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DIRA1_MOUSE
ID   DIRA1_MOUSE             Reviewed;         198 AA.
AC   Q91Z61;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=GTP-binding protein Di-Ras1;
DE   AltName: Full=Distinct subgroup of the Ras family member 1;
DE   AltName: Full=Small GTP-binding tumor suppressor 1;
DE   Flags: Precursor;
GN   Name=Diras1; Synonyms=Gbts1;
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].
RC   STRAIN=129/SvJ;
RA   Gong L., Wu K.;
RT   "Molecular cloning of GBTS1, a novel gene encoding a small GTP-binding
RT   tumor suppressor.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
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:O95057}.
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; AY059640; AAL17967.1; -; mRNA.
DR   EMBL; BC057556; AAH57556.1; -; mRNA.
DR   CCDS; CCDS24040.1; -.
DR   RefSeq; NP_660252.1; NM_145217.2.
DR   RefSeq; XP_006513501.1; XM_006513438.3.
DR   AlphaFoldDB; Q91Z61; -.
DR   SMR; Q91Z61; -.
DR   IntAct; Q91Z61; 1.
DR   MINT; Q91Z61; -.
DR   STRING; 10090.ENSMUSP00000055605; -.
DR   iPTMnet; Q91Z61; -.
DR   PhosphoSitePlus; Q91Z61; -.
DR   SwissPalm; Q91Z61; -.
DR   MaxQB; Q91Z61; -.
DR   PaxDb; Q91Z61; -.
DR   PeptideAtlas; Q91Z61; -.
DR   PRIDE; Q91Z61; -.
DR   ProteomicsDB; 277453; -.
DR   Antibodypedia; 23037; 243 antibodies from 27 providers.
DR   DNASU; 208666; -.
DR   Ensembl; ENSMUST00000055125; ENSMUSP00000055605; ENSMUSG00000043670.
DR   GeneID; 208666; -.
DR   KEGG; mmu:208666; -.
DR   UCSC; uc007gfo.1; mouse.
DR   CTD; 148252; -.
DR   MGI; MGI:2183442; Diras1.
DR   VEuPathDB; HostDB:ENSMUSG00000043670; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000159915; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; Q91Z61; -.
DR   OMA; MMKEVKG; -.
DR   OrthoDB; 1218505at2759; -.
DR   PhylomeDB; Q91Z61; -.
DR   TreeFam; TF313014; -.
DR   BioGRID-ORCS; 208666; 1 hit in 73 CRISPR screens.
DR   PRO; PR:Q91Z61; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q91Z61; protein.
DR   Bgee; ENSMUSG00000043670; Expressed in retinal neural layer and 101 other tissues.
DR   ExpressionAtlas; Q91Z61; baseline and differential.
DR   Genevisible; Q91Z61; 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; ISO:MGI.
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; Prenylation; Reference proteome.
FT   CHAIN           1..195
FT                   /note="GTP-binding protein Di-Ras1"
FT                   /id="PRO_0000191649"
FT   PROPEP          196..198
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370776"
FT   MOTIF           36..44
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   BINDING         17..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O95057"
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..125
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O95057"
FT   BINDING         151..152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT   BINDING         151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O95057"
FT   MOD_RES         195
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           195
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   198 AA;  22265 MW;  2033DE94B27A5B9D CRC64;
     MPEQSNDYRV VVFGAGGVGK SSLVLRFVKG TFRDTYIPTI EDTYRQVISC DKSVCTLQIT
     DTTGSHQFPA MQRLSISKGH AFILVFSVTS KQSLDELSPI YKLIVQIKGS VEDIPIMLVG
     NKCDETQREV HTREAQAVAQ EWKCAFMETS AKMNYNVKEL FQELLTLETR RSVSLSVDGK
     RSSKQKRADR IKGKCALM
 
 
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