ID   RRAS2_MOUSE             Reviewed;         204 AA.
AC   P62071; P17082; Q3TA79; Q8C5D1; Q9D0H6;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   04-NOV-2026, entry version 182.
DE   RecName: Full=Ras-related protein R-Ras2;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P62070};
DE   Flags: Precursor;
GN   Name=Rras2 {ECO:0000312|MGI:MGI:1914172};
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].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Colon, Embryo, and Spleen;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   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: GTP-binding protein with GTPase activity, involved in the
CC       regulation of MAPK signaling pathway and thereby controlling multiple
CC       cellular processes (By similarity). Regulates craniofacial development
CC       (By similarity). {ECO:0000250|UniProtKB:P62070}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P62070};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P62070};
CC   -!- SUBUNIT: Interacts with RASSF5. {ECO:0000250|UniProtKB:P62070}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P62070};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P62070}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P62070}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P62070}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P62070}.
CC   -!- PTM: May be post-translationally modified by both palmitoylation and
CC       polyisoprenylation. {ECO:0000250|UniProtKB:P62070}.
CC   -!- PTM: Fatty-acylation at Lys-192, Lys-194; lys-196 and Lys-197 is
CC       required for localization to the plasma membrane and activity. Defatty-
CC       acylated by SIRT6, affecting its localization to the plasma membrane.
CC       {ECO:0000250|UniProtKB:P62070}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; AK011419; BAB27607.1; -; mRNA.
DR   EMBL; AK078870; BAC37432.1; -; mRNA.
DR   EMBL; AK172037; BAE42790.1; -; mRNA.
DR   EMBL; BC003871; AAH03871.1; -; mRNA.
DR   CCDS; CCDS21758.1; -.
DR   RefSeq; NP_080122.2; NM_025846.2.
DR   AlphaFoldDB; P62071; -.
DR   SMR; P62071; -.
DR   BioGRID; 211811; 10.
DR   FunCoup; P62071; 2055.
DR   STRING; 10090.ENSMUSP00000069752; -.
DR   GlyGen; P62071; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62071; -.
DR   PhosphoSitePlus; P62071; -.
DR   SwissPalm; P62071; -.
DR   jPOST; P62071; -.
DR   PaxDb; 10090-ENSMUSP00000069752; -.
DR   PeptideAtlas; P62071; -.
DR   ProteomicsDB; 262707; -.
DR   Pumba; P62071; -.
DR   Antibodypedia; 4173; 293 antibodies from 38 providers.
DR   DNASU; 66922; -.
DR   Ensembl; ENSMPUT00000013278; ENSMPUP00000013067; ENSMPUG00000013165.
DR   Ensembl; ENSMUST00000069449.7; ENSMUSP00000069752.6; ENSMUSG00000055723.7.
DR   GeneID; 66922; -.
DR   KEGG; mmu:66922; -.
DR   UCSC; uc009jhw.2; mouse.
DR   AGR; MGI:1914172; -.
DR   CTD; 22800; -.
DR   MGI; MGI:1914172; Rras2.
DR   VEuPathDB; HostDB:ENSMUSG00000055723; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000155328; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; P62071; -.
DR   OMA; AARLDXF; -.
DR   OrthoDB; 5976022at2759; -.
DR   PhylomeDB; P62071; -.
DR   Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR   BioGRID-ORCS; 66922; 3 hits in 76 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:P62071; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P62071; protein.
DR   Bgee; ENSMUSG00000055723; Expressed in ureter smooth muscle and 249 other cell types or tissues.
DR   ExpressionAtlas; P62071; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR   GO; GO:0030335; P:positive regulation of cell migration; IGI:MGI.
DR   GO; GO:0007265; P:Ras protein signal transduction; IDA:MGI.
DR   CDD; cd04145; M_R_Ras_like; 1.
DR   FunFam; 3.40.50.300:FF:000080; Ras-like GTPase Ras1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR020849; Small_GTPase_Ras-type.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR24070; RAS, DI-RAS, AND RHEB FAMILY MEMBERS OF SMALL GTPASE SUPERFAMILY; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Golgi apparatus; GTP-binding; Hydrolase;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding; Palmitate;
KW   Phosphoprotein; Prenylation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   CHAIN           2..201
FT                   /note="Ras-related protein R-Ras2"
FT                   /id="PRO_0000082653"
FT   PROPEP          202..204
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P10114"
FT                   /id="PRO_0000281303"
FT   MOTIF           43..51
FT                   /note="Effector region"
FT   BINDING         21..29
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   BINDING         68..72
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P01112"
FT   BINDING         127..130
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   BINDING         157..159
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         201
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   LIPID           192
FT                   /note="N6-palmitoyl lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   LIPID           194
FT                   /note="N6-palmitoyl lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   LIPID           196
FT                   /note="N6-palmitoyl lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   LIPID           197
FT                   /note="N6-palmitoyl lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   LIPID           199
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   LIPID           201
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P62070"
FT   CONFLICT        4
FT                   /note="A -> D (in Ref. 1; BAC37432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96
FT                   /note="T -> R (in Ref. 1; BAB27607)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   204 AA;  23400 MW;  BA7D4759DC49446F CRC64;
     MAAAGWRDGS GQEKYRLVVV GGGGVGKSAL TIQFIQSYFV TDYDPTIEDS YTKQCVIDDR
     AARLDILDTA GQEEFGAMRE QYMRTGEGFL LVFSVTDRGS FEEIYKFQRQ ILRVKDRDEF
     PMILIGNKAD LDHQRQVTQE EGQQLARQLK VTYMEASAKI RMNVDQAFHE LVRVIRKFQE
     QECPPSPEPT RKEKDKKGCH CVIF
//