KRAF1_DROME
ID KRAF1_DROME Reviewed; 739 AA.
AC P11346; A8JUV5; Q0KHW7; Q8I086; Q8I0D9; Q8ISE1; Q8ISE2; Q8ISE3; Q9NEH9;
AC Q9W4Z3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 6.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Raf homolog serine/threonine-protein kinase Raf {ECO:0000303|PubMed:3135183};
DE Short=D-Raf {ECO:0000303|PubMed:8423783};
DE Short=dRAF-1 {ECO:0000303|PubMed:3135183};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P15056};
DE AltName: Full=Protein pole-hole {ECO:0000312|FlyBase:FBgn0003079};
GN Name=Raf {ECO:0000303|PubMed:3135183, ECO:0000312|FlyBase:FBgn0003079};
GN Synonyms=ph {ECO:0000312|FlyBase:FBgn0003079},
GN phl {ECO:0000312|FlyBase:FBgn0003079};
GN ORFNames=CG2845 {ECO:0000312|FlyBase:FBgn0003079};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=3135183; DOI=10.1002/j.1460-2075.1988.tb02875.x;
RA Nishida Y., Hata M., Ayaki T., Ryo H., Yamagata M., Shimizu K.,
RA Nishizuka Y.;
RT "Proliferation of both somatic and germ cells is affected in the Drosophila
RT mutants of raf proto-oncogene.";
RL EMBO J. 7:775-781(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-739, AND VARIANTS LEU-322; THR-327;
RP ARG-360 AND THR-465.
RC STRAIN=5-17-88b#5, AA1, AA16, AA18, AA20, AA3, AM2, CA2, G5b, JS, KK1, KK2,
RC KK3, KK4, KKb2, KLGC5, KLH4, KLH6, KM1, KMb1, PYR2, and Reids2;
RX PubMed=12694293; DOI=10.1046/j.1365-294x.2003.01741.x;
RA Riley R.M., Jin W., Gibson G.;
RT "Contrasting selection pressures on components of the Ras-mediated signal
RT transduction pathway in Drosophila.";
RL Mol. Ecol. 12:1315-1323(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 423-711.
RX PubMed=3037346; DOI=10.1128/mcb.7.6.2134-2140.1987;
RA Mark G.E., Macintyre R.J., Digan M.E., Ambrosio L., Perrimon N.;
RT "Drosophila melanogaster homologs of the raf oncogene.";
RL Mol. Cell. Biol. 7:2134-2140(1987).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RX PubMed=8423783; DOI=10.1128/mcb.13.2.1163-1172.1993;
RA Sprenger F., Torsoclair M.M., Morrison D.K.;
RT "Biochemical analysis of torso and D-raf during Drosophila embryogenesis:
RT implications for terminal signal transduction.";
RL Mol. Cell. Biol. 13:1163-1172(1993).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19965758; DOI=10.1126/science.1176450;
RA Rewitz K.F., Yamanaka N., Gilbert L.I., O'Connor M.B.;
RT "The insect neuropeptide PTTH activates receptor tyrosine kinase torso to
RT initiate metamorphosis.";
RL Science 326:1403-1405(2009).
RN [11]
RP ACTIVITY REGULATION, AND INTERACTION WITH KSR AND DSOR1.
RX PubMed=29433126; DOI=10.1038/nature25478;
RA Lavoie H., Sahmi M., Maisonneuve P., Marullo S.A., Thevakumaran N., Jin T.,
RA Kurinov I., Sicheri F., Therrien M.;
RT "MEK drives BRAF activation through allosteric control of KSR proteins.";
RL Nature 554:549-553(2018).
CC -!- FUNCTION: Serine/threonine kinase required in the early embryo for the
CC formation of terminal structure (PubMed:3135183, PubMed:8423783). Also
CC required during the proliferation of imaginal cells (PubMed:3135183).
CC May act downstream of Ras85D in the tor signal transduction pathway
CC (PubMed:8423783). During larval development, mediates Ptth/tor
CC signaling leading to the production of ecdysone, a hormone required for
CC the initiation of metamorphosis (PubMed:19965758).
CC {ECO:0000269|PubMed:19965758, ECO:0000269|PubMed:8423783}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P15056};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P15056};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: In quiescent cells, maintained in an inactive
CC state via an intramolecular interaction between the protein kinase and
CC N-terminal domains (By similarity). Following mitogen-mediated cell
CC activation, binds via its RGB domain to active Ras85D (GTP-bound) which
CC releases the inhibitory intramolecular interaction between the two
CC domains (By similarity). This allows the Dsor1/MEK1-mediated
CC dimerization of ksr and Raf which activates Raf (PubMed:29433126).
CC {ECO:0000250|UniProtKB:P15056, ECO:0000269|PubMed:29433126}.
CC -!- SUBUNIT: Interacts with Dsor1/MEK1 and ksr; Dsor1 binding to ksr
CC probably promotes ksr and Raf dimerization and ksr-mediated Raf
CC transactivation. {ECO:0000269|PubMed:29433126}.
CC -!- INTERACTION:
CC P11346; Q24324: Dsor1; NbExp=4; IntAct=EBI-664624, EBI-671282;
CC P11346; P00528: Src64B; NbExp=3; IntAct=EBI-664624, EBI-87092;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Zygotically expressed throughout embryogenesis.
CC {ECO:0000269|PubMed:3135183, ECO:0000269|PubMed:8423783}.
CC -!- PTM: Extensively phosphorylated 1 to 2 hours after egg laying.
CC {ECO:0000269|PubMed:18327897, ECO:0000269|PubMed:8423783}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the prothoracic gland
CC (PG) delays the onset of pupariation by prolonging the L3 larval stage.
CC {ECO:0000269|PubMed:19965758}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30166.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB72239.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X07181; CAA30166.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014298; AAF45774.1; -; Genomic_DNA.
DR EMBL; AE014298; ABW09328.3; -; Genomic_DNA.
DR EMBL; AL133503; CAB72239.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY089490; AAL90228.1; -; mRNA.
DR EMBL; AY135031; AAN17541.1; -; Genomic_DNA.
DR EMBL; AY135032; AAN17542.1; -; Genomic_DNA.
DR EMBL; AY135033; AAN17543.1; -; Genomic_DNA.
DR EMBL; AY135034; AAN17544.1; -; Genomic_DNA.
DR EMBL; AY135035; AAN17545.1; -; Genomic_DNA.
DR EMBL; AY135036; AAN17546.1; -; Genomic_DNA.
DR EMBL; AY135037; AAN17547.1; -; Genomic_DNA.
DR EMBL; AY135038; AAN17548.1; -; Genomic_DNA.
DR EMBL; AY135039; AAN17549.1; -; Genomic_DNA.
DR EMBL; AY135040; AAN17550.1; -; Genomic_DNA.
DR EMBL; AY135041; AAN17551.1; -; Genomic_DNA.
DR EMBL; AY135042; AAN17552.1; -; Genomic_DNA.
DR EMBL; AY135043; AAN17553.1; -; Genomic_DNA.
DR EMBL; AY135044; AAN17554.1; -; Genomic_DNA.
DR EMBL; AY135045; AAN17555.1; -; Genomic_DNA.
DR EMBL; AY135046; AAN17556.1; -; Genomic_DNA.
DR EMBL; AY135047; AAN17557.1; -; Genomic_DNA.
DR EMBL; AY135048; AAN17558.1; -; Genomic_DNA.
DR EMBL; AY135049; AAN17559.1; -; Genomic_DNA.
DR EMBL; AY135050; AAN17560.1; -; Genomic_DNA.
DR EMBL; AY135051; AAN17561.1; -; Genomic_DNA.
DR EMBL; AY135052; AAN17562.1; -; Genomic_DNA.
DR EMBL; M16598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S00393; TVFFDF.
DR RefSeq; NP_001096867.3; NM_001103397.3.
DR RefSeq; NP_525047.1; NM_080308.4.
DR AlphaFoldDB; P11346; -.
DR SMR; P11346; -.
DR BioGRID; 57758; 149.
DR DIP; DIP-29769N; -.
DR IntAct; P11346; 6.
DR MINT; P11346; -.
DR STRING; 7227.FBpp0305946; -.
DR iPTMnet; P11346; -.
DR PRIDE; P11346; -.
DR EnsemblMetazoa; FBtr0070401; FBpp0070385; FBgn0003079.
DR EnsemblMetazoa; FBtr0344007; FBpp0310458; FBgn0003079.
DR GeneID; 31221; -.
DR KEGG; dme:Dmel_CG2845; -.
DR UCSC; CG2845-RB; d. melanogaster.
DR UCSC; CG2845-RC; d. melanogaster.
DR CTD; 31221; -.
DR FlyBase; FBgn0003079; Raf.
DR VEuPathDB; VectorBase:FBgn0003079; -.
DR eggNOG; KOG0193; Eukaryota.
DR GeneTree; ENSGT00940000171269; -.
DR HOGENOM; CLU_023684_1_0_1; -.
DR InParanoid; P11346; -.
DR OMA; MYLMEYQ; -.
DR OrthoDB; 243095at2759; -.
DR PhylomeDB; P11346; -.
DR BRENDA; 2.7.10.2; 1994.
DR Reactome; R-DME-1295596; Spry regulation of FGF signaling.
DR Reactome; R-DME-170968; Frs2-mediated activation.
DR Reactome; R-DME-209190; Phosphorylation of CI.
DR Reactome; R-DME-209214; Phosphorylation of SMO.
DR Reactome; R-DME-392517; Rap1 signalling.
DR Reactome; R-DME-430116; GP1b-IX-V activation signalling.
DR Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DME-5673000; RAF activation.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-5674499; Negative feedback regulation of MAPK pathway.
DR Reactome; R-DME-5675221; Negative regulation of MAPK pathway.
DR SignaLink; P11346; -.
DR BioGRID-ORCS; 31221; 2 hits in 3 CRISPR screens.
DR ChiTaRS; phr; fly.
DR GenomeRNAi; 31221; -.
DR PRO; PR:P11346; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003079; Expressed in egg cell and 37 other tissues.
DR Genevisible; P11346; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IGI:FlyBase.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IGI:FlyBase.
DR GO; GO:0008069; P:dorsal/ventral axis specification, ovarian follicular epithelium; IMP:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IGI:FlyBase.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:FlyBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0007369; P:gastrulation; IMP:FlyBase.
DR GO; GO:0042386; P:hemocyte differentiation; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0002168; P:instar larval development; IMP:FlyBase.
DR GO; GO:0035171; P:lamellocyte differentiation; IMP:FlyBase.
DR GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:FlyBase.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:FlyBase.
DR GO; GO:0042461; P:photoreceptor cell development; IGI:UniProtKB.
DR GO; GO:0046530; P:photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; HGI:FlyBase.
DR GO; GO:0046534; P:positive regulation of photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:FlyBase.
DR GO; GO:0007465; P:R7 cell fate commitment; IMP:FlyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; HGI:FlyBase.
DR GO; GO:0030641; P:regulation of cellular pH; IGI:FlyBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0045500; P:sevenless signaling pathway; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
DR GO; GO:0007362; P:terminal region determination; IMP:FlyBase.
DR GO; GO:0008293; P:torso signaling pathway; IMP:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0035309; P:wing and notum subfield formation; IGI:FlyBase.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR CDD; cd00029; C1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02196; RBD; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00455; RBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50898; RBD; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Coiled coil; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..739
FT /note="Raf homolog serine/threonine-protein kinase Raf"
FT /id="PRO_0000086194"
FT DOMAIN 141..212
FT /note="RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 429..690
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 222..268
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 301..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 50..86
FT /evidence="ECO:0000255"
FT COMPBIAS 378..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 548
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 435..443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 322
FT /note="P -> L (in strain: AA1)"
FT /evidence="ECO:0000269|PubMed:12694293"
FT VARIANT 327
FT /note="S -> T (in strain: KLH4 and KLH6)"
FT /evidence="ECO:0000269|PubMed:12694293"
FT VARIANT 360
FT /note="S -> R (in strain: Reids2)"
FT /evidence="ECO:0000269|PubMed:12694293"
FT VARIANT 465
FT /note="A -> T (in strain: 5-17-88b#5)"
FT /evidence="ECO:0000269|PubMed:12694293"
FT CONFLICT 118
FT /note="N -> T (in Ref. 1; CAA30166)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="A -> P (in Ref. 1; CAA30166)"
FT /evidence="ECO:0000305"
FT CONFLICT 478..480
FT /note="KKT -> RKA (in Ref. 7; M16598)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="G -> R (in Ref. 7; M16598)"
FT /evidence="ECO:0000305"
FT CONFLICT 658..661
FT /note="PQAL -> RRHS (in Ref. 1; CAA30166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 83729 MW; B685A895D05048C1 CRC64;
MSSESSTEGD SDLYDPLAEE LHNVQLVKHV TRENIDALNA KFANLQEPPA MYLIEYQELT
SKLHELEAKE QELMERLNSQ DQQEDSSLVE RFKEQPHYQN QTQILQQQRQ LARVHHGNDL
TDSLGSQPGS QCGTLTRQPK ILLRAHLPNQ QRTSVEVISG VRLCDALMKA LKLRQLTPDM
CEVSTTHSGR HIIPWHTDIG TLHVEEIFVR LLDKFPIRTH IKHQIIRKTF FSLVFCEGCR
RLLFTGFYCS QCNFRFHQRC ANRVPMLCQP FPMDSYYQLL LAENPDNGVG FPGRGTAVRF
NMSSRSRSRR CSSSGSSSSS KPPSSSSGNH RQGRPPRISQ DDRSNSAPNV CINNIRSVTS
EVQRSLIMQA RPPLPHPCTD HSNSTQASPT STLKHNRPRA RSADESNKNL LLRDAKSSEE
NWNILAEEIL IGPRIGSGSF GTVYRAHWHG PVAVKTLNVK TPSPAQLQAF KNEVAMLKKT
RHCNILLFMG CVSKPSLAIV TQWCEGSSLY KHVHVSETKF KLNTLIDIGR QVAQGMDYLH
AKNIIHRDLK SNNIFLHEDL SVKIGDFGLA TAKTRWSGEK QANQPTGSIL WMAPEVIRMQ
ELNPYSFQSD VYAFGIVMYE LLAECLPYGH ISNKDQILFM VGRGLLRPDM SQVRSDAPQA
LKRLAEDCIK YTPKDRPLFR PLLNMLENML RTLPKIHRSA SEPNLTQSQL QNDEFLYLPS
PKTPVNFNNF QFFGSAGNI
