ID A0A0B4LFF8_DROME Unreviewed; 2456 AA. AC A0A0B4LFF8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 13-FEB-2019, entry version 40. DE SubName: Full=Rho guanine nucleotide exchange factor 2, isoform H {ECO:0000313|EMBL:AHN56311.1}; GN Name=RhoGEF2 {ECO:0000313|EMBL:AHN56311.1, GN ECO:0000313|FlyBase:FBgn0023172}; GN Synonyms=Dmel\CG9635 {ECO:0000313|EMBL:AHN56311.1}, DRhoGEF GN {ECO:0000313|EMBL:AHN56311.1}, dRhoGEF {ECO:0000313|EMBL:AHN56311.1}, GN DRhoGEF2 {ECO:0000313|EMBL:AHN56311.1}, DrhoGEF2 GN {ECO:0000313|EMBL:AHN56311.1}, dRhoGEF2 {ECO:0000313|EMBL:AHN56311.1}, GN Gef2 {ECO:0000313|EMBL:AHN56311.1}, l(2)04291 GN {ECO:0000313|EMBL:AHN56311.1}, RG2 {ECO:0000313|EMBL:AHN56311.1}, GN Rho-GEF2 {ECO:0000313|EMBL:AHN56311.1}, RhoGEF GN {ECO:0000313|EMBL:AHN56311.1}, RhoGef2 {ECO:0000313|EMBL:AHN56311.1}, GN rhoGEF2 {ECO:0000313|EMBL:AHN56311.1}, rhogef2 GN {ECO:0000313|EMBL:AHN56311.1}, RhoGF2 {ECO:0000313|EMBL:AHN56311.1}, GN shar {ECO:0000313|EMBL:AHN56311.1}, Su(Rho1)2B GN {ECO:0000313|EMBL:AHN56311.1}, T2 {ECO:0000313|EMBL:AHN56311.1}; GN ORFNames=CG9635 {ECO:0000313|EMBL:AHN56311.1, GN ECO:0000313|FlyBase:FBgn0023172}, Dmel_CG9635 GN {ECO:0000313|EMBL:AHN56311.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., RA Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., RA Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., RA Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). 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; AE013599; AHN56311.1; -; Genomic_DNA. DR RefSeq; NP_001286515.1; NM_001299586.1. DR SMR; A0A0B4LFF8; -. DR EnsemblMetazoa; FBtr0340124; FBpp0309117; FBgn0023172. DR GeneID; 36915; -. DR CTD; 36915; -. DR FlyBase; FBgn0023172; RhoGEF2. DR eggNOG; ENOG410IR0U; Eukaryota. DR eggNOG; ENOG411079M; LUCA. DR GeneTree; ENSGT00940000168706; -. DR OMA; VNRSMSI; -. DR Reactome; R-DME-193648; NRAGE signals death through JNK. DR Reactome; R-DME-194840; Rho GTPase cycle. DR Reactome; R-DME-416482; G alpha (12/13) signalling events. DR ChiTaRS; RhoGEF2; fly. DR GenomeRNAi; 36915; -. DR Proteomes; UP000000803; Chromosome 2R. DR ExpressionAtlas; A0A0B4LFF8; differential. DR GO; GO:0030478; C:actin cap; IDA:FlyBase. DR GO; GO:0005826; C:actomyosin contractile ring; IDA:FlyBase. DR GO; GO:0045179; C:apical cortex; IDA:FlyBase. DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase. DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase. DR GO; GO:0045178; C:basal part of cell; IDA:FlyBase. DR GO; GO:0016328; C:lateral plasma membrane; IDA:FlyBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IMP:FlyBase. DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:FlyBase. DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase. DR GO; GO:0070252; P:actin-mediated cell contraction; IGI:FlyBase. DR GO; GO:0007375; P:anterior midgut invagination; IMP:FlyBase. DR GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IMP:FlyBase. DR GO; GO:0007349; P:cellularization; IMP:FlyBase. DR GO; GO:0007377; P:germ-band extension; IMP:FlyBase. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:FlyBase. DR GO; GO:0007277; P:pole cell development; IMP:FlyBase. DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:FlyBase. DR GO; GO:0007374; P:posterior midgut invagination; IMP:FlyBase. DR GO; GO:0030589; P:pseudocleavage involved in syncytial blastoderm formation; IMP:FlyBase. DR GO; GO:0050770; P:regulation of axonogenesis; IGI:FlyBase. DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase. DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase. DR GO; GO:0043519; P:regulation of myosin II filament organization; IMP:FlyBase. DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase. DR GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase. DR CDD; cd00029; C1; 1. DR CDD; cd00160; RhoGEF; 1. DR Gene3D; 1.20.900.10; -; 1. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR035899; DBL_dom_sf. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR002219; PE/DAG-bd. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR015212; RGS-like_dom. DR InterPro; IPR036305; RGS_sf. DR Pfam; PF00130; C1_1; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF09128; RGS-like; 1. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00325; RhoGEF; 1. DR SUPFAM; SSF48065; SSF48065; 1. DR SUPFAM; SSF48097; SSF48097; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Metal-binding {ECO:0000256|SAAS:SAAS00515414}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A0B4LFF8}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Zinc {ECO:0000256|SAAS:SAAS00515409}. FT DOMAIN 260 336 PDZ. {ECO:0000259|PROSITE:PS50106}. FT DOMAIN 1047 1097 Phorbol-ester/DAG-type. FT {ECO:0000259|PROSITE:PS50081}. FT DOMAIN 1435 1630 DH. {ECO:0000259|PROSITE:PS50010}. FT COILED 382 402 {ECO:0000256|SAM:Coils}. FT COILED 408 428 {ECO:0000256|SAM:Coils}. FT COILED 1422 1449 {ECO:0000256|SAM:Coils}. FT COILED 2270 2290 {ECO:0000256|SAM:Coils}. FT COILED 2360 2387 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 2456 AA; 269559 MW; B958C362CF326394 CRC64; MDDPSIKKRL LDLYTDEHEY DEVQEIPEES SIQPPETSTS HTSTNGSSHS GPGTATGPGA TSAGPSAGAP QSPVIVVDSV PELPAPKQKS VKNSKSKQKQ KQLANKSKIP RSPSLASSLS SLASSLSGHR DRDKDRDKDR ENQNAVPPQT PPLPPSYKQN QMNGDSTAAA GGGVSAPATP TTANNNNASH NNGSIMGGGV QLNQSDNSNP VLQAPGERSS LNLTPLSRDL SGGHTQESTT PATTPSTPSL ALPKNFQYLT LTVRKDSNGY GMKVSGDNPV FVESVKPGGA AEIAGLVAGD MILRVNGHEV RLEKHPTVVG LIKASTTVEL AVKRSQKLTR PSSVSVVTPS TPILSGRDRT ASITGPQPVD SIKRREMETY KIQTLQKMLE QEKLNLERLK SDQNNPSYKL SEANIRKLRE QLHQVGAEQQ RMSHQAESMS QSMHQHTSTP TSQQFFHPHQ QQHRFKETGP TSKGKNKFLI SRSLIEEDVP PPLPQRNPPR QLNLDLKNGN ASPGGSHLVA PVSDLDRATS PQLNRSQQQQ LPSSTDNSPS NAKSKRSKIK TKALSDPKMS TQMFLQMESA SAAGAAGGSI EVDGGPPPLP PRLPGMMTED MSRGSCQNLA QPNSVGTAFN YPLVSTTTAV QNDNLNIAFP LSQRPNIVQQ LQQYQQQQQH QMSGGQATGA LGQTPNLGKN KHRRVGSSPD NMHPRHPDRI TKTTSGSWEI VEKDGESSPP GTPPPPYLSS SHMTVLEDPN ENNRGAAAAG PGVFIESHQF TPMAGASSPI PISLHSSHMH AAQSNDTQKE IISMEDENSD LDEPFIDENG PFNNLTRLLE AENVTFLAIF LNYVISNSDP APLLFYLITE LYKEGTSKDM RKWAYEIHST FLVPRAPLSW YRQDESLARE VDNVLQLEYD KVEILRTVFL RSRKRAKDLI SEQLREFQQK RTAGLGTIYG PTDDKLAEAK TDKLREQIID KYLMPNLHAL IEDENGSPPE DVRKVALCSA LSTVIYRIFN TRPPPSSIVE RVHHFVSRDK SFKSRIMGKN RKMNVRGHPL VLRQYYEVTH CNHCQTIIWG VSPQGYHCTD CKLNIHRQCS KVVDESCPGP LPQAKRLAHN DKISKFMGKI RPRTSDVIGN EKRSRQDEEL DVELTPDRGQ ASIVRQPSDR RPDANISIRS NGNTSCNTSG LNTTDLQSSF HGSCANDSIN PGGGAGCNMD LSTSVASTTP STSGSVAAGL SAFAELNALD TVDKEARRER YSQHPKHKSA PVSVNRSESY KERLSNKRNR NSRRKTSDPS LSSRPNDEQL DLGLSNATYV GSSNSSLSSA GGSESPSTSM EHFAAPGAAG GVQVPPMGLN QNQHPHLLIQ QHAQQYCQQD SFQAGLAGAA GSSAASNSSF WNAGHPLPVA RWTLESEDED DVNEADWSSM VAAEVLAALT DAEKKRQEII NEIYQTERNH VRTLKLLDRL FFLPLYESGL LSQDHLLLLF PPALLSLREI HGAFEQSLKQ RRIEHNHVVN TIGDLLADMF DGQSGVVLCE FAAQFCARQQ IALEALKEKR NKDEMLQKLL KKSESHKACR RLELKDLLPT VLQRLTKYPL LFENLYKVTV RLLPENTTEA EAIQRAVESS KRILVEVNQA VKTAEDAHKL QNIQRKLDRS SYDKEEFKKL DLTQHHLIHD GNLTIKKNPS VQLHGLLFEN MIVLLTKQDD KYYLKNLHTP LSITNKPVSP IMSIDADTLI RQEAADKNSF FLIKMKTSQM LELRAPSSSE CKTWFKHFSD VAARQSKNRS KNASSNHDTS ISDPALAAIP HSNTKESLEL STDTVQPLAA TATLTTTPLA PMLPIATVTP APATNNSNVS SLTGVQLRNP QRDATASESD ADYVNTPKPR SSQNEVNRTM SIRSTGEPIQ KYSANGTEAN DVTLRHSQST RESVRPGSTG EERNSTYGMV GGNSKRDSAS IVCSNNSNNT RTLLMQSPLV DPTAIQVSIS PAHTAEPVLT PGEKLRRLDA SIRNDLLEKQ KIICDIFRLP VEHYDQIVDI AMMPEAPKDS ADIALAAYDQ IQTLTKMLNE YMHVTPEQEV SAVSTAVCGH CHEKEKLRKK VAPSSSFSSS PPPLPPPNRQ HAQAQAQIPP SRLMPKLQTL DLDEVAIHED DDGYCEIDEL RLPAIPSKPH ERPTTPLAPF NTEPKTSQSV IDASKRQSTD AVPEGLLEQE PLEGDKTETK GEDNEVKTVP SDKLSESCNE ERQCVEADIT KEVADPTTSK NEAAASVDEL PSQSREIKTA ENASKSVADK KEDNEETIEE GVASTVDSST QTSPTESPKE TDKLTGGSSS TCGPNRIQHA SVLEPSVPCH ALSSIVTILN EQISMLLPKI NERDMERERL RKENQHLREL LSALHDRQRV DEVKETPFDL KKLMHAEDVE FDDDIDAISN SSLTPTPTPI PTASPSASGQ VETAEAMRIT STEDEE //