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Database: UniProt
Entry: O44113_DROME
LinkDB: O44113_DROME
Original site: O44113_DROME 
ID   O44113_DROME            Unreviewed;      2559 AA.
AC   O44113;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   16-APR-2014, entry version 97.
DE   SubName: Full=Putative guanine nucleotide exchange factor RhoGEF2;
GN   Name=RhoGEF2; Synonyms=rhoGEF2; ORFNames=CG9635;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9428514; DOI=10.1016/S0092-8674(00)80482-1;
RA   Barrett K., Leptin M., Settleman J.;
RT   "The Rho GTPase and a putative RhoGEF mediate a signaling pathway for
RT   the cell shape changes in Drosophila gastrulation.";
RL   Cell 91:905-915(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Haecker U., Perrimon N.;
RT   "DRhoGEF2 encodes a member of the Dbl-family of oncogenes and
RT   orchestrates cell shape changes during gastrulation in Drosophila.";
RL   Genes Dev. 0:0-0(1998).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains PH domain.
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DR   EMBL; AF031930; AAB88816.1; -; mRNA.
DR   PIR; T09144; T09144.
DR   ProteinModelPortal; O44113; -.
DR   STRING; 7227.FBpp0086124; -.
DR   PRIDE; O44113; -.
DR   FlyBase; FBgn0023172; RhoGEF2.
DR   InParanoid; O44113; -.
DR   SignaLink; O44113; -.
DR   ChiTaRS; RhoGEF2; drosophila.
DR   Bgee; O44113; -.
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:0007369; P:gastrulation; TAS: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:0032319; P:regulation of Rho GTPase activity; IMP:GOC.
DR   GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR   GO; GO:0038032; P:termination of G-protein coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
DR   Gene3D; 1.20.900.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   InterPro; IPR015212; RGS-like_dom.
DR   InterPro; IPR015721; RhoGEF-like.
DR   PANTHER; PTHR22825; PTHR22825; 1.
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   2: Evidence at transcript level;
KW   Metal-binding; Zinc.
SQ   SEQUENCE   2559 AA;  280949 MW;  7BC661AA1E6EB40E 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
     QLHQVGAEDA PTVKLQAAAG NKNTALLTPN QIQHLSASAT HSNQQFHHLH HHHNLHNNNY
     PPQQQPASTS PAFLSLLPRS LSSLSLGTRK NKTEKDLTTS SPFGLTTDFL QQQRMSHQAE
     SMSQSMHQHT STPTSQQFFH PHQQQHRFKE TGPTSKGKNK FLISRSLIEE DVPPPLPQRN
     PPRQLNLDLK NGNASPGGSH LVAPVSDLDR ATSPQLNRSQ QQQLPRSTDN SPSNAKSKRS
     KIKTKALSDP KMSTQMFLQM ESASAAGAAG GSIEVDGGPP PLPPRLPGMM TEDMSRGSCQ
     NLAQPNSVGT AFNYPLVSTT TAVQNDNLNI AFPLSQRPNI VQQLQQYQQQ QQHQMSGGQA
     TGALGQTPNL GKNKHRRVGS SPDNMHPRHP DRITKTTSGS WEIVEKDGES SPPGTPPPPY
     LSSSHMTVLE DPNENNRGAA AAGPGVFIES HQFTPMAGAS SPIPISLHSN HMHAAQSNDT
     QKEIISMEDE NSDLDEPFID ENGPFNNLTR LLEAENVTFL AIFLNYVISN SDPAPLLFYL
     ITELYKEGTS KDMRKWAYEI HSTFLVPRAP LSWYRQDESL AREVDNVLQL EYDKVEILRT
     VFLRSRKRAK DLISEQLREF QQKRTAGLGT IYGPTDDKLA EAKTDKLREQ IIDKYLMPNL
     HALIEDENGS PPEDVRKVAL CSALSTVIYR IFNTRPPPSS IVERVHHFVS RDKSFKSRIM
     GKNRKMNVRG HPLVLRQYYE VTHCNHCQTI IWGVSPQGYH CTDCKLNIHR QCSKVVDESC
     PGPLPQAKRL AHNDKISKFM GKIRPRTSDV IGNEKRSRQD EELNVELTPD RGQASIVRQP
     SDRRPDANIS IRSNGNTSCN TSGLNTTDLQ SSFHGSCAND SINPGGGAGC NMDLSTSVAS
     TTPSTSGSVA AGLSAFAELN ALDTVDKEAR RERYSQHPKH KSAPVSVNWS ESYKERLSNK
     RNRNSRRKTS DPSLSSRPND EQLDLGLSNA TYVGSSNSSL SSAGGTESPS TSMEHFAAPG
     AAGGVQVPPM GLNQNQHPHL LIQQHAQQYC QQDSFQAGLA GAAGSSAASN SSFWNAGHPL
     PVARWTLESE DEDDVNEADW SSMVAAEVSA ALTDAEKKRQ EIINEIYQTE RNHVRTLKLL
     DRLFFLPLYE SGLLSQDHLL LLFPPALLSL REIHGAFEQS LKQRRIEHNH VVNTIGDLLA
     DMFDGQSGVV LCEFAAQFCA RQQIALEALK EKRNKDEMLQ KLLKKSESHK ACRRLELKDL
     LPTVLQRLTK YPLLFENLYK VTVRLLPENT TEAEAIQRAV ESSKRILVEV NQAVRTAEDA
     HKLQNIQRKL DRSSYDKEEF KKLDLTQHHL IHDGNLTIKK NPSVQLHGLL FENMIVLLTK
     QDDKYYLKNL HTPLSITNKP VSPIMSIDAD TLIRQEAADK NSFFLIKMKT SQMLELRAPS
     SSECKTWFKH FSDVAARQSK NRSKNASSNH DTSISDPALA AIPHSNTKES LELSTDTVQP
     LAATATLTTT PLAPMLPIAT VTPAPATNNS NVSSLTGVQL RNPQRDATAS ESDADYVNTP
     KPRSSQNEVN RTMSIRSTGE PIQKYSANGT EANDVTLRHS QSTRESVRPG STGEERNSTY
     GMVGGNSKRD SASIVCSNNS NNTRTLLMQS PLVDPTAIQV SISPAHTAEP VLTPGEKLRR
     LDASIRNDLL EKQKIICDIF RLPVEHYDQI VDIAMMPEAP KDSADIALAA YDQIQTLTKM
     LNEYMHVTPE QEVSAVSTAV CGHCHEKEKL RKKVAPSSSF SSSPPPLPPP NRQHAQAQAQ
     IPPSRLMPKL QTLDLDEVAI HEDDDGYCEI DELRLPAIPS KPHERPTTPL APFNTEPKTS
     QSVIDASKRQ STDAVPEGLL EQEPLEGDKT ETKGEDNEVK TVPSDKLSES CNEERQCVEA
     DITKEVADPT TSKNEAAASV DELPSQSREI KTAENASKSV ADKKEDNEET IEEGVASTVD
     SSTQTSPTES PKETDKLTGG SSSTCGPNRI QHASVLEPSV PCHALSSIVT ILNEQISMLL
     PKINERDMER ERLRKENQHL RELLSALHDR QRVDEVKETP FDLKKLMHAE DVEFDDDIDA
     ISNSSLTPTP TPIPTASPSA SGQVETAEAM RITSTEDEE
//
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