RGPS2_MOUSE
ID RGPS2_MOUSE Reviewed; 590 AA.
AC Q9ERD6; Q7TPZ6; Q80YA6; Q8BZ37; Q8BZU2; Q9D2Y7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ras-specific guanine nucleotide-releasing factor RalGPS2;
DE AltName: Full=Ral GEF with PH domain and SH3-binding motif 2;
DE AltName: Full=RalA exchange factor RalGPS2;
GN Name=Ralgps2;
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).
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=12485849; DOI=10.1111/j.1749-6632.2002.tb04621.x;
RA Martegani E., Ceriani M., Tisi R., Berruti G.;
RT "Cloning and characterization of a new Ral-GEF expressed in mouse testis.";
RL Ann. N. Y. Acad. Sci. 973:135-137(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Cecum, Colon, and Vagina;
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 MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Egg;
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 MOTIF.
RX PubMed=10747847; DOI=10.1074/jbc.c000085200;
RA Rebhun J.F., Chen H., Quilliam L.A.;
RT "Identification and characterization of a new family of guanine nucleotide
RT exchange factors for the ras-related GTPase Ral.";
RL J. Biol. Chem. 275:13406-13410(2000).
RN [5]
RP FUNCTION, INTERACTION WITH GRB2 AND PLCG1, SUBCELLULAR LOCATION,
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, DOMAIN, AND MOTIF.
RX PubMed=17462626; DOI=10.1016/j.yexcr.2007.03.016;
RA Ceriani M., Scandiuzzi C., Amigoni L., Tisi R., Berruti G., Martegani E.;
RT "Functional analysis of RalGPS2, a murine guanine nucleotide exchange
RT factor for RalA GTPase.";
RL Exp. Cell Res. 313:2293-2307(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND IDENTIFICATION BY
RP 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-293; SER-296; SER-308;
RP THR-333; SER-336; SER-350 AND SER-429, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, 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).
CC -!- FUNCTION: Guanine nucleotide exchange factor for the small GTPase RALA.
CC May be involved in cytoskeletal organization. May also be involved in
CC the stimulation of transcription in a Ras-independent fashion.
CC {ECO:0000269|PubMed:17462626}.
CC -!- SUBUNIT: Interacts with RALA (By similarity). Interacts with the SH3
CC domains of GRB2 and PLCG1. {ECO:0000250, ECO:0000269|PubMed:17462626}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17462626}. Cell
CC membrane {ECO:0000269|PubMed:17462626}. Note=Associates with membranes
CC through the PH domain.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9ERD6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ERD6-2; Sequence=VSP_031972;
CC Name=3;
CC IsoId=Q9ERD6-3; Sequence=VSP_031973;
CC Name=4;
CC IsoId=Q9ERD6-4; Sequence=VSP_031974, VSP_031975;
CC -!- TISSUE SPECIFICITY: Abundant in brain and testis.
CC {ECO:0000269|PubMed:17462626}.
CC -!- DOMAIN: The PH domain mediates binding to phosphatidylinositol 4,5-
CC bisphosphate. {ECO:0000269|PubMed:17462626}.
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DR EMBL; AF312924; AAG34162.1; -; mRNA.
DR EMBL; AK018622; BAB31312.1; -; mRNA.
DR EMBL; AK033549; BAC28351.1; -; mRNA.
DR EMBL; AK036803; BAC29580.1; -; mRNA.
DR EMBL; AK169368; BAE41116.1; -; mRNA.
DR EMBL; BC043132; AAH43132.1; -; mRNA.
DR EMBL; BC052663; AAH52663.1; -; mRNA.
DR CCDS; CCDS15396.1; -. [Q9ERD6-1]
DR CCDS; CCDS48405.1; -. [Q9ERD6-2]
DR CCDS; CCDS48406.1; -. [Q9ERD6-3]
DR RefSeq; NP_001153437.1; NM_001159965.1. [Q9ERD6-1]
DR RefSeq; NP_001153438.1; NM_001159966.1. [Q9ERD6-1]
DR RefSeq; NP_001153439.1; NM_001159967.1. [Q9ERD6-3]
DR RefSeq; NP_001153440.1; NM_001159968.1. [Q9ERD6-2]
DR RefSeq; NP_076373.3; NM_023884.4. [Q9ERD6-1]
DR RefSeq; XP_006497091.1; XM_006497028.3. [Q9ERD6-1]
DR RefSeq; XP_006497092.1; XM_006497029.2. [Q9ERD6-1]
DR RefSeq; XP_006497093.1; XM_006497030.2. [Q9ERD6-1]
DR RefSeq; XP_006497094.1; XM_006497031.3. [Q9ERD6-1]
DR RefSeq; XP_006497095.1; XM_006497032.3. [Q9ERD6-1]
DR AlphaFoldDB; Q9ERD6; -.
DR SMR; Q9ERD6; -.
DR BioGRID; 219285; 3.
DR STRING; 10090.ENSMUSP00000130581; -.
DR iPTMnet; Q9ERD6; -.
DR PhosphoSitePlus; Q9ERD6; -.
DR jPOST; Q9ERD6; -.
DR MaxQB; Q9ERD6; -.
DR PaxDb; Q9ERD6; -.
DR PRIDE; Q9ERD6; -.
DR ProteomicsDB; 254943; -. [Q9ERD6-1]
DR ProteomicsDB; 254944; -. [Q9ERD6-2]
DR ProteomicsDB; 254945; -. [Q9ERD6-3]
DR ProteomicsDB; 254946; -. [Q9ERD6-4]
DR Antibodypedia; 34414; 101 antibodies from 17 providers.
DR DNASU; 78255; -.
DR Ensembl; ENSMUST00000027886; ENSMUSP00000027886; ENSMUSG00000026594. [Q9ERD6-3]
DR Ensembl; ENSMUST00000063199; ENSMUSP00000063872; ENSMUSG00000026594. [Q9ERD6-1]
DR Ensembl; ENSMUST00000171292; ENSMUSP00000130581; ENSMUSG00000026594. [Q9ERD6-1]
DR Ensembl; ENSMUST00000172057; ENSMUSP00000132533; ENSMUSG00000026594. [Q9ERD6-2]
DR Ensembl; ENSMUST00000185198; ENSMUSP00000139618; ENSMUSG00000026594. [Q9ERD6-4]
DR Ensembl; ENSMUST00000191605; ENSMUSP00000139645; ENSMUSG00000026594. [Q9ERD6-1]
DR GeneID; 78255; -.
DR KEGG; mmu:78255; -.
DR UCSC; uc007dcu.2; mouse. [Q9ERD6-1]
DR UCSC; uc007dcv.2; mouse. [Q9ERD6-3]
DR UCSC; uc007dcy.2; mouse. [Q9ERD6-4]
DR UCSC; uc011wuj.1; mouse. [Q9ERD6-2]
DR CTD; 55103; -.
DR MGI; MGI:1925505; Ralgps2.
DR VEuPathDB; HostDB:ENSMUSG00000026594; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000154079; -.
DR HOGENOM; CLU_021333_0_1_1; -.
DR InParanoid; Q9ERD6; -.
DR OMA; HVSFWTV; -.
DR OrthoDB; 343666at2759; -.
DR PhylomeDB; Q9ERD6; -.
DR TreeFam; TF352150; -.
DR BioGRID-ORCS; 78255; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Ralgps2; mouse.
DR PRO; PR:Q9ERD6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9ERD6; protein.
DR Bgee; ENSMUSG00000026594; Expressed in spermatocyte and 264 other tissues.
DR ExpressionAtlas; Q9ERD6; baseline and differential.
DR Genevisible; Q9ERD6; 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; 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:0032485; P:regulation of Ral protein signal transduction; IEA:InterPro.
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; IPR030708; RalGPS1/2.
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 PANTHER; PTHR23113:SF180; PTHR23113:SF180; 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 Alternative splicing; Cell membrane; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..590
FT /note="Ras-specific guanine nucleotide-releasing factor
FT RalGPS2"
FT /id="PRO_0000322601"
FT DOMAIN 49..287
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 464..576
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 288..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..590
FT /note="Required for stimulation of nucleotide exchange by
FT RALA"
FT /evidence="ECO:0000250"
FT MOTIF 331..334
FT /note="PXXP"
FT COMPBIAS 390..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86X27"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X27"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 20..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031972"
FT VAR_SEQ 423..448
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031973"
FT VAR_SEQ 552..568
FT /note="NSYKFQAGSRMNAMLWF -> ERLDRLGSSTADPNSGS (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031974"
FT VAR_SEQ 569..590
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031975"
FT CONFLICT 252
FT /note="I -> M (in Ref. 1; AAG34162)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="E -> G (in Ref. 3; AAH52663)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="S -> T (in Ref. 2; BAC28351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 65530 MW; 49EAF1951FDF5DB7 CRC64;
MDLMNGQASS VTIAATVSEK SSSSESLSEK GSELKKSFDA VVFDVLKVTP EEYAGQITLM
DVPVFKAIQP DELSSCGWNK KEKYSSAPNA VAFTRRFNHV SFWVVREILH AQTLKIRAEV
LSHYIKTAKK LYELNNLHAL MAVVSGLQSA PIFRLTKTWA LLSRKDKTTF EKLEYVMSKE
DNYKRLRDYI SSLKMTPCIP YLGIYLSDLT YIDSAYPSTG SILENEQRSN LMNNILRIIS
DLQQSCEYDI PILPHVQKYL NSVQYIEELQ KFVEDDNYKL SLKIEPGAST PRSAASREDL
AGPDIGASPQ GGRKSSAAAA AAAAAEGALL PQTPPSPRNL IPHGHRKCHS LGYNFIHKMN
TAEFKSATFP NAGPRHLLDD SVMEPHAPSR GQAESSTLSS GISIGSSDGS ELSEETSWPA
FERNRLYHSL GPVTRVPRNG YRSHTKASSS AESEDLAVHL YPGAVTIQGV LRRKTLLKEG
KKPTVASWTK YWAALCGTQL FYYAAKSLKA TERKHFKSTS NKNVSVVGWM VMMADDPEHP
DLFLLTDSEK GNSYKFQAGS RMNAMLWFKH LSAACQSNKQ QVPTNLMTFE
