NCF1_RAT
ID NCF1_RAT Reviewed; 389 AA.
AC F1M707;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Neutrophil cytosolic factor 1 {ECO:0000312|RGD:61307};
DE Short=NCF-1;
GN Name=Ncf1 {ECO:0000312|RGD:61307};
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]
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., 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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:P14598,
CC ECO:0000250|UniProtKB:Q09014}.
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 (via C-terminus) with
CC NCF2 (via the C-terminal SH3 domain). Interacts with NCF4. Interacts
CC with CYBB. Interacts (via the second SH3 domain) with CYBA. Interacts
CC with NOXA1. Interacts with ADAM15. Interacts with TRAF4. Interacts with
CC FASLG (By similarity). Interacts with PARK7 (via C-terminus); the
CC interaction is enhanced by LPS and modulates NCF1 phosphorylation and
CC membrane translocation (By similarity). {ECO:0000250|UniProtKB:P14598,
CC ECO:0000250|UniProtKB:Q09014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P14598}. Membrane
CC {ECO:0000250|UniProtKB:P14598}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14598}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P14598}.
CC -!- DOMAIN: The PX domain mediates interaction with phosphatidylinositol
CC 3,4-bisphosphate and other anionic phospholipids. In the autoinhibited,
CC unphosphorylated state an intramolecular interaction with the C-
CC terminal SH3 domain precludes phospholipid binding and interaction with
CC CYBA. Phosphorylation disrupts the autoinhibited state (By similarity).
CC {ECO:0000250|UniProtKB:P14598}.
CC -!- PTM: Phosphorylated by PRKCD; phosphorylation induces activation of
CC NCF1 and NADPH oxidase activity. {ECO:0000250|UniProtKB:P14598}.
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; AABR07035855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473973; EDM13444.1; -; Genomic_DNA.
DR AlphaFoldDB; F1M707; -.
DR SMR; F1M707; -.
DR STRING; 10116.ENSRNOP00000002028; -.
DR iPTMnet; F1M707; -.
DR PaxDb; F1M707; -.
DR PRIDE; F1M707; -.
DR Ensembl; ENSRNOT00000002028; ENSRNOP00000002028; ENSRNOG00000001480.
DR RGD; 61307; Ncf1.
DR eggNOG; KOG4773; Eukaryota.
DR GeneTree; ENSGT00940000160014; -.
DR InParanoid; F1M707; -.
DR OMA; WWVVRKD; -.
DR TreeFam; TF329347; -.
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:F1M707; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Bgee; ENSRNOG00000001480; Expressed in spleen and 18 other tissues.
DR ExpressionAtlas; F1M707; baseline and differential.
DR Genevisible; F1M707; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043020; C:NADPH oxidase complex; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISO:RGD.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; ISO:RGD.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IDA:RGD.
DR GO; GO:0006915; P:apoptotic process; IMP:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0006968; P:cellular defense response; ISO:RGD.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0050832; P:defense response to fungus; ISO:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0001909; P:leukocyte mediated cytotoxicity; ISO:RGD.
DR GO; GO:0006691; P:leukotriene metabolic process; ISO:RGD.
DR GO; GO:0045986; P:negative regulation of smooth muscle contraction; ISO:RGD.
DR GO; GO:0070947; P:neutrophil-mediated killing of fungus; ISO:RGD.
DR GO; GO:0070946; P:neutrophil-mediated killing of gram-positive bacterium; ISO:RGD.
DR GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; ISO:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006612; P:protein targeting to membrane; ISO:RGD.
DR GO; GO:1903409; P:reactive oxygen species biosynthetic process; IMP:RGD.
DR GO; GO:0060264; P:regulation of respiratory burst involved in inflammatory response; IMP:RGD.
DR GO; GO:0045730; P:respiratory burst; IMP:RGD.
DR GO; GO:0002679; P:respiratory burst involved in defense response; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0001878; P:response to yeast; ISO:RGD.
DR GO; GO:0042554; P:superoxide anion generation; ISO:RGD.
DR CDD; cd06887; PX_p47phox; 1.
DR CDD; cd12021; SH3_p47phox_1; 1.
DR CDD; cd12022; SH3_p47phox_2; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR015039; NADPH_oxidase_p47Phox_C.
DR InterPro; IPR035756; NCF1_SH3_1.
DR InterPro; IPR035757; NCF1_SH3_2.
DR InterPro; IPR032136; NECFESHC.
DR InterPro; IPR001655; P47PHOX.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR034909; PX_p47phox.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15706:SF6; PTHR15706:SF6; 1.
DR Pfam; PF16621; NECFESHC; 1.
DR Pfam; PF08944; p47_phox_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 2.
DR PRINTS; PR00498; P47PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..389
FT /note="Neutrophil cytosolic factor 1"
FT /id="PRO_0000433927"
FT DOMAIN 4..125
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 156..215
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 226..285
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 292..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
SQ SEQUENCE 389 AA; 44712 MW; BB71832F5434E80C CRC64;
MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRKFTEIYEF HKMLKEMFPI
EAGEIHTENR VIPHLPAPRW YDGQRAAESR QGTLTEYFNS LMGLPMKISR CPHLLNFFKV
RPDDLKLPND SQVKKPETYL TAKDGKNNVA DITGPIILQT YRAIADYEKG SKTEMTVATG
DVVDVVEKSE SGWWFCQMKT KRGWVPASYL EPLDSPDEAE DPDPNYAGEP YVTIKAYAAV
EEDEVSLSEG EAIEVIHKLL DGWWVVRKGD ITGYFPSMYL QKAGEEITQA QRQIRSRGAP
PRRSTIRNAQ SIHQRSRKRL SQDTYRRNSV RFLQQRRRPA RPGPQSPDSK DNPSTPRAKP
QPAVPPRPSS DLILHRCTES TKRKLTSAV
