GNDS_RAT
ID GNDS_RAT Reviewed; 895 AA.
AC Q03386;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Ral guanine nucleotide dissociation stimulator;
DE Short=RalGDS;
DE AltName: Full=Ral guanine nucleotide exchange factor;
DE Short=RalGEF;
GN Name=Ralgds;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=8094051; DOI=10.1002/j.1460-2075.1993.tb05662.x;
RA Albright C.F., Giddings B.W., Liu J., Vito M., Weinberg R.A.;
RT "Characterization of a guanine nucleotide dissociation stimulator for a
RT ras-related GTPase.";
RL EMBO J. 12:339-347(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 778-864.
RX PubMed=9253406; DOI=10.1038/nsb0897-609;
RA Huang L., Weng X., Hofer F., Martin G.S., Kim S.H.;
RT "Three-dimensional structure of the Ras-interacting domain of RalGDS.";
RL Nat. Struct. Biol. 4:609-615(1997).
CC -!- FUNCTION: Functions as a guanine nucleotide exchange factor (GEF)
CC activating either RalA or RalB GTPases and plays an important role in
CC intracellular transport. Interacts and acts as an effector molecule for
CC R-Ras, H-Ras, K-Ras, and Rap. During bacterial clearance, recognizes
CC 'Lys-33'-linked polyubiquitinated TRAF3 and subsequently mediates
CC assembly of the exocyst complex. {ECO:0000250|UniProtKB:Q03385,
CC ECO:0000250|UniProtKB:Q12967}.
CC -!- SUBUNIT: Interacts with RIT1 and RIT2 (By similarity). Interacts with
CC TRAF3. Interacts with HRAS (By similarity).
CC {ECO:0000250|UniProtKB:Q03385, ECO:0000250|UniProtKB:Q12967}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q03385}. Nucleus
CC {ECO:0000250|UniProtKB:Q03385}. Note=Localizes mainly in the peripheral
CC region of the cytoplasmic membrane in oocytes and in preimplantation
CC embryos until the 8-cell stage. Between the late 1-cell and the early
CC 2-cell stages, nuclear localization becomes stronger. After the 4-cell
CC stage, not detected in the nucleus. {ECO:0000250|UniProtKB:Q03385}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC -!- DOMAIN: The Ras-associating domain interacts with Ras.
CC -!- PTM: Phosphorylation of Tyr-795 by MET blocks HRAS binding.
CC {ECO:0000250|UniProtKB:Q03385}.
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; L07925; AAA41259.1; -; mRNA.
DR RefSeq; NP_062123.2; NM_019250.2.
DR PDB; 1LFD; X-ray; 2.10 A; A/C=778-864.
DR PDB; 1LXD; X-ray; 2.40 A; A/B=767-864.
DR PDBsum; 1LFD; -.
DR PDBsum; 1LXD; -.
DR AlphaFoldDB; Q03386; -.
DR SMR; Q03386; -.
DR IntAct; Q03386; 1.
DR STRING; 10116.ENSRNOP00000013809; -.
DR iPTMnet; Q03386; -.
DR PhosphoSitePlus; Q03386; -.
DR PaxDb; Q03386; -.
DR PRIDE; Q03386; -.
DR GeneID; 29622; -.
DR KEGG; rno:29622; -.
DR UCSC; RGD:3533; rat.
DR CTD; 5900; -.
DR RGD; 3533; Ralgds.
DR eggNOG; KOG3629; Eukaryota.
DR InParanoid; Q03386; -.
DR OrthoDB; 940219at2759; -.
DR PhylomeDB; Q03386; -.
DR Reactome; R-RNO-171007; p38MAPK events.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR EvolutionaryTrace; Q03386; -.
DR PRO; PR:Q03386; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030695; F:GTPase regulator activity; ISO:RGD.
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:0007264; P:small GTPase mediated signal transduction; TAS:RGD.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR015758; RalGDS.
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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR PANTHER; PTHR23113:SF35; PTHR23113:SF35; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Guanine-nucleotide releasing factor; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..895
FT /note="Ral guanine nucleotide dissociation stimulator"
FT /id="PRO_0000068879"
FT DOMAIN 112..237
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 367..629
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 779..866
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 301..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 795
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q12967"
FT STRAND 779..789
FT /evidence="ECO:0007829|PDB:1LFD"
FT STRAND 791..801
FT /evidence="ECO:0007829|PDB:1LFD"
FT HELIX 806..816
FT /evidence="ECO:0007829|PDB:1LFD"
FT HELIX 824..826
FT /evidence="ECO:0007829|PDB:1LFD"
FT STRAND 827..836
FT /evidence="ECO:0007829|PDB:1LFD"
FT STRAND 838..840
FT /evidence="ECO:0007829|PDB:1LFD"
FT HELIX 847..850
FT /evidence="ECO:0007829|PDB:1LFD"
FT STRAND 858..863
FT /evidence="ECO:0007829|PDB:1LFD"
SQ 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
