RGPS1_MOUSE
ID RGPS1_MOUSE Reviewed; 585 AA.
AC A2AR50; A2AR51; A2AR52; Q6GQS4; Q6ZQD2; Q8BVR9; Q8C1I2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ras-specific guanine nucleotide-releasing factor RalGPS1;
DE AltName: Full=Ral GEF with PH domain and SH3-binding motif 1;
DE AltName: Full=Ral guanine nucleotide exchange factor 2;
DE Short=RalGEF 2;
DE AltName: Full=RalA exchange factor RalGPS1;
GN Name=Ralgps1; Synonyms=Kiaa0351, Ralgef2, Ralgps1a;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 for the small GTPase RALA.
CC May be involved in cytoskeleton organization. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the SH3 domains of GRB2, NCK1, PLCG1 and SRC.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Associates with membranes through the PH domain.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A2AR50-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AR50-2; Sequence=VSP_033482, VSP_033485;
CC Name=3;
CC IsoId=A2AR50-3; Sequence=VSP_033486;
CC Name=4;
CC IsoId=A2AR50-4; Sequence=VSP_033483, VSP_033484;
CC -!- DOMAIN: The PH domain mediates binding to membranes. It is required for
CC efficient GEF activity. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25535.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25535.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC97933.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM22215.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM25545.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK129123; BAC97933.1; ALT_INIT; mRNA.
DR EMBL; AK017939; BAC25535.1; ALT_SEQ; mRNA.
DR EMBL; AK076767; BAC36473.1; -; mRNA.
DR EMBL; AL845277; CAM22214.1; -; Genomic_DNA.
DR EMBL; AL929197; CAM22214.1; JOINED; Genomic_DNA.
DR EMBL; AL845277; CAM22215.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL929197; CAM22215.1; JOINED; Genomic_DNA.
DR EMBL; AL845277; CAM22216.1; -; Genomic_DNA.
DR EMBL; AL929197; CAM22216.1; JOINED; Genomic_DNA.
DR EMBL; AL845277; CAM22217.1; -; Genomic_DNA.
DR EMBL; AL929197; CAM25544.1; -; Genomic_DNA.
DR EMBL; AL845277; CAM25544.1; JOINED; Genomic_DNA.
DR EMBL; AL929197; CAM25545.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL845277; CAM25545.1; JOINED; Genomic_DNA.
DR EMBL; AL929197; CAM25546.1; -; Genomic_DNA.
DR EMBL; AL845277; CAM25546.1; JOINED; Genomic_DNA.
DR EMBL; BC072656; AAH72656.1; -; mRNA.
DR CCDS; CCDS15939.1; -. [A2AR50-1]
DR CCDS; CCDS71031.1; -. [A2AR50-2]
DR CCDS; CCDS79779.1; -. [A2AR50-3]
DR RefSeq; NP_001277499.1; NM_001290570.1. [A2AR50-2]
DR RefSeq; NP_001277501.1; NM_001290572.1. [A2AR50-3]
DR RefSeq; NP_780420.1; NM_175211.5. [A2AR50-1]
DR RefSeq; XP_006498095.1; XM_006498032.2. [A2AR50-1]
DR PDB; 2DTC; X-ray; 1.70 A; A/B=460-585.
DR PDBsum; 2DTC; -.
DR AlphaFoldDB; A2AR50; -.
DR SMR; A2AR50; -.
DR STRING; 10090.ENSMUSP00000088563; -.
DR iPTMnet; A2AR50; -.
DR PhosphoSitePlus; A2AR50; -.
DR MaxQB; A2AR50; -.
DR PaxDb; A2AR50; -.
DR PeptideAtlas; A2AR50; -.
DR PRIDE; A2AR50; -.
DR ProteomicsDB; 254939; -. [A2AR50-1]
DR ProteomicsDB; 254940; -. [A2AR50-2]
DR ProteomicsDB; 254941; -. [A2AR50-3]
DR ProteomicsDB; 254942; -. [A2AR50-4]
DR Antibodypedia; 30625; 72 antibodies from 17 providers.
DR DNASU; 241308; -.
DR Ensembl; ENSMUST00000042615; ENSMUSP00000048451; ENSMUSG00000038831. [A2AR50-2]
DR Ensembl; ENSMUST00000091039; ENSMUSP00000088563; ENSMUSG00000038831. [A2AR50-1]
DR Ensembl; ENSMUST00000131298; ENSMUSP00000118363; ENSMUSG00000038831. [A2AR50-3]
DR GeneID; 241308; -.
DR KEGG; mmu:241308; -.
DR UCSC; uc008jhm.2; mouse. [A2AR50-1]
DR UCSC; uc008jhn.2; mouse. [A2AR50-3]
DR UCSC; uc008jho.2; mouse. [A2AR50-2]
DR CTD; 9649; -.
DR MGI; MGI:1922008; Ralgps1.
DR VEuPathDB; HostDB:ENSMUSG00000038831; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000154079; -.
DR HOGENOM; CLU_021333_0_1_1; -.
DR InParanoid; A2AR50; -.
DR OMA; GPCICAL; -.
DR OrthoDB; 343666at2759; -.
DR PhylomeDB; A2AR50; -.
DR TreeFam; TF352150; -.
DR BioGRID-ORCS; 241308; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ralgps1; mouse.
DR EvolutionaryTrace; A2AR50; -.
DR PRO; PR:A2AR50; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AR50; protein.
DR Bgee; ENSMUSG00000038831; Expressed in cortical plate and 183 other tissues.
DR ExpressionAtlas; A2AR50; baseline and differential.
DR Genevisible; A2AR50; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO: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:0032485; P:regulation of Ral protein signal transduction; ISO:MGI.
DR CDD; cd00155; RasGEF; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00617; RasGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Reference proteome.
FT CHAIN 1..585
FT /note="Ras-specific guanine nucleotide-releasing factor
FT RalGPS1"
FT /id="PRO_0000333193"
FT DOMAIN 50..289
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 459..571
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 289..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..585
FT /note="Required for stimulation of nucleotide exchange by
FT RALA"
FT /evidence="ECO:0000250"
FT MOTIF 330..333
FT /note="PXXP"
FT COMPBIAS 380..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 56..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_033482"
FT VAR_SEQ 205..243
FT /note="IYLLDLIYIDSAYPASGSIMENEQRSNQMNNILRIIADL -> MSLSYFIIN
FT FPGNITCSGPNKMFLQFLVEMFPGSSRDHG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033483"
FT VAR_SEQ 244..585
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033484"
FT VAR_SEQ 346..417
FT /note="NLMCQLSVVESKSATFPSEKARHLLDDSVLESRSPRRGLTHTSSTAITNGLS
FT LGSSESSEFSEEMSAGLESR -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_033485"
FT VAR_SEQ 347..416
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033486"
FT CONFLICT 96
FT /note="R -> L (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="Q -> H (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="E -> K (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="R -> K (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 123..134
FT /note="SHFVKIAKKLLE -> TPCPVKNRPNKLSNN (in Ref. 2;
FT BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="L -> H (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..155
FT /note="SAPIFR -> IATIFL (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="L -> P (in Ref. 4; AAH72656)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="R -> L (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="K -> M (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="L -> P (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="N -> I (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="G -> C (in Ref. 2; BAC25535)"
FT /evidence="ECO:0000305"
FT STRAND 462..473
FT /evidence="ECO:0007829|PDB:2DTC"
FT STRAND 484..491
FT /evidence="ECO:0007829|PDB:2DTC"
FT STRAND 494..503
FT /evidence="ECO:0007829|PDB:2DTC"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:2DTC"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:2DTC"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:2DTC"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:2DTC"
FT STRAND 547..552
FT /evidence="ECO:0007829|PDB:2DTC"
FT HELIX 556..570
FT /evidence="ECO:0007829|PDB:2DTC"
SQ SEQUENCE 585 AA; 65475 MW; 96579853188EC18F CRC64;
MYKRNGLMAS VLVTSATPQG SSSSDSLEGQ SCDYASKSYD AVVFDVLKVT PEEFASQITL
MDIPVFKAIQ PEELASCGWS KKEKHSLAPN VVAFTRRFNQ VSFWVVREIL TAQTLKIRAE
ILSHFVKIAK KLLELNNLHS LMSVVSALQS APIFRLTKTW ALLNRKDKTT FEKLDYLMSK
EDNYKRTRDY IRSLKMVPSI PYLGIYLLDL IYIDSAYPAS GSIMENEQRS NQMNNILRII
ADLQVSCSYD HLTTLPHVQK YLKSVRYIEE LQKFVEDDNY KLSLRIEPGS SSPRLVSSKE
DLAGPSAGSS SARFRRRPTC PDTSVAGSLP TPPVPRHRKS HSLGNNLMCQ LSVVESKSAT
FPSEKARHLL DDSVLESRSP RRGLTHTSST AITNGLSLGS SESSEFSEEM SAGLESRGRL
YATLGPNWRV PVRNSPRTRS CVYSPTSPCT CTVGSSATVP TMEGPLRRKT LLKEGRKPAL
SSWTRYWVVL SGATLLYYGA KSLRGTDRKH YKSTPGKKVS IVGWMVQLPD DPEHPDIFQL
NNPDKGNVYK FQTGSRFHAI LWHKHLDDAC KSSRPQVPAN LMSFE
