ID   RASD1_RAT               Reviewed;         280 AA.
AC   Q9JKF8; Q4KLL2;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Dexamethasone-induced Ras-related protein 1;
DE   Flags: Precursor;
GN   Name=Rasd1; Synonyms=Dexras1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CAPON AND NOS1, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11086993; DOI=10.1016/s0896-6273(00)00095-7;
RA   Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.;
RT   "Dexras1: a G protein specifically coupled to neuronal nitric oxide
RT   synthase via CAPON.";
RL   Neuron 28:183-193(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH APBB1 AND APP,
RP   INTERACTION WITH APBB1, AND MUTAGENESIS OF ALA-178.
RX   PubMed=18922798; DOI=10.1074/jbc.m801874200;
RA   Lau K.-F., Chan W.-M., Perkinton M.S., Tudor E.L., Chang R.C.C.,
RA   Chan H.-Y., McLoughlin D.M., Miller C.C.J.;
RT   "Dexras1 interacts with FE65 to regulate FE65-amyloid precursor protein-
RT   dependent transcription.";
RL   J. Biol. Chem. 283:34728-34737(2008).
CC   -!- FUNCTION: Small GTPase. Negatively regulates the transcription
CC       regulation activity of the APBB1/FE65-APP complex via its interaction
CC       with APBB1/FE65.
CC   -!- SUBUNIT: Forms a ternary complex with CAPON and NOS1. Component of a
CC       complex, at least composed of APBB1, RASD1/DEXRAS1 and APP. Interacts
CC       with APBB1/FE65. Forms. {ECO:0000269|PubMed:11086993,
CC       ECO:0000269|PubMed:18922798}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear
CC       region {ECO:0000269|PubMed:18922798}. Nucleus
CC       {ECO:0000269|PubMed:18922798}.
CC   -!- TISSUE SPECIFICITY: Prominently found in brain at both mRNA and protein
CC       levels. Moderate expression in testis and lung. Slightly expressed in
CC       heart, spleen, skeletal muscle, liver and kidney.
CC       {ECO:0000269|PubMed:11086993}.
CC   -!- PTM: S-nitrosylation stimulates guanine-nucleotide exchange activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. RasD family.
CC       {ECO:0000305}.
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DR   EMBL; AF239157; AAF43090.1; -; mRNA.
DR   EMBL; BC099136; AAH99136.1; -; mRNA.
DR   RefSeq; NP_001257883.1; NM_001270954.1.
DR   RefSeq; XP_008766093.1; XM_008767871.2.
DR   RefSeq; XP_008766094.1; XM_008767872.2.
DR   RefSeq; XP_017453012.1; XM_017597523.1.
DR   AlphaFoldDB; Q9JKF8; -.
DR   SMR; Q9JKF8; -.
DR   CORUM; Q9JKF8; -.
DR   STRING; 10116.ENSRNOP00000004475; -.
DR   PaxDb; Q9JKF8; -.
DR   Ensembl; ENSRNOT00000004475; ENSRNOP00000004475; ENSRNOG00000003348.
DR   GeneID; 64455; -.
DR   KEGG; rno:64455; -.
DR   UCSC; RGD:619727; rat.
DR   CTD; 51655; -.
DR   RGD; 619727; Rasd1.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000161274; -.
DR   HOGENOM; CLU_041217_9_3_1; -.
DR   InParanoid; Q9JKF8; -.
DR   OMA; MRTKTCA; -.
DR   OrthoDB; 1398885at2759; -.
DR   PhylomeDB; Q9JKF8; -.
DR   TreeFam; TF316238; -.
DR   PRO; PR:Q9JKF8; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000003348; Expressed in ovary and 20 other tissues.
DR   Genevisible; Q9JKF8; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0007263; P:nitric oxide mediated signal transduction; IDA:RGD.
DR   GO; GO:0007165; P: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   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; Cytoplasm; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Nucleus; Prenylation; Reference proteome;
KW   S-nitrosylation.
FT   CHAIN           1..277
FT                   /note="Dexamethasone-induced Ras-related protein 1"
FT                   /id="PRO_0000082719"
FT   PROPEP          278..280
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281374"
FT   MOTIF           53..61
FT                   /note="Effector region"
FT   BINDING         31..38
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         78..82
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         145..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y272"
FT   MOD_RES         277
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           277
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         178
FT                   /note="A->V: Constitively active mutant. Does not affect
FT                   interaction with APBB1/FE65."
FT                   /evidence="ECO:0000269|PubMed:18922798"
SQ   SEQUENCE   280 AA;  31714 MW;  E551203186B8F9D5 CRC64;
     MKLAAMIKKM CPSDSELSIP AKNCYRMVIL GSSKVGKTAI VSRFLTGRFE DAYTPTIEDF
     HRKFYSIRGE VYQLDILDTS GNHPFPAMRR LSILTGDVFI LVFSLDNRDS FEEVQRLKQQ
     ILDTKSCLKN KTKENVDVPL VICGNKGDRD FYREVEQREI EQLVGDDPQR CAYFEISAKK
     NSSLDQMFRA LFAMAKLPSE MSPDLHRKVS VQYCDVLHKK ALRNKKLLRA GSGGGGDHGD
     AFGILAPFAR RPSVHSDLMY IREKTSVSSQ AKDKERCVIS