ID B8Q6A8_DROME Unreviewed; 1435 AA.
AC B8Q6A8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Dizzy isoform CI {ECO:0000313|EMBL:ABY71207.1};
GN Name=dzy {ECO:0000313|EMBL:ABY71207.1};
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 {ECO:0000313|EMBL:ABY71207.1};
RN [1] {ECO:0000313|EMBL:ABY71207.1}
RP NUCLEOTIDE SEQUENCE.
RA Reuter R., Marchese D., Hepper C., Donohoe C.;
RT "Alternative splicing of dzy produces five isoproteins two of which
RT regulate migration and adhesion of embryonic macrophages in Drosophila.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RAPGEF2 family.
CC {ECO:0000256|ARBA:ARBA00010829}.
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DR EMBL; EU362915; ABY71207.1; -; mRNA.
DR EnsemblMetazoa; FBtr0300039; FBpp0289316; FBgn0265778.
DR VEuPathDB; VectorBase:FBgn0265778; -.
DR GeneTree; ENSGT00940000168958; -.
DR HOGENOM; CLU_002782_2_2_1; -.
DR Bgee; FBgn0265778; Expressed in central nervous system and 16 other cell types or tissues.
DR ExpressionAtlas; B8Q6A8; baseline and differential.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01785; RA_PDZ-GEF1; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR23113:SF249; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 2; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 2: Evidence at transcript level;
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168}.
FT DOMAIN 128..241
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 279..402
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 405..486
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 757..843
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 868..1096
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 33..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1435 AA; 156532 MW; FA9EE51C7FC60C3A CRC64;
MDPYHHIRHH YPPTSIAGTG VVVGSSTTIN RPELHQKCNR GSHSSDTSSA YSGSDTMASN
YASSLEAEEI DLSGLVESVV DSDEEDLAES MDSLTVRDAV RDCLEKDPAE RSEEDVEVLL
EFTQGLKAFT NITLAVRRAL CSVMVFAVVD KAGTVVMSDG EELDSWSVLI NGAVEIEHAN
GSREELQMGD SFGILPTMDK LYHRGVMRTK CDDCQFVCIT QTDYYRIQHQ GEENTRRHED
ENGFVVMVTE LRSIGGAGTD SAGSGGSATG ASASLNMKRG HVVIRGTPER LLQQLVEENS
MTDPTYVEDF LLTHRIFIQN PQEVTSKLLH WFDLEQVDAH KTQELRDRVT RVVLLWVNNH
FTDFEADYEM MEFLEVFEAL LERKKLLSQL RLLHIACAAK ARMRSCTLTR SSRDEPLNFR
IVGGYELRGV AIATGNAAVG IYISHVEPGS KAQDVGLKRG DQIHEVNGQS LDHVTSKRAL
EILTGTTHLS ISVKSNLLGF KEIMQALEHG GGTAGSGSIS AGSGSFKSVR SPRRICANDI
AKLHGRSDST TDELSSVSAS NRAHMVRLSS VDMLLDQPDC APPQTPPVSG SGNMASNFMQ
QLLQSVNNSS AKKSGGNSNS DQQDTKGGFM TLAPKRRLQK ALAKMNLLNK QNHGSSLNDS
SDTLLNDPKS KLSAVSSCSS STQSSINGCT VSGGGRLYQS QSNPDLTSLN YDGGSDAGGN
GGGRLQVNYL NAHIHRPSAA STLTTNSTQS HLLPDYPDHV LKVYKADQTC KYVLIYKETT
AHEVVMLTLQ EFGIHDPSSN FSLCEVSVGD GGMVKQRRLP DQLQNLAERI SFAARYYLKL
NDSTEPLVPD ELALELVRES NVHFLHLNAY ELAIQLTLQD FANFRQIEST EYVDELFELR
SRYGVPMLSK FAELVNREMF WVVSEICAEH NIVRRMKIVK QFIKIARHCK ECRNFNSMFA
IVSGLGHGAV SRLRQTWEKL PSKYQRLFND LQDLMDPSRN MSKYRQLVSA ELLAQHPIIP
FYPIVKKDLT FIHLGNDTRV DGLINFEKLR MLAKEVRLLT HMCSSPYDLL SILELKGQSP
SNALFSLNQM SASQSNAAAG TVIAANAGQA TIKRRKKSTA APNPKKMFEE AQMVRRVKAY
LNSLKILSDE DLLHKFSLEC EPAHGSTYSG SISHGNTSHR SGGGGSISGG AGGSSGGGGG
GSSSLNAGDQ LSIYSHTSSS SAPNSSLSLR KRHPSSPTLS TTSSTSSTSD HQRRQMHNNG
PKFGTASPQA VKKMLSLSES SKIRPHQPFV PRHGSTMAGV IPPLHHMHAA HGFSTPSPGG
VVTSPATSAV ANVQCTPSPS PCSHRRLASG GNIIPSRAIH ERSHSDTPAP PPPLPSVDLS
LESSSVTTFR DLPLRKSVTS GGPPNFMDST KCTICPMPPM NQNNFKAQHN NETIN
//
