RASE_MOUSE
ID RASE_MOUSE Reviewed; 227 AA.
AC Q7TN89;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=GTPase ERas;
DE Short=E-Ras;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=Embryonic stem cell-expressed Ras;
DE Flags: Precursor;
GN Name=Eras;
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], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH PIK3CD.
RX PubMed=12774123; DOI=10.1038/nature01646;
RA Takahashi K., Mitsui K., Yamanaka S.;
RT "Role of Eras in promoting tumor-like properties in mouse embryonic stem
RT cells.";
RL Nature 423:541-545(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity. Plays an important role in the tumor-like growth properties
CC of embryonic stem cells. {ECO:0000269|PubMed:12774123}.
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; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P01116};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBUNIT: Interacts with PIK3CD. {ECO:0000269|PubMed:12774123}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in several undifferentiated mouse
CC embryonic stem cell lines. {ECO:0000269|PubMed:12774123}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; AB093573; BAC76996.1; -; mRNA.
DR EMBL; AK141212; BAE24591.1; -; mRNA.
DR CCDS; CCDS29980.1; -.
DR RefSeq; NP_853526.1; NM_181548.2.
DR AlphaFoldDB; Q7TN89; -.
DR SMR; Q7TN89; -.
DR STRING; 10090.ENSMUSP00000033500; -.
DR iPTMnet; Q7TN89; -.
DR PhosphoSitePlus; Q7TN89; -.
DR PaxDb; Q7TN89; -.
DR PRIDE; Q7TN89; -.
DR ProteomicsDB; 254986; -.
DR Antibodypedia; 25880; 433 antibodies from 31 providers.
DR DNASU; 353283; -.
DR Ensembl; ENSMUST00000033500; ENSMUSP00000033500; ENSMUSG00000031160.
DR GeneID; 353283; -.
DR KEGG; mmu:353283; -.
DR UCSC; uc009sng.1; mouse.
DR CTD; 3266; -.
DR MGI; MGI:2665023; Eras.
DR VEuPathDB; HostDB:ENSMUSG00000031160; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000162901; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q7TN89; -.
DR OMA; KAMCRCG; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; Q7TN89; -.
DR TreeFam; TF312796; -.
DR BioGRID-ORCS; 353283; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q7TN89; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q7TN89; protein.
DR Bgee; ENSMUSG00000031160; Expressed in interventricular septum and 17 other tissues.
DR ExpressionAtlas; Q7TN89; baseline and differential.
DR Genevisible; Q7TN89; MM.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
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:0007265; P:Ras protein signal transduction; IBA:GO_Central.
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 Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Palmitate; Prenylation; Reference proteome.
FT CHAIN 1..224
FT /note="GTPase ERas"
FT /id="PRO_0000247540"
FT PROPEP 225..227
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000247541"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 70..78
FT /note="Effector region"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 95..99
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 151..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 224
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 220
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 222
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 224
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 24321 MW; 0F0EC10163027FCE CRC64;
MALPTKSSIL DLSSGTPCTR SPEESHEAWA QCKDAGRQLP EYKAVVVGAS GVGKSALTIQ
MTHQCFVKDH DPTIQDSYWK EVARDNGGYI LNVLDTSGQD IHRALRDQCL ASGDGVLGVF
ALDDPSSLDQ LQQIWSTWTP HHKQPLVLVG NKCDLVTTAG DAHAAAALLA HKLGAPLVKT
SAKTRQGVEE AFALLVHEIQ RAQEAVAESS KKTRHQKAVC SCGCSVA
