQAF
TKSINRDKHS AVAYFQRGML YYRMEKYDLA IKDLKEALTQ LRGNQLIDYK ILGLQFKLFA
CEVLYNIALM HAKKEEWKKA EEQLALATNM KSEPRHSKID KAMESIWKQK LFEPVVIPVG
RLFRPNERQV AQLAKKDYLG KATVVASVVH QDNFSGFAPL QPQSAEPPPR PKTPEIFRAL
EGEAHRVLFG FVPETPEELQ VMPGNIVFVL KKGSDNWATV MFNGQKGLVP CNYLEPVELR
IHPQSQPQED TSPESDIPPP PNSSPPGRLQ LSPGHKQKEP KELKLSVPMP YMLKVHYKYT
VVMETRLGLP YSQLRNMVSK KLALSPEHTK LSYRRRDSHE LLLLSEESMK DAWGQVKNYC
LTLWCEHTVG DQGLIDEPIQ RENSDASKQT TEPQPKEGTQ VVAIFSYEAA QPEDLEFVEG
DVILVLSHVN EEWLEGECKG KVGIFPKAFV EGCAAKNLEG IPREV
