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RGRF2_DANRE
ID   RGRF2_DANRE             Reviewed;        1244 AA.
AC   A2CEA7; B0S6A1;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Ras-specific guanine nucleotide-releasing factor 2;
DE            Short=Ras-GRF2;
DE   AltName: Full=Ras guanine nucleotide exchange factor 2;
GN   Name=rasgrf2; ORFNames=si:ch211-194b21.1, si:dkey-56d12.3;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Functions as a calcium-regulated nucleotide exchange factor
CC       activating both Ras and rac1 through the exchange of bound GDP for GTP.
CC       May function in synaptic plasticity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic
CC       reticulum membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}.
CC   -!- DOMAIN: The Ras-GEF domain and the N-terminal Ras-GEF domain mediate
CC       Ras activation. {ECO:0000250}.
CC   -!- DOMAIN: The IQ domain is dispensable for the Ras-GEF activity.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The DH (DBL-homology) domain is required for rac1 activation.
CC       {ECO:0000250}.
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DR   EMBL; BX470070; CAQ13408.1; -; Genomic_DNA.
DR   EMBL; CR848716; CAQ13408.1; JOINED; Genomic_DNA.
DR   EMBL; CR388055; CAM16158.1; -; Genomic_DNA.
DR   RefSeq; NP_001121705.1; NM_001128233.1.
DR   AlphaFoldDB; A2CEA7; -.
DR   SMR; A2CEA7; -.
DR   STRING; 7955.ENSDARP00000077785; -.
DR   PaxDb; A2CEA7; -.
DR   PRIDE; A2CEA7; -.
DR   Ensembl; ENSDART00000083350; ENSDARP00000077785; ENSDARG00000002816.
DR   GeneID; 553520; -.
DR   KEGG; dre:553520; -.
DR   CTD; 553520; -.
DR   ZFIN; ZDB-GENE-060504-1; rasgrf2b.
DR   eggNOG; KOG3417; Eukaryota.
DR   GeneTree; ENSGT00940000155679; -.
DR   HOGENOM; CLU_003405_0_1_1; -.
DR   InParanoid; A2CEA7; -.
DR   OMA; WMKVDKM; -.
DR   OrthoDB; 70788at2759; -.
DR   PhylomeDB; A2CEA7; -.
DR   TreeFam; TF317296; -.
DR   Reactome; R-DRE-193648; NRAGE signals death through JNK.
DR   Reactome; R-DRE-416482; G alpha (12/13) signalling events.
DR   Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-DRE-8980692; RHOA GTPase cycle.
DR   Reactome; R-DRE-9013148; CDC42 GTPase cycle.
DR   Reactome; R-DRE-9013149; RAC1 GTPase cycle.
DR   PRO; PR:A2CEA7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000002816; Expressed in retina and 3 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.10.840.10; -; 1.
DR   Gene3D; 1.20.900.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
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; IPR030744; RasGRF2.
DR   PANTHER; PTHR23113; PTHR23113; 1.
DR   PANTHER; PTHR23113:SF187; PTHR23113:SF187; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; SSF48065; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   3: Inferred from homology;
KW   Calcium; Calmodulin-binding; Cell membrane; Coiled coil; Cytoplasm;
KW   Endoplasmic reticulum; Guanine-nucleotide releasing factor; Membrane;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1244
FT                   /note="Ras-specific guanine nucleotide-releasing factor 2"
FT                   /id="PRO_0000312866"
FT   DOMAIN          22..129
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          201..230
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          239..425
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          466..584
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          631..745
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT   DOMAIN          1009..1241
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT   REGION          704..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          843..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          147..189
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        724..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1244 AA;  141587 MW;  7C69A7FBFF358C71 CRC64;
     MQKSVRYNEG HALFLSVIAR KEGTKRGYLS KKTTENSKWH EKFFALYQNV LFYFDTDQSA
     RPSGIYLLEG CTCERVPALK VSTVGKDALD KLQYFLVVFG HDGQKPLELR TEEESDCDEW
     VEAIQQASYS DIIIEREVLM QKYIHLVQIV ETEKVAANQL RTQLEDQDTE IERLKAEIIA
     LNKTKERMRP YHVFQEEEDP DIKKIKKVQS FMRGWLCRRK WKIIVQDYIC SPHAESMRKR
     NQIVFNMVEA ETEYVHQLSI LVNCFLRPLR MAASSKKPPI SHDDVSSIFL NSETIMFLHE
     IFHQGLKARI ANWPTLVLAD LFDILLPMLN IYQEFVRNHQ YSLQVLANCK QNRDFDKLLK
     QYESNAACEG RMLETFLTYP MFQIPRYIIT LHELLAHTPH EHVERKSLEF AKSKLEELSR
     VMHDEVSDTE NIRKNLAIER MIVEGCDILL DTSQTFVRQG SLIQLPSVER GKLSKVRLGS
     LSLKKEGERQ CFLFTKHFLI CTRSSGGKLH LLKQGGVLSL IECTLIEEPD ANDEDAKNSG
     QVFGHLDFKI VVEPSDAPAF TVVLLAPSRQ EKAAWTSDIS QCIDNIRCNG LMTSVFEENS
     KVTVPHMIKS DARLHKDDVD ICFSKTLNSC KVPQIRYASV ERLLERLTDL RFLSIDFLNT
     FLHTYRIFTT ATVVMEKLAD IYKKPFTSIP VRSLELFFAT NQNNRSGDHV NDKSPRLCRK
     FSSPPPLSIS SRTSSPVRTR KLSLNSPIGS KVGILDLSTT SSSAASSPTS ANPTISPPPS
     NNNNNSKPPL DLSRGQSPSS PEQSPGALDD NAEVPRIDAL CGKLRRSIRR AVLESVSLDK
     FIPESPQASE PGEISPCRSP STPRHLRYRQ SGVQTAENSR CSVSPASAFA IATAAAGHSS
     PPVFNNSERT CDKEFIIRRA ATNRVLNVLR HWVSKHSQDF EMNGELKMGV ICLLEEVLRD
     PDLLPQERKA TANILSALSQ DDQDDAQLKI EDILQMAECP KAECFESLSA MEIAEQITLL
     DHIVFRSIPY EEFLGQGWMK TDKTERTPYI MKTSQHFNDM SNLVASQIMS HTDVGSRAGS
     IEKWVAVADI CRCLNNYNGV LEITSALNRS AIYRLKKTWA KVCKQTKALM DKLQKTVSSE
     GRFKNLRETL KNCNPPCVPY LGMYLTDLAF IEEGTPNFTE EGLVNFSKMR MISHIIREIR
     QFQQTPYRIE HQPKVTQYLL DKTLIMDEDT LYDLSLKIEP RLPA
 
 
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