RGL3_MOUSE
ID RGL3_MOUSE Reviewed; 709 AA.
AC Q3UYI5; Q6KAR7; Q8BKD3; Q924M8; Q9DBL8; Q9JID4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ral guanine nucleotide dissociation stimulator-like 3;
DE Short=RalGDS-like 3;
DE AltName: Full=RalGDS-related effector protein of M-Ras;
DE AltName: Full=Ras pathway modulator;
DE Short=RPM;
GN Name=Rgl3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RIT1 AND
RP HRAS, DOMAIN, AND TISSUE SPECIFICITY.
RX PubMed=10869344; DOI=10.1074/jbc.m002241200;
RA Shao H., Andres D.A.;
RT "A novel RalGEF-like protein, RGL3, as a candidate effector for rit and
RT Ras.";
RL J. Biol. Chem. 275:26914-26924(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH HRAS AND
RP MRAS, AND TISSUE SPECIFICITY.
RX PubMed=11313946; DOI=10.1038/sj.onc.1204053;
RA Ehrhardt G.R., Korherr C., Wieler J.S., Knaus M., Schrader J.W.;
RT "A novel potential effector of M-Ras and p21 Ras negatively regulates p21
RT Ras-mediated gene induction and cell growth.";
RL Oncogene 20:188-197(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Eye, Liver, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 180-684 (ISOFORM 1).
RC STRAIN=ICR; TISSUE=Embryonic tail;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [5]
RP PROTEIN SEQUENCE OF 362-368, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510; SER-568 AND SER-572, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506; SER-510; SER-553;
RP SER-568; SER-572 AND SER-577, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for Ral-A. Potential
CC effector of GTPase HRas and Ras-related protein M-Ras. Negatively
CC regulates Elk-1-dependent gene induction downstream of HRas and MEKK1.
CC {ECO:0000269|PubMed:10869344, ECO:0000269|PubMed:11313946}.
CC -!- SUBUNIT: Interacts with GTP-bound forms of RIT1, HRAS and MRAS.
CC {ECO:0000269|PubMed:10869344, ECO:0000269|PubMed:11313946}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UYI5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UYI5-2; Sequence=VSP_028471, VSP_028472, VSP_028473,
CC VSP_028474;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the
CC liver and kidney. {ECO:0000269|PubMed:10869344,
CC ECO:0000269|PubMed:11313946}.
CC -!- DOMAIN: The Ras-associating domain plays a central role in the
CC activation of Ral-A GDP/GTP exchange activity.
CC {ECO:0000269|PubMed:10869344}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35425.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF237669; AAF78208.1; -; mRNA.
DR EMBL; AF239661; AAK91126.1; -; mRNA.
DR EMBL; AK004876; BAB23634.1; -; mRNA.
DR EMBL; AK053550; BAC35425.1; ALT_FRAME; mRNA.
DR EMBL; AK134654; BAE22227.1; -; mRNA.
DR EMBL; AK131140; BAD21390.1; -; Transcribed_RNA.
DR CCDS; CCDS22916.1; -. [Q3UYI5-1]
DR RefSeq; NP_076111.2; NM_023622.4. [Q3UYI5-1]
DR AlphaFoldDB; Q3UYI5; -.
DR SMR; Q3UYI5; -.
DR BioGRID; 214896; 4.
DR STRING; 10090.ENSMUSP00000035726; -.
DR iPTMnet; Q3UYI5; -.
DR PhosphoSitePlus; Q3UYI5; -.
DR jPOST; Q3UYI5; -.
DR MaxQB; Q3UYI5; -.
DR PaxDb; Q3UYI5; -.
DR PeptideAtlas; Q3UYI5; -.
DR PRIDE; Q3UYI5; -.
DR ProteomicsDB; 255320; -. [Q3UYI5-1]
DR ProteomicsDB; 255321; -. [Q3UYI5-2]
DR Antibodypedia; 52109; 33 antibodies from 12 providers.
DR DNASU; 71746; -.
DR Ensembl; ENSMUST00000045726; ENSMUSP00000035726; ENSMUSG00000040146. [Q3UYI5-1]
DR Ensembl; ENSMUST00000214026; ENSMUSP00000148965; ENSMUSG00000040146. [Q3UYI5-1]
DR GeneID; 71746; -.
DR KEGG; mmu:71746; -.
DR UCSC; uc009onf.1; mouse. [Q3UYI5-1]
DR CTD; 57139; -.
DR MGI; MGI:1918996; Rgl3.
DR VEuPathDB; HostDB:ENSMUSG00000040146; -.
DR eggNOG; KOG3629; Eukaryota.
DR GeneTree; ENSGT00940000161935; -.
DR HOGENOM; CLU_010252_1_1_1; -.
DR InParanoid; Q3UYI5; -.
DR OMA; FEHLCET; -.
DR OrthoDB; 940219at2759; -.
DR PhylomeDB; Q3UYI5; -.
DR TreeFam; TF315204; -.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR BioGRID-ORCS; 71746; 3 hits in 70 CRISPR screens.
DR PRO; PR:Q3UYI5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3UYI5; protein.
DR Bgee; ENSMUSG00000040146; Expressed in cerebellar cortex and 118 other tissues.
DR ExpressionAtlas; Q3UYI5; baseline and differential.
DR Genevisible; Q3UYI5; MM.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
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:MGI.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
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; IPR030750; RGL3.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR PANTHER; PTHR23113:SF220; PTHR23113:SF220; 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 Alternative splicing; Direct protein sequencing;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome.
FT CHAIN 1..709
FT /note="Ral guanine nucleotide dissociation stimulator-like
FT 3"
FT /id="PRO_0000306800"
FT DOMAIN 64..201
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 248..503
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 612..699
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 26..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..706
FT /note="Interaction with HRAS, MRAS and RIT1"
FT /evidence="ECO:0000269|PubMed:10869344,
FT ECO:0000269|PubMed:11313946"
FT COMPBIAS 30..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3MIN7"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028471"
FT VAR_SEQ 100..125
FT /note="RAFVPTARVLGFLLPPPPPPPPPPAG -> MAPCTASPCGGSAASARPQRGL
FT EKAR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028472"
FT VAR_SEQ 442
FT /note="G -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028473"
FT VAR_SEQ 443..709
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028474"
FT CONFLICT 179
FT /note="A -> V (in Ref. 1; AAF78208)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="R -> K (in Ref. 3; BAB23634)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="I -> N (in Ref. 3; BAE22227)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="A -> T (in Ref. 3; BAC35425)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="N -> K (in Ref. 3; BAC35425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 77945 MW; 60F7CEA71873E609 CRC64;
MERTAGKELA LAPLQDWGEE TEDGAVYSVS LRRQRSQRST PERSGEGQTP IPATDTFLHY
RTSKVRALRA ARLERLVHEL VSGDREQDPG FVPAFLATHR AFVPTARVLG FLLPPPPPPP
PPPAGVDSKR TEGQDLNFSK NLRAVVSVLG SWLRNHPQDF RDPPDHQNLG NVRIFLGWAA
PGGAEAREAE KLLEDFLKEA KGEQTEEEKR LAWSGPPRIA QTPGSEFAED CVEEEGPSSE
GPELLDFSVD DVAEQLTLMD VELFLRVRSC ECLGSMWSQR DRPGAAGISP TVRATVAQFN
TVTGCVLGSV LAAPGLAASQ RAQRIEKWIR IAQRCRELRN FSSLRAILSA LQSNPIYRLK
RSWGAVSREP LSVFRKLSQI FSDEDNHLSS RAILSQEETT EDDDCPSGSL PSKLPPGPVP
YLGTFLTDLV MLDTALPDTL KGNLINFEKR RKEWEILARI QQLQQRCQRY SLSPRPPILA
ALRAQRQLSE EQSYRVSRVI EPPAASCPSS PRIRRRISLT KRLSAKLSRE KNSSPGGSPG
DPSSPTSSVS PGSPPSSPRN REPPPPGSPP ASPGPQSPST KLSLTMDPPG PWPVTLTPSS
SRVPLLGQQT SEARVIRVSI NNNHGNLYRS ILLTCQDKAP SVVQRALEKH NVPQPWARDY
QLFQVLPGDR ELLIPDGANV FYAMSPAAPG DFLLRRKEGT GHTLSASPT
