ID NCF2_RAT Reviewed; 527 AA.
AC A7E3N2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-APR-2013, entry version 45.
DE RecName: Full=Neutrophil cytosol factor 2;
DE Short=NCF-2;
DE AltName: Full=Neutrophil NADPH oxidase factor 2;
GN Name=Ncf2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into
RT mammalian evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION.
RX PubMed=17612411; DOI=10.1186/1471-2148-7-109;
RA Kawahara B.T., Quinn M.T., Lambeth J.D.;
RT "Molecular evolution of the reactive oxygen-generating NADPH oxidase
RT (Nox/Duox) family of enzymes.";
RL BMC Evol. Biol. 7:109-109(2007).
CC -!- FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are
CC required for activation of the latent NADPH oxidase (necessary for
CC superoxide production) (By similarity).
CC -!- SUBUNIT: Interacts with SYTL1 and RAC1. Interacts with NCF4. May
CC interact with NOXO1 (By similarity). Interacts with S100A8 and
CC calprotectin (S100A8/9) (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: The OPR/PB1 domain mediates the association with NCF4/p40-
CC PHOX (By similarity).
CC -!- SIMILARITY: Belongs to the NCF2/NOXA1 family.
CC -!- SIMILARITY: Contains 1 OPR domain.
CC -!- SIMILARITY: Contains 2 SH3 domains.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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DR EMBL; AABR03084702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03088578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BR000294; FAA00361.1; -; mRNA.
DR IPI; IPI00858334; -.
DR RefSeq; NP_001094454.1; NM_001100984.1.
DR UniGene; Rn.162331; -.
DR ProteinModelPortal; A7E3N2; -.
DR SMR; A7E3N2; 1-167, 234-289, 351-429, 456-516.
DR STRING; 10116.ENSRNOP00000038616; -.
DR PRIDE; A7E3N2; -.
DR Ensembl; ENSRNOT00000066331; ENSRNOP00000060733; ENSRNOG00000028016.
DR GeneID; 364018; -.
DR KEGG; rno:364018; -.
DR UCSC; RGD:1309424; rat.
DR CTD; 4688; -.
DR RGD; 1309424; Ncf2.
DR eggNOG; NOG248396; -.
DR GeneTree; ENSGT00530000063843; -.
DR HOGENOM; HOG000237312; -.
DR HOVERGEN; HBG001521; -.
DR KO; K08010; -.
DR OrthoDB; EOG49ZXPC; -.
DR NextBio; 684661; -.
DR Genevestigator; A7E3N2; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Compara.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:Compara.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IDA:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0042493; P:response to drug; IEP:RGD.
DR GO; GO:0009749; P:response to glucose stimulus; IDA:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0034616; P:response to laminar fluid shear stress; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:RGD.
DR GO; GO:0032570; P:response to progesterone stimulus; IEP:RGD.
DR GO; GO:0042554; P:superoxide anion generation; IEA:Compara.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR000270; OPR_PB1.
DR InterPro; IPR000108; p67phox.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001440; TPR-1.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF00515; TPR_1; 1.
DR PRINTS; PR00499; P67PHOX.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF50044; SH3; 2.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS50005; TPR; FALSE_NEG.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Cytoplasm; Reference proteome; Repeat; SH3 domain;
KW TPR repeat.
FT CHAIN 1 527 Neutrophil cytosol factor 2.
FT /FTId=PRO_0000312228.
FT REPEAT 37 70 TPR 1.
FT REPEAT 72 104 TPR 2.
FT REPEAT 119 152 TPR 3.
FT DOMAIN 232 291 SH3 1.
FT DOMAIN 352 430 OPR.
FT DOMAIN 458 517 SH3 2.
SQ SEQUENCE 527 AA; 59573 MW; E025D50A0BA222E5 CRC64;
MSLAEAIRLW NEGVQAADKK DWKGALEAFS EVQDPHSRIC FNIGCMYTIL DNLQEAEQAF
TKSINRDKHL AVAYFQRGML YYSMEKYRPA SVGRKAALLF LGSYNLVARI IVGYPLSPGK
VLYNIALMHA KKEEWKKAEE QLALATNMKS EPRHSKIDKA MESIWKRCPT SHLPLDPPQV
TMALWFEEGG VGKRSVVASV VHQDNFSGFA PLQPQSAEPP PRPKTPEIFR ALEGEAHRVL
FGFVPETPEE LQVMPGNIVF VLKKGSDNWA TVMFNGQKGL VPCNYLEPVE LRIHPQSQPQ
EDTSLESDIP PPPNSSPPER LQLSPGWCQQ LGPLRCPPFL LHQEVKRSVP MPYMLKVHYK
YTVVMETQLG LPYSQLRNMV SKKLELLPEH TKLSYQRRDS PELLLLSEES MKDAWAQVKN
YCLTLWCEHT VGDQGFVDEP KEKENSDADN RTTEPQPKEG TQVVAIFSYD ATQPEDLEFV
EGDVILVLSH VNEEWLEGEC KGKIGIFPKA FVEGCAAKNL EGTPREV
//
