RRAS2_MOUSE
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 03-AUG-2022, entry version 163.
DE RecName: Full=Ras-related protein R-Ras2;
DE EC=3.6.5.- {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, Pancreas,
RC 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, thereby controlling multiple
CC cellular processes. Involved in the regulation of MAPK signaling
CC pathway. Regulation of craniofacial development.
CC {ECO:0000250|UniProtKB:P62070}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
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; 9.
DR STRING; 10090.ENSMUSP00000069752; -.
DR iPTMnet; P62071; -.
DR PhosphoSitePlus; P62071; -.
DR SwissPalm; P62071; -.
DR EPD; P62071; -.
DR jPOST; P62071; -.
DR MaxQB; P62071; -.
DR PaxDb; P62071; -.
DR PeptideAtlas; P62071; -.
DR PRIDE; P62071; -.
DR ProteomicsDB; 262707; -.
DR Antibodypedia; 4173; 274 antibodies from 36 providers.
DR DNASU; 66922; -.
DR Ensembl; ENSMUST00000069449; ENSMUSP00000069752; ENSMUSG00000055723.
DR GeneID; 66922; -.
DR KEGG; mmu:66922; -.
DR UCSC; uc009jhw.2; mouse.
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; KNKRGCH; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; P62071; -.
DR TreeFam; TF312796; -.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 66922; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Rras2; mouse.
DR PRO; PR:P62071; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P62071; protein.
DR Bgee; ENSMUSG00000055723; Expressed in ureter smooth muscle and 246 other tissues.
DR ExpressionAtlas; P62071; baseline and differential.
DR Genevisible; P62071; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:1900149; P:positive regulation of Schwann cell migration; IGI:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:MGI.
DR GO; GO:1901214; P:regulation of neuron death; ISO:MGI.
DR GO; GO:0036135; P:Schwann cell migration; IGI:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 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
