RGL2_MOUSE
ID RGL2_MOUSE Reviewed; 778 AA.
AC Q61193; Q9QUJ2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ral guanine nucleotide dissociation stimulator-like 2;
DE Short=RalGDS-like 2;
DE AltName: Full=RalGDS-like factor;
DE AltName: Full=Ras-associated protein RAB2L;
GN Name=Rgl2; Synonyms=Rab2l, Rlf;
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].
RX PubMed=8710374;
RA Wolthuis R.M.F., Bauer B., Van'T Veer L.J., de Vries-Smits A.M.M.,
RA Cool R.H., Spaargaren M., Wittinghofer A., Burgering B.M.T., Bos J.L.;
RT "RalGDS-like factor (Rlf) is a novel Ras and Rap 1A-associating protein.";
RL Oncogene 13:353-362(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., Hall J., James R., Dors M.,
RA Shaffer T., Abbasi N., Ratcliffe A., Dickhoff R., Lasky S., Hood L.;
RT "Sequence of the mouse major histocompatibility complex class II region.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
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).
RN [5]
RP STRUCTURE BY NMR OF 646-735.
RX PubMed=9753431; DOI=10.1021/bi9811664;
RA Esser D., Bauer B., Wolthuis R.M., Wittinghofer A., Cool R.H., Bayer P.;
RT "Structure determination of the Ras-binding domain of the Ral-specific
RT guanine nucleotide exchange factor Rlf.";
RL Biochemistry 37:13453-13462(1998).
CC -!- FUNCTION: Probable guanine nucleotide exchange factor. Putative
CC effector of Ras and/or Rap. Associates with the GTP-bound form of Rap
CC 1A and H-Ras in vitro.
CC -!- SUBUNIT: Interacts with SAMD9. {ECO:0000250}.
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DR EMBL; U54639; AAC52724.1; -; mRNA.
DR EMBL; AF110520; AAC97974.1; -; Genomic_DNA.
DR EMBL; AF100956; AAC69894.1; -; Genomic_DNA.
DR EMBL; BC068121; AAH68121.1; -; mRNA.
DR CCDS; CCDS28635.1; -.
DR PIR; PC4379; PC4379.
DR RefSeq; NP_033085.2; NM_009059.2.
DR PDB; 1RLF; NMR; -; A=646-735.
DR PDB; 4JGW; X-ray; 2.30 A; A/B=50-514.
DR PDB; 5CM8; X-ray; 2.60 A; A=50-514.
DR PDB; 5CM9; X-ray; 2.60 A; A/B=50-514.
DR PDBsum; 1RLF; -.
DR PDBsum; 4JGW; -.
DR PDBsum; 5CM8; -.
DR PDBsum; 5CM9; -.
DR AlphaFoldDB; Q61193; -.
DR SMR; Q61193; -.
DR IntAct; Q61193; 3.
DR STRING; 10090.ENSMUSP00000041082; -.
DR iPTMnet; Q61193; -.
DR PhosphoSitePlus; Q61193; -.
DR EPD; Q61193; -.
DR jPOST; Q61193; -.
DR MaxQB; Q61193; -.
DR PaxDb; Q61193; -.
DR PeptideAtlas; Q61193; -.
DR PRIDE; Q61193; -.
DR ProteomicsDB; 255248; -.
DR Antibodypedia; 29066; 196 antibodies from 26 providers.
DR DNASU; 19732; -.
DR Ensembl; ENSMUST00000047503; ENSMUSP00000041082; ENSMUSG00000041354.
DR GeneID; 19732; -.
DR KEGG; mmu:19732; -.
DR UCSC; uc008cag.1; mouse.
DR CTD; 5863; -.
DR MGI; MGI:107483; Rgl2.
DR VEuPathDB; HostDB:ENSMUSG00000041354; -.
DR eggNOG; KOG3629; Eukaryota.
DR GeneTree; ENSGT00940000161403; -.
DR HOGENOM; CLU_010252_0_2_1; -.
DR InParanoid; Q61193; -.
DR OMA; IQQWLRG; -.
DR OrthoDB; 940219at2759; -.
DR PhylomeDB; Q61193; -.
DR TreeFam; TF315204; -.
DR BRENDA; 6.2.1.3; 3474.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR BioGRID-ORCS; 19732; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Rgl2; mouse.
DR EvolutionaryTrace; Q61193; -.
DR PRO; PR:Q61193; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q61193; protein.
DR Bgee; ENSMUSG00000041354; Expressed in granulocyte and 267 other tissues.
DR ExpressionAtlas; Q61193; baseline and differential.
DR Genevisible; Q61193; 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:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IDA:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0032485; P:regulation of Ral protein signal transduction; IDA: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; IPR030749; RGL2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR PANTHER; PTHR23113:SF213; PTHR23113:SF213; 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; Guanine-nucleotide releasing factor; Reference proteome.
FT CHAIN 1..778
FT /note="Ral guanine nucleotide dissociation stimulator-like
FT 2"
FT /id="PRO_0000068889"
FT DOMAIN 88..212
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 243..513
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 649..736
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 147
FT /note="H -> Y (in Ref. 1; AAC52724)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="M -> T (in Ref. 1; AAC52724)"
FT /evidence="ECO:0000305"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:4JGW"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:4JGW"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:4JGW"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 149..169
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5CM8"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 244..260
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:4JGW"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:4JGW"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 285..305
FT /evidence="ECO:0007829|PDB:4JGW"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:4JGW"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:4JGW"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 325..344
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 348..359
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 367..371
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:4JGW"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 433..445
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 457..477
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 486..494
FT /evidence="ECO:0007829|PDB:4JGW"
FT HELIX 500..510
FT /evidence="ECO:0007829|PDB:4JGW"
FT STRAND 650..657
FT /evidence="ECO:0007829|PDB:1RLF"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:1RLF"
FT STRAND 668..672
FT /evidence="ECO:0007829|PDB:1RLF"
FT HELIX 680..687
FT /evidence="ECO:0007829|PDB:1RLF"
FT TURN 688..691
FT /evidence="ECO:0007829|PDB:1RLF"
FT STRAND 698..702
FT /evidence="ECO:0007829|PDB:1RLF"
FT TURN 703..706
FT /evidence="ECO:0007829|PDB:1RLF"
FT HELIX 719..722
FT /evidence="ECO:0007829|PDB:1RLF"
FT STRAND 727..733
FT /evidence="ECO:0007829|PDB:1RLF"
SQ SEQUENCE 778 AA; 83826 MW; B23CB882A5416564 CRC64;
MLPRPLRLLL DTTPPGGVVL SSFRSRDPEE GGDPGGRAVG GGQEEEDEEE EEASVSVWDE
EEDGATFTVT SRQYRPLDPL APLPPPRSSR RLRAGTLEAL VRHLLDARTA GADMMFTPAL
LATHRAFTST PALFGLVADR LEALESHPPG ELERTTGVAI SVLSTWLASH PEDFGSEVKG
QLDRLESFLL RTGYAAREGV VGGSADLIRN LRARVDPRAP DLPKPLALPG DSPADPTDVL
VFLADHLAEQ LTLLDAELFL NLIPSQCLGG LWGHRDRPGH SHLCPSVRAT VTQFNKVAGA
VVSSVLGATS IGEGPREVTV RPLRPPQRAR LLEKWIRVAE ECRLLRNFSS VYAVVSALQS
SPIHRLRAAW GETTRDSLRV FSSLCQIFSE EDNYSQSREL LMQEVKPQPP VEPHSKKAPR
SGFRGGGVVP YLGTFLKDLV MLDAASKDEL ENGYINFDKR RKEFAILSEL LRLQKECRGY
DLRPNSDIQQ WLQGLQPLTE AQSHRVSCEV EPPGTSDSPA ARTPRPTLVI TQWTEVLGSV
GGPTPLVSWD RPSVGGDEVP GTPAPLLTRL AQHMKWPSVS SLDSALESSP SLHSPADPGH
LSPPASSPRP SRGHRRSASC GSPLSGNTGE GTSRSAGCGG GVSGPGSSDC RIIRVQMELG
EDGSVYKSIL VTSQDKAPSV ISRVLKKNNR DSAVASEFEL VQLLPGDREL TIPHSANVFY
AMDGASHDFL LRQRRRPSAA TPGSHSGPSA SGTPPSEGGG GSFPRIKATG RKIARALF
