DIRA2_MOUSE
ID DIRA2_MOUSE Reviewed; 199 AA.
AC Q5PR73;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=GTP-binding protein Di-Ras2;
DE AltName: Full=Distinct subgroup of the Ras family member 2;
DE Flags: Precursor;
GN Name=Diras2;
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; 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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-126, AND
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: Displays low GTPase activity and exists predominantly in the
CC GTP-bound form. {ECO:0000250|UniProtKB:Q96HU8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Di-Ras family.
CC {ECO:0000305}.
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DR EMBL; BC086799; AAH86799.1; -; mRNA.
DR CCDS; CCDS26516.1; -.
DR RefSeq; NP_001019645.1; NM_001024474.2.
DR RefSeq; XP_006517013.1; XM_006516950.3.
DR AlphaFoldDB; Q5PR73; -.
DR SMR; Q5PR73; -.
DR BioGRID; 212726; 9.
DR IntAct; Q5PR73; 1.
DR STRING; 10090.ENSMUSP00000055416; -.
DR iPTMnet; Q5PR73; -.
DR PhosphoSitePlus; Q5PR73; -.
DR SwissPalm; Q5PR73; -.
DR MaxQB; Q5PR73; -.
DR PaxDb; Q5PR73; -.
DR PRIDE; Q5PR73; -.
DR ProteomicsDB; 279692; -.
DR Antibodypedia; 28067; 137 antibodies from 22 providers.
DR DNASU; 68203; -.
DR Ensembl; ENSMUST00000057442; ENSMUSP00000055416; ENSMUSG00000047842.
DR GeneID; 68203; -.
DR KEGG; mmu:68203; -.
DR UCSC; uc007qmv.1; mouse.
DR CTD; 54769; -.
DR MGI; MGI:1915453; Diras2.
DR VEuPathDB; HostDB:ENSMUSG00000047842; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000158196; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q5PR73; -.
DR OMA; CKETNGA; -.
DR OrthoDB; 1218505at2759; -.
DR PhylomeDB; Q5PR73; -.
DR TreeFam; TF313014; -.
DR BioGRID-ORCS; 68203; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Diras2; mouse.
DR PRO; PR:Q5PR73; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q5PR73; protein.
DR Bgee; ENSMUSG00000047842; Expressed in cerebellar vermis and 172 other tissues.
DR ExpressionAtlas; Q5PR73; baseline and differential.
DR Genevisible; Q5PR73; MM.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..196
FT /note="GTP-binding protein Di-Ras2"
FT /id="PRO_0000191652"
FT PROPEP 197..199
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370779"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT BINDING 33..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT BINDING 152..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 196
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 196
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 199 AA; 22498 MW; C1A69D3145C3EACD CRC64;
MPEQSNDYRV AVFGAGGVGK SSLVLRFVKG TFRESYIPTV EDTYRQVISC DKSICTLQIT
DTTGSHQFPA MQRLSISKGH AFILVYSITS RQSLEELKPI YEQICEIKGD VESIPIMLVG
NKCDESPNRE VQSSEAEALA RTWKCAFMET SAKLNHNVKE LFQELLNLEK RRTVSLQIDG
KKSKQQKRKE KLKGKCVVM
