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Ral guanine nucleotide dissociation stimulator (RalGDS) (Ral guanine nucleotide exchange factor) (RalGEF)

 GNDS_RAT                Reviewed;         895 AA.
Q03386;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
23-MAY-2018, entry version 139.
RecName: Full=Ral guanine nucleotide dissociation stimulator;
Short=RalGDS;
AltName: Full=Ral guanine nucleotide exchange factor;
Short=RalGEF;
Name=Ralgds;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=8094051;
Albright C.F., Giddings B.W., Liu J., Vito M., Weinberg R.A.;
"Characterization of a guanine nucleotide dissociation stimulator for
a ras-related GTPase.";
EMBO J. 12:339-347(1993).
[2]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 778-864.
PubMed=9253406; DOI=10.1038/nsb0897-609;
Huang L., Weng X., Hofer F., Martin G.S., Kim S.H.;
"Three-dimensional structure of the Ras-interacting domain of
RalGDS.";
Nat. Struct. Biol. 4:609-615(1997).
-!- FUNCTION: Stimulates the dissociation of GDP from the Ras-related
RalA and RalB GTPases which allows GTP binding and activation of
the GTPases. Interacts and acts as an effector molecule for R-Ras,
H-Ras, K-Ras, and Rap.
-!- SUBUNIT: Interacts with RIT1 and RIT2. Interacts (via Ras-
associating domain) with Oog1. {ECO:0000250|UniProtKB:Q03385}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q03385}.
Nucleus {ECO:0000250|UniProtKB:Q03385}. Note=Localizes mainly in
the peripheral region of the cytoplasmic membrane in oocytes and
in preimplantation embryos until the 8-cell stage. Between the
late 1-cell and the early 2-cell stages, nuclear localization
becomes stronger. After the 4-cell stage, not detected in the
nucleus. {ECO:0000250|UniProtKB:Q03385}.
-!- TISSUE SPECIFICITY: Expressed in all tissues examined.
-!- DOMAIN: The Ras-associating domain interacts with Ras.
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EMBL; L07925; AAA41259.1; -; mRNA.
RefSeq; NP_062123.2; NM_019250.2.
UniGene; Rn.40174; -.
PDB; 1LFD; X-ray; 2.10 A; A/C=778-864.
PDB; 1LXD; X-ray; 2.40 A; A/B=767-864.
PDBsum; 1LFD; -.
PDBsum; 1LXD; -.
ProteinModelPortal; Q03386; -.
SMR; Q03386; -.
IntAct; Q03386; 1.
STRING; 10116.ENSRNOP00000013809; -.
iPTMnet; Q03386; -.
PhosphoSitePlus; Q03386; -.
PaxDb; Q03386; -.
PRIDE; Q03386; -.
GeneID; 29622; -.
KEGG; rno:29622; -.
UCSC; RGD:3533; rat.
CTD; 5900; -.
RGD; 3533; Ralgds.
eggNOG; KOG3629; Eukaryota.
eggNOG; ENOG410ZQ4B; LUCA.
HOGENOM; HOG000231592; -.
HOVERGEN; HBG005864; -.
InParanoid; Q03386; -.
KO; K08732; -.
PhylomeDB; Q03386; -.
EvolutionaryTrace; Q03386; -.
PRO; PR:Q03386; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0008321; F:Ral guanyl-nucleotide exchange factor activity; TAS:RGD.
GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:RGD.
CDD; cd00155; RasGEF; 1.
CDD; cd06224; REM; 1.
Gene3D; 1.10.840.10; -; 1.
InterPro; IPR000159; RA_dom.
InterPro; IPR015758; RalGDS.
InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
InterPro; IPR023578; Ras_GEF_dom_sf.
InterPro; IPR001895; RASGEF_cat_dom.
InterPro; IPR036964; RASGEF_cat_dom_sf.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR23113:SF35; PTHR23113:SF35; 1.
Pfam; PF00788; RA; 1.
Pfam; PF00617; RasGEF; 1.
Pfam; PF00618; RasGEF_N; 1.
SMART; SM00314; RA; 1.
SMART; SM00147; RasGEF; 1.
SMART; SM00229; RasGEFN; 1.
SUPFAM; SSF48366; SSF48366; 2.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50200; RA; 1.
PROSITE; PS00720; RASGEF; 1.
PROSITE; PS50009; RASGEF_CAT; 1.
PROSITE; PS50212; RASGEF_NTER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm;
Guanine-nucleotide releasing factor; Nucleus; Reference proteome.
CHAIN 1 895 Ral guanine nucleotide dissociation
stimulator.
/FTId=PRO_0000068879.
DOMAIN 112 237 N-terminal Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00135}.
DOMAIN 367 629 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
DOMAIN 779 866 Ras-associating. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
STRAND 779 789 {ECO:0000244|PDB:1LFD}.
STRAND 791 801 {ECO:0000244|PDB:1LFD}.
HELIX 806 816 {ECO:0000244|PDB:1LFD}.
HELIX 824 826 {ECO:0000244|PDB:1LFD}.
STRAND 827 836 {ECO:0000244|PDB:1LFD}.
STRAND 838 840 {ECO:0000244|PDB:1LFD}.
HELIX 847 850 {ECO:0000244|PDB:1LFD}.
STRAND 858 863 {ECO:0000244|PDB:1LFD}.
SEQUENCE 895 AA; 98869 MW; 43E1674675A4E1C9 CRC64;
MVQRMWAEAS GPIGGAEPLF PGSRRSRSVW DAVRLEVGVP DSCPVVLHSF TQLDPDLPRL
ESSTQEIGEE LINGVIYSIS LRKVQLYPGA TKGQRWLGCE NESALNLYET CKVRTVKAGT
LEKLVEHLVP AFQGSDLSYV TVFLCTYRAF TTTQQVLDLL FKRYGCILPY SSEDGGPQDQ
LKNAISSILG TWLDQYSEDF CQPPDFPCLK QLVAYVQLNM PGSDLERRAH LLLAQLEDLE
PSEVEPEALS PAPVLSLKPA SQLEPAPALL LTPSRAVAST PVREPAPVPV LASSPVVAPA
SELEPALEPP LDPEPTLAPA PELDPTVSQS LHLEPAPVPA PALEPSWPLP ETTENGLCAK
PHLLLFPPDL VAEQFTLMDA ELFKKVVPYH CLGSIWSQRA KKGKEHLAPT IRATVAQFNN
VANCVITTCL GDQSMKASDR ARVVEHWIEV ARECRVLKNF SSLYAILSAL QSNAIHRLKK
TWEEVSRGSF RVFQKLSEIF SDENNYSLSR ELLIKEGTSK FATLEMNPRR TQRRQKETGV
IQGTVPYLGT FLTDLVMLDT AMKDYLYGRL INFEKRRKEF EVIAQIKLLQ SACNNYSIVP
EEHFGAWFRA MGRLSEAESY NLSCELEPPS ESASNTLRSK KSTAIVKRWE RRQAPSTELS
TSSSAHSKSC DQLRCSPYLS SGDITDALSV HSAGSSTSDV EEINMSFVPE SPDGQEKKFW
ESASQSSPET SGISSASSST SSSSASTTPV STTRTHKRSV SGVCSYSSSL PLYNQQVGDC
CIIRVSLDVD NGNMYKSILV TSQDKAPTVI RKAMDKHNLD EDEPEDYELL QIISEDHKLK
IPENANVFYA MNSAANYDFI LKKRAFTKGA KVKHGASSTL PRMKQKGLRI ARGIF


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