GRAP_DROME
ID GRAP_DROME Reviewed; 211 AA.
AC Q08012; A4UZF9; Q0E989; Q9V6Q5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Growth factor receptor-bound protein 2 {ECO:0000250|UniProtKB:P62993};
DE AltName: Full=Downstream of receptor kinase {ECO:0000312|FlyBase:FBgn0004638};
DE AltName: Full=Protein enhancer of sevenless 2B {ECO:0000303|PubMed:8462097};
GN Name=drk {ECO:0000303|PubMed:8462097, ECO:0000312|FlyBase:FBgn0004638};
GN Synonyms=E(sev)2B {ECO:0000303|PubMed:8462097},
GN Grb2 {ECO:0000312|FlyBase:FBgn0004638};
GN ORFNames=CG6033 {ECO:0000312|FlyBase:FBgn0004638};
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 [MRNA], FUNCTION, AND INTERACTION WITH SEV AND SOS.
RC TISSUE=Eye;
RX PubMed=8462097; DOI=10.1016/0092-8674(93)90169-q;
RA Simon M.A., Dodson G.S., Rubin G.M.;
RT "An SH3-SH2-SH3 protein is required for p21Ras1 activation and binds to
RT sevenless and Sos proteins in vitro.";
RL Cell 73:169-177(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH SEV AND SOS, AND MUTAGENESIS OF ARG-67 AND HIS-106.
RC TISSUE=Embryo;
RX PubMed=8462098; DOI=10.1016/0092-8674(93)90170-u;
RA Olivier J.P., Raabe T., Henkemeyer M., Dickson B., Mbamalu G., Margolis B.,
RA Schlessinger J., Hafen E., Pawson T.;
RT "A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless
RT tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos.";
RL Cell 73:179-191(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ann Arbor1, Ann Arbor16, Ann Arbor18, Ann Arbor20, Ann Arbor3, CA2,
RC CT1, Georgia-5b, Kakamega-2, Kakamega-b1, Kakamega-b2, Kenya-HLa3,
RC Kenya-HLa4, Kenya-HLa6, Kenya-LGC, M2, Makindu-1, Makindu-b1, Makindu-b5,
RC PYR2, Reids2, and Sapporo;
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [7]
RP INTERACTION WITH DAB, AND MUTAGENESIS OF PRO-49; ARG-85 AND GLY-199.
RX PubMed=9671493; DOI=10.1128/mcb.18.8.4844;
RA Le N., Simon M.A.;
RT "Disabled is a putative adaptor protein that functions during signaling by
RT the sevenless receptor tyrosine kinase.";
RL Mol. Cell. Biol. 18:4844-4854(1998).
RN [8]
RP INTERACTION WITH DOS.
RX PubMed=12128212; DOI=10.1016/s0925-4773(02)00147-8;
RA Feller S.M., Wecklein H., Lewitzky M., Kibler E., Raabe T.;
RT "SH3 domain-mediated binding of the Drk protein to Dos is an important step
RT in signaling of Drosophila receptor tyrosine kinases.";
RL Mech. Dev. 116:129-139(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH ACK.
RX PubMed=22615583; DOI=10.1371/journal.pgen.1002725;
RA Schoenherr J.A., Drennan J.M., Martinez J.S., Chikka M.R., Hall M.C.,
RA Chang H.C., Clemens J.C.;
RT "Drosophila activated Cdc42 kinase has an anti-apoptotic function.";
RL PLoS Genet. 8:E1002725-E1002725(2012).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=30610177; DOI=10.1073/pnas.1810951116;
RA Li C., Bademci G., Subasioglu A., Diaz-Horta O., Zhu Y., Liu J.,
RA Mitchell T.G., Abad C., Seyhan S., Duman D., Cengiz F.B., Tokgoz-Yilmaz S.,
RA Blanton S.H., Farooq A., Walz K., Zhai R.G., Tekin M.;
RT "Dysfunction of GRAP, encoding the GRB2-related adaptor protein, is linked
RT to sensorineural hearing loss.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:1347-1352(2019).
RN [11] {ECO:0007744|PDB:2A36, ECO:0007744|PDB:2A37, ECO:0007744|PDB:2AZS, ECO:0007744|PDB:2AZV}
RP STRUCTURE BY NMR OF 1-59, AND MUTAGENESIS OF THR-22.
RX PubMed=16300404; DOI=10.1021/bi0512795;
RA Bezsonova I., Singer A., Choy W.Y., Tollinger M., Forman-Kay J.D.;
RT "Structural comparison of the unstable drkN SH3 domain and a stable
RT mutant.";
RL Biochemistry 44:15550-15560(2005).
CC -!- FUNCTION: Adapter protein which modulates signaling mediated by several
CC receptor tyrosine kinases such as sev and Ack (PubMed:8462097,
CC PubMed:22615583, PubMed:8462098). Required for proper signaling by
CC sevenless (PubMed:8462097, PubMed:8462098). May act to stimulate the
CC ability of Sos to catalyze Ras1 activation by linking sevenless and Sos
CC in a signaling complex (PubMed:8462097, PubMed:8462098). Required for
CC functional and morphological integrities of the scolopidia, sensory
CC neurons and the antennal mechanosensory and motor center (AMMC) brain
CC neuropil (PubMed:30610177). Required for Ack-dependent suppression of
CC apoptosis in the eye (PubMed:22615583). {ECO:0000269|PubMed:22615583,
CC ECO:0000269|PubMed:30610177, ECO:0000269|PubMed:8462097,
CC ECO:0000269|PubMed:8462098}.
CC -!- SUBUNIT: Interacts with autophosphorylated sev via SH2 domain and Sos,
CC Dos and Dab via SH3 domains (PubMed:12128212, PubMed:8462097,
CC PubMed:8462098, PubMed:9671493). Binds to tyrosine phosphorylated Dab
CC via the SH2 domain (PubMed:9671493). Interacts with phosphorylated Ack
CC (PubMed:22615583). {ECO:0000269|PubMed:12128212,
CC ECO:0000269|PubMed:22615583, ECO:0000269|PubMed:8462097,
CC ECO:0000269|PubMed:8462098, ECO:0000269|PubMed:9671493}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8462098}; Peripheral
CC membrane protein {ECO:0000269|PubMed:8462098}. Synapse
CC {ECO:0000269|PubMed:30610177}. Note=Localizes at the presynaptic
CC terminal. {ECO:0000269|PubMed:30610177}.
CC -!- TISSUE SPECIFICITY: Found mainly in the developing eye and in the
CC antennal disk. Also observed in other imaginal disks tested and in the
CC embryo. Expressed in Johnston's organ, the hearing organ, neurons (at
CC protein level) (PubMed:30610177). {ECO:0000269|PubMed:30610177}.
CC -!- DISRUPTION PHENOTYPE: Embryonically lethal (PubMed:30610177). Loss in
CC Johnston's organ causes scolopidium abnormalities (PubMed:30610177).
CC {ECO:0000269|PubMed:30610177}.
CC -!- SIMILARITY: Belongs to the GRB2/sem-5/DRK family. {ECO:0000305}.
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DR EMBL; L12446; AAA28898.1; -; mRNA.
DR EMBL; L13173; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY135053; AAN17564.1; -; Genomic_DNA.
DR EMBL; AY135054; AAN17565.1; -; Genomic_DNA.
DR EMBL; AY135055; AAN17566.1; -; Genomic_DNA.
DR EMBL; AY135056; AAN17567.1; -; Genomic_DNA.
DR EMBL; AY135057; AAN17568.1; -; Genomic_DNA.
DR EMBL; AY135058; AAN17569.1; -; Genomic_DNA.
DR EMBL; AY135059; AAN17570.1; -; Genomic_DNA.
DR EMBL; AY135060; AAN17571.1; -; Genomic_DNA.
DR EMBL; AY135061; AAN17572.1; -; Genomic_DNA.
DR EMBL; AY135062; AAN17573.1; -; Genomic_DNA.
DR EMBL; AY135063; AAN17574.1; -; Genomic_DNA.
DR EMBL; AY135064; AAN17575.1; -; Genomic_DNA.
DR EMBL; AY135065; AAN17576.1; -; Genomic_DNA.
DR EMBL; AY135066; AAN17577.1; -; Genomic_DNA.
DR EMBL; AY135067; AAN17578.1; -; Genomic_DNA.
DR EMBL; AY135068; AAN17579.1; -; Genomic_DNA.
DR EMBL; AY135069; AAN17580.1; -; Genomic_DNA.
DR EMBL; AY135070; AAN17581.1; -; Genomic_DNA.
DR EMBL; AY135071; AAN17582.1; -; Genomic_DNA.
DR EMBL; AY135072; AAN17583.1; -; Genomic_DNA.
DR EMBL; AY135073; AAN17584.1; -; Genomic_DNA.
DR EMBL; AY135074; AAN17585.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58368.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68582.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68583.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68584.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68585.1; -; Genomic_DNA.
DR EMBL; AY061142; AAL28690.1; -; mRNA.
DR PIR; A46444; A46444.
DR RefSeq; NP_476858.1; NM_057510.4.
DR RefSeq; NP_725302.1; NM_165994.2.
DR RefSeq; NP_725303.1; NM_165995.2.
DR RefSeq; NP_725304.1; NM_165996.2.
DR RefSeq; NP_725306.1; NM_165998.2.
DR PDB; 2A36; NMR; -; A=1-59.
DR PDB; 2A37; NMR; -; A=1-59.
DR PDB; 2AZS; NMR; -; A=1-59.
DR PDB; 2AZV; NMR; -; A=1-59.
DR PDBsum; 2A36; -.
DR PDBsum; 2A37; -.
DR PDBsum; 2AZS; -.
DR PDBsum; 2AZV; -.
DR AlphaFoldDB; Q08012; -.
DR SMR; Q08012; -.
DR BioGRID; 62256; 76.
DR DIP; DIP-21223N; -.
DR IntAct; Q08012; 5.
DR MINT; Q08012; -.
DR STRING; 7227.FBpp0086812; -.
DR PaxDb; Q08012; -.
DR PRIDE; Q08012; -.
DR DNASU; 36497; -.
DR EnsemblMetazoa; FBtr0087694; FBpp0086813; FBgn0004638.
DR EnsemblMetazoa; FBtr0087695; FBpp0086814; FBgn0004638.
DR EnsemblMetazoa; FBtr0087696; FBpp0086815; FBgn0004638.
DR EnsemblMetazoa; FBtr0087697; FBpp0086816; FBgn0004638.
DR EnsemblMetazoa; FBtr0087698; FBpp0086817; FBgn0004638.
DR GeneID; 36497; -.
DR KEGG; dme:Dmel_CG6033; -.
DR UCSC; CG6033-RC; d. melanogaster.
DR CTD; 36497; -.
DR FlyBase; FBgn0004638; drk.
DR VEuPathDB; VectorBase:FBgn0004638; -.
DR eggNOG; KOG3601; Eukaryota.
DR GeneTree; ENSGT00940000155738; -.
DR HOGENOM; CLU_073617_1_0_1; -.
DR InParanoid; Q08012; -.
DR OMA; MVPEEML; -.
DR OrthoDB; 1091250at2759; -.
DR PhylomeDB; Q08012; -.
DR Reactome; R-DME-109704; PI3K Cascade.
DR Reactome; R-DME-112412; SOS-mediated signalling.
DR Reactome; R-DME-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-DME-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DME-1295596; Spry regulation of FGF signaling.
DR Reactome; R-DME-167044; Signalling to RAS.
DR Reactome; R-DME-179812; GRB2 events in EGFR signaling.
DR Reactome; R-DME-180292; GAB1 signalosome.
DR Reactome; R-DME-180336; SHC1 events in EGFR signaling.
DR Reactome; R-DME-182971; EGFR downregulation.
DR Reactome; R-DME-186763; Downstream signal transduction.
DR Reactome; R-DME-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-DME-210993; Tie2 Signaling.
DR Reactome; R-DME-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-DME-2424491; DAP12 signaling.
DR Reactome; R-DME-2428933; SHC-related events triggered by IGF1R.
DR Reactome; R-DME-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-DME-2871796; FCERI mediated MAPK activation.
DR Reactome; R-DME-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-DME-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-DME-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-DME-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-DME-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-DME-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-DME-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-DME-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-DME-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-DME-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-DME-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-DME-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-DME-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-DME-5654720; PI-3K cascade:FGFR4.
DR Reactome; R-DME-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DME-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-DME-74749; Signal attenuation.
DR Reactome; R-DME-74751; Insulin receptor signalling cascade.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-9013420; RHOU GTPase cycle.
DR Reactome; R-DME-9027284; Erythropoietin activates RAS.
DR Reactome; R-DME-912631; Regulation of signaling by CBL.
DR Reactome; R-DME-9607240; FLT3 Signaling.
DR Reactome; R-DME-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; Q08012; -.
DR BioGRID-ORCS; 36497; 3 hits in 3 CRISPR screens.
DR ChiTaRS; drk; fly.
DR EvolutionaryTrace; Q08012; -.
DR GenomeRNAi; 36497; -.
DR PRO; PR:Q08012; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004638; Expressed in seminal fluid secreting gland and 41 other tissues.
DR Genevisible; Q08012; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:FlyBase.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:FlyBase.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:UniProtKB.
DR GO; GO:0005118; F:sevenless binding; IDA:FlyBase.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IPI:FlyBase.
DR GO; GO:0008306; P:associative learning; 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; IMP:FlyBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IPI:FlyBase.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:FlyBase.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IGI:FlyBase.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:FlyBase.
DR GO; GO:0007465; P:R7 cell fate commitment; IGI:FlyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IPI:FlyBase.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IDA:UniProtKB.
DR GO; GO:0045500; P:sevenless signaling pathway; IDA:FlyBase.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0008293; P:torso signaling pathway; IDA:FlyBase.
DR GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IMP:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:FlyBase.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR030219; Grb2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR19969:SF19; PTHR19969:SF19; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Reference proteome; Repeat; SH2 domain; SH3 domain;
KW Synapse; Transducer.
FT CHAIN 1..211
FT /note="Growth factor receptor-bound protein 2"
FT /id="PRO_0000088210"
FT DOMAIN 1..58
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 60..151
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 152..211
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT MUTAGEN 22
FT /note="T->G: Increases the stability of the SH3 1 domain."
FT /evidence="ECO:0000269|PubMed:16300404"
FT MUTAGEN 49
FT /note="P->L: Inactivates the SH3 domain. Abolishes binding
FT to Dab; when associated with R-199."
FT /evidence="ECO:0000269|PubMed:9671493"
FT MUTAGEN 67
FT /note="R->H: In Su(sevs11)R1 mutant; ommatidial cell
FT development obstruction."
FT /evidence="ECO:0000269|PubMed:8462098"
FT MUTAGEN 85
FT /note="R->K: Disrupts the SH2 domain. Does not affect
FT binding to Dab."
FT /evidence="ECO:0000269|PubMed:9671493"
FT MUTAGEN 106
FT /note="H->Y: In E(sev)2B mutant; ommatidial cell
FT development obstruction."
FT /evidence="ECO:0000269|PubMed:8462098"
FT MUTAGEN 199
FT /note="G->R: Disrupts the SH3 domain. Abolishes binding to
FT Dab; when associated with L-49."
FT /evidence="ECO:0000269|PubMed:9671493"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2A36"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:2AZV"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2A36"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:2A37"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2A36"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:2A36"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2A37"
SQ SEQUENCE 211 AA; 24435 MW; A1D0614AF358F3C0 CRC64;
MEAIAKHDFS ATADDELSFR KTQILKILNM EDDSNWYRAE LDGKEGLIPS NYIEMKNHDW
YYGRITRADA EKLLSNKHEG AFLIRISESS PGDFSLSVKC PDGVQHFKVL RDAQSKFFLW
VVKFNSLNEL VEYHRTASVS RSQDVKLRDM IPEEMLVQAL YDFVPQESGE LDFRRGDVIT
VTDRSDENWW NGEIGNRKGI FPATYVTPYH S
