DIRA1_HUMAN
ID DIRA1_HUMAN Reviewed; 198 AA.
AC O95057;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=GTP-binding protein Di-Ras1;
DE AltName: Full=Distinct subgroup of the Ras family member 1;
DE AltName: Full=Ras-related inhibitor of cell growth;
DE Short=Rig;
DE AltName: Full=Small GTP-binding tumor suppressor 1;
DE Flags: Precursor;
GN Name=DIRAS1; Synonyms=GBTS1, RIG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GTPASE ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12194967; DOI=10.1074/jbc.m202150200;
RA Kontani K., Tada M., Ogawa T., Okai T., Saito K., Araki Y., Katada T.;
RT "Di-Ras, a distinct subgroup of ras family GTPases with unique biochemical
RT properties.";
RL J. Biol. Chem. 277:41070-41078(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12107278; DOI=10.1073/pnas.142193799;
RA Ellis C.A., Vos M.D., Howell H., Vallecorsa T., Fults D.W., Clark G.J.;
RT "Rig is a novel Ras-related protein and potential neural tumor
RT suppressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9876-9881(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Cismowski M.J., Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH GTP ANALOG.
RG Structural genomics consortium (SGC);
RT "The crystal structure of the human DiRas1 GTPase in the inactive GDP bound
RT state.";
RL Submitted (MAR-2006) to the PDB data bank.
CC -!- FUNCTION: Displays low GTPase activity and exists predominantly in the
CC GTP-bound form. {ECO:0000269|PubMed:12194967}.
CC -!- INTERACTION:
CC O95057; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-11993172, EBI-1105153;
CC O95057; P52306-5: RAP1GDS1; NbExp=5; IntAct=EBI-11993172, EBI-12832744;
CC O95057; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-11993172, EBI-11952721;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and brain.
CC {ECO:0000269|PubMed:12107278, ECO:0000269|PubMed:12194967}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Di-Ras family.
CC {ECO:0000305}.
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DR EMBL; AB076888; BAC01115.1; -; mRNA.
DR EMBL; AY056037; AAL23715.1; -; mRNA.
DR EMBL; AY059641; AAL17968.1; -; mRNA.
DR EMBL; AY180973; AAO22153.1; -; mRNA.
DR EMBL; AC006538; AAD13119.1; -; Genomic_DNA.
DR EMBL; BC030660; AAH30660.1; -; mRNA.
DR CCDS; CCDS12092.1; -.
DR RefSeq; NP_660156.1; NM_145173.3.
DR PDB; 2GF0; X-ray; 1.90 A; A/B/C/D=1-198.
DR PDBsum; 2GF0; -.
DR AlphaFoldDB; O95057; -.
DR SMR; O95057; -.
DR BioGRID; 127135; 31.
DR IntAct; O95057; 8.
DR STRING; 9606.ENSP00000325836; -.
DR iPTMnet; O95057; -.
DR PhosphoSitePlus; O95057; -.
DR BioMuta; DIRAS1; -.
DR EPD; O95057; -.
DR jPOST; O95057; -.
DR MassIVE; O95057; -.
DR MaxQB; O95057; -.
DR PaxDb; O95057; -.
DR PeptideAtlas; O95057; -.
DR PRIDE; O95057; -.
DR ProteomicsDB; 50634; -.
DR Antibodypedia; 23037; 243 antibodies from 27 providers.
DR DNASU; 148252; -.
DR Ensembl; ENST00000323469.5; ENSP00000325836.3; ENSG00000176490.5.
DR Ensembl; ENST00000585334.1; ENSP00000468417.1; ENSG00000176490.5.
DR GeneID; 148252; -.
DR KEGG; hsa:148252; -.
DR MANE-Select; ENST00000323469.5; ENSP00000325836.3; NM_145173.4; NP_660156.1.
DR UCSC; uc002lwf.4; human.
DR CTD; 148252; -.
DR DisGeNET; 148252; -.
DR GeneCards; DIRAS1; -.
DR HGNC; HGNC:19127; DIRAS1.
DR HPA; ENSG00000176490; Tissue enhanced (brain, heart muscle, tongue).
DR MIM; 607862; gene.
DR neXtProt; NX_O95057; -.
DR OpenTargets; ENSG00000176490; -.
DR PharmGKB; PA134951835; -.
DR VEuPathDB; HostDB:ENSG00000176490; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000159915; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; O95057; -.
DR OMA; MMKEVKG; -.
DR OrthoDB; 1218505at2759; -.
DR PhylomeDB; O95057; -.
DR TreeFam; TF313014; -.
DR PathwayCommons; O95057; -.
DR SignaLink; O95057; -.
DR BioGRID-ORCS; 148252; 7 hits in 1070 CRISPR screens.
DR EvolutionaryTrace; O95057; -.
DR GenomeRNAi; 148252; -.
DR Pharos; O95057; Tbio.
DR PRO; PR:O95057; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95057; protein.
DR Bgee; ENSG00000176490; Expressed in left ventricle myocardium and 139 other tissues.
DR ExpressionAtlas; O95057; baseline and differential.
DR Genevisible; O95057; HS.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
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 3D-structure; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..195
FT /note="GTP-binding protein Di-Ras1"
FT /id="PRO_0000191648"
FT PROPEP 196..198
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370775"
FT REGION 178..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000305|Ref.7, ECO:0007744|PDB:2GF0"
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:0000305|Ref.7, ECO:0007744|PDB:2GF0"
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:0000305|Ref.7, ECO:0007744|PDB:2GF0"
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"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:2GF0"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:2GF0"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:2GF0"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:2GF0"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2GF0"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:2GF0"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:2GF0"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:2GF0"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2GF0"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2GF0"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2GF0"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:2GF0"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:2GF0"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:2GF0"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:2GF0"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2GF0"
SQ SEQUENCE 198 AA; 22329 MW; 32E979AF80BB9A7F CRC64;
MPEQSNDYRV VVFGAGGVGK SSLVLRFVKG TFRDTYIPTI EDTYRQVISC DKSVCTLQIT
DTTGSHQFPA MQRLSISKGH AFILVFSVTS KQSLEELGPI YKLIVQIKGS VEDIPVMLVG
NKCDETQREV DTREAQAVAQ EWKCAFMETS AKMNYNVKEL FQELLTLETR RNMSLNIDGK
RSGKQKRTDR VKGKCTLM
