RG68F_DROME
ID RG68F_DROME Reviewed; 476 AA.
AC Q9VTU3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Rho GTPase-activating protein 68F;
GN Name=RhoGAP68F; ORFNames=CG6811;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16609869; DOI=10.1007/s00427-006-0067-6;
RA Sanny J., Chui V., Langmann C., Pereira C., Zahedi B., Harden N.;
RT "Drosophila RhoGAP68F is a putative GTPase activating protein for RhoA
RT participating in gastrulation.";
RL Dev. Genes Evol. 216:543-550(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-31, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251, 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).
CC -!- FUNCTION: Functions as a GTPase-activating protein (GAP) for RhoA/Rho1
CC during gastrulation by converting it to an inactive GDP-bound state.
CC {ECO:0000269|PubMed:16609869}.
CC -!- DISRUPTION PHENOTYPE: Defects during gastrulation.
CC {ECO:0000269|PubMed:16609869}.
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DR EMBL; AE014296; AAF49953.1; -; Genomic_DNA.
DR EMBL; AY069311; AAL39456.1; -; mRNA.
DR RefSeq; NP_001261744.1; NM_001274815.1.
DR RefSeq; NP_648552.1; NM_140295.3.
DR AlphaFoldDB; Q9VTU3; -.
DR SMR; Q9VTU3; -.
DR BioGRID; 64739; 44.
DR DIP; DIP-23611N; -.
DR IntAct; Q9VTU3; 46.
DR STRING; 7227.FBpp0075729; -.
DR iPTMnet; Q9VTU3; -.
DR PaxDb; Q9VTU3; -.
DR PRIDE; Q9VTU3; -.
DR DNASU; 39385; -.
DR EnsemblMetazoa; FBtr0075997; FBpp0075729; FBgn0036257.
DR EnsemblMetazoa; FBtr0334092; FBpp0306217; FBgn0036257.
DR GeneID; 39385; -.
DR KEGG; dme:Dmel_CG6811; -.
DR UCSC; CG6811-RA; d. melanogaster.
DR CTD; 39385; -.
DR FlyBase; FBgn0036257; RhoGAP68F.
DR VEuPathDB; VectorBase:FBgn0036257; -.
DR eggNOG; KOG4406; Eukaryota.
DR GeneTree; ENSGT00940000165508; -.
DR InParanoid; Q9VTU3; -.
DR OrthoDB; 1511935at2759; -.
DR PhylomeDB; Q9VTU3; -.
DR Reactome; R-DME-8980692; RHOA GTPase cycle.
DR Reactome; R-DME-9013026; RHOB GTPase cycle.
DR Reactome; R-DME-9013106; RHOC GTPase cycle.
DR Reactome; R-DME-9013148; CDC42 GTPase cycle.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR Reactome; R-DME-9035034; RHOF GTPase cycle.
DR SignaLink; Q9VTU3; -.
DR BioGRID-ORCS; 39385; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39385; -.
DR PRO; PR:Q9VTU3; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036257; Expressed in arthropod fat body and 31 other tissues.
DR ExpressionAtlas; Q9VTU3; baseline and differential.
DR Genevisible; Q9VTU3; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IDA:FlyBase.
DR GO; GO:0055037; C:recycling endosome; IDA:FlyBase.
DR GO; GO:0005096; F:GTPase activator activity; IDA:FlyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:2001136; P:negative regulation of endocytic recycling; IDA:FlyBase.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IDA:FlyBase.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:FlyBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Gastrulation; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..476
FT /note="Rho GTPase-activating protein 68F"
FT /id="PRO_0000372857"
FT DOMAIN 91..244
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 276..464
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 476 AA; 54969 MW; AF302C00E8A1BEA3 CRC64;
MDAHSRFAPR LPGPAINPIV DNSDEPQPSL SDLHDFEPKL EFDDTELLAP SPLEKDVMVG
DFVLAEDPEL EPEEDVNPLE DDFEDQLREQ SENFQTPRNK CDFLGTDKQG RHIFGIYASR
FPEKSQLEGF VREIIKEIEP FVENDYILVY FHQGLKEDNK PSAQFLWNSY KELDRNFRKN
LKTLYVVHPT WFIRVIWNFF SPFISDKFRK KLVYISSLDE LRQALGLNKL KLPDNICDLD
DKLNPSRKPS TPPPSSNINA SRQQQHKMAT THQFGVPLKF IVMNSPCLNS IPPIVRKCVD
SLSITGVIDT EGIFRRSGNH SEIMALKERV NRGEDVDLKS VNVHVIAGLL KSFLRDLAEP
LLTFELYEDV TGFLDWPKEE RSRNVTQLIR EKLPEENYEL FKYIVEFLVR VMDCEDLNKM
TSSNLAIVFG PNFLWSRSTS TSLEEIAPIN AFVDFVLQNH KDIYLIDVNQ RTVSVD
