NCF2_RAT
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-AUG-2022, entry version 98.
DE RecName: Full=Neutrophil cytosol factor 2;
DE Short=NCF-2;
DE AltName: Full=Neutrophil NADPH oxidase factor 2;
GN Name=Ncf2 {ECO:0000312|EMBL:FAA00361.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
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., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., 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., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., 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., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|EMBL:FAA00361.1}
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 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. Interacts with NCF4. Interacts
CC (via the C-terminal SH3 domain) with NCF1 (via C-terminus). Interacts
CC with SYTL1 and RAC1. May interact with NOXO1. Interacts with S100A8 and
CC calprotectin (S100A8/9) (By similarity). Interacts with GBP7 (via
CC GB1/RHD3-type G domain) (By similarity). Interacts with CYBB; the
CC interaction is enhanced in the presence of GBP7 (By similarity).
CC {ECO:0000250|UniProtKB:O70145, ECO:0000250|UniProtKB:P19878}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 RefSeq; NP_001094454.1; NM_001100984.1.
DR AlphaFoldDB; A7E3N2; -.
DR SMR; A7E3N2; -.
DR STRING; 10116.ENSRNOP00000060733; -.
DR iPTMnet; A7E3N2; -.
DR PhosphoSitePlus; A7E3N2; -.
DR PaxDb; A7E3N2; -.
DR PeptideAtlas; A7E3N2; -.
DR GeneID; 364018; -.
DR KEGG; rno:364018; -.
DR UCSC; RGD:1309424; rat.
DR CTD; 4688; -.
DR RGD; 1309424; Ncf2.
DR eggNOG; KOG4225; Eukaryota.
DR InParanoid; A7E3N2; -.
DR OrthoDB; 431898at2759; -.
DR PhylomeDB; A7E3N2; -.
DR TreeFam; TF329087; -.
DR Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-RNO-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:A7E3N2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043020; C:NADPH oxidase complex; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IDA:RGD.
DR GO; GO:0006909; P:phagocytosis; IEA:InterPro.
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:1903426; P:regulation of reactive oxygen species biosynthetic process; IMP:RGD.
DR GO; GO:0045730; P:respiratory burst; IEA:InterPro.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; 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:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0042554; P:superoxide anion generation; ISO:RGD.
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; IPR019734; TPR_repeat.
DR PANTHER; PTHR15175:SF3; PTHR15175:SF3; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF13181; TPR_8; 1.
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; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW TPR repeat.
FT CHAIN 1..527
FT /note="Neutrophil cytosol factor 2"
FT /id="PRO_0000312228"
FT REPEAT 37..70
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 72..104
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 119..152
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT DOMAIN 232..291
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 352..430
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 458..517
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 297..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70145"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70145"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70145"
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
