RASD1_MOUSE
ID RASD1_MOUSE Reviewed; 280 AA.
AC O35626;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Dexamethasone-induced Ras-related protein 1;
DE Flags: Precursor;
GN Name=Rasd1; Synonyms=Dexras1;
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], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9452419; DOI=10.1074/jbc.273.6.3129;
RA Kemppainen R.J., Behrend E.N.;
RT "Dexamethasone rapidly induces a novel ras superfamily member-related gene
RT in AtT-20 cells.";
RL J. Biol. Chem. 273:3129-3131(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [4]
RP INTERACTION WITH CAPON AND NOS1, AND S-NITROSYLATION.
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).
CC -!- FUNCTION: Small GTPase. Negatively regulates the transcription
CC regulation activity of the APBB1/FE65-APP complex via its interaction
CC with APBB1/FE65 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex, at least composed of APBB1,
CC RASD1/DEXRAS1 and APP. Interacts with APBB1/FE65 (By similarity). Forms
CC a ternary complex with CAPON and NOS1. {ECO:0000250,
CC ECO:0000269|PubMed:11086993}.
CC -!- INTERACTION:
CC O35626; P43136: Nr2f6; NbExp=5; IntAct=EBI-4319979, EBI-4319956;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney and liver.
CC {ECO:0000269|PubMed:9452419}.
CC -!- INDUCTION: By dexamethasone. {ECO:0000269|PubMed:9452419}.
CC -!- PTM: S-nitrosylation stimulates guanine-nucleotide exchange activity.
CC {ECO:0000269|PubMed:11086993}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. RasD family.
CC {ECO:0000305}.
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DR EMBL; AF009246; AAC53538.1; -; mRNA.
DR EMBL; AK038932; BAC30173.1; -; mRNA.
DR EMBL; BC034166; AAH34166.1; -; mRNA.
DR CCDS; CCDS24781.1; -.
DR RefSeq; NP_033052.1; NM_009026.5.
DR AlphaFoldDB; O35626; -.
DR SMR; O35626; -.
DR BioGRID; 202599; 8.
DR CORUM; O35626; -.
DR IntAct; O35626; 8.
DR STRING; 10090.ENSMUSP00000051959; -.
DR iPTMnet; O35626; -.
DR PhosphoSitePlus; O35626; -.
DR PaxDb; O35626; -.
DR PRIDE; O35626; -.
DR ProteomicsDB; 300235; -.
DR Antibodypedia; 25457; 81 antibodies from 21 providers.
DR DNASU; 19416; -.
DR Ensembl; ENSMUST00000062405; ENSMUSP00000051959; ENSMUSG00000049892.
DR GeneID; 19416; -.
DR KEGG; mmu:19416; -.
DR UCSC; uc007jfh.2; mouse.
DR CTD; 51655; -.
DR MGI; MGI:1270848; Rasd1.
DR VEuPathDB; HostDB:ENSMUSG00000049892; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000161274; -.
DR HOGENOM; CLU_041217_9_3_1; -.
DR InParanoid; O35626; -.
DR OMA; FYREVEP; -.
DR OrthoDB; 1398885at2759; -.
DR PhylomeDB; O35626; -.
DR TreeFam; TF316238; -.
DR BioGRID-ORCS; 19416; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Rasd1; mouse.
DR PRO; PR:O35626; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O35626; protein.
DR Bgee; ENSMUSG00000049892; Expressed in gonadal fat pad and 119 other tissues.
DR ExpressionAtlas; O35626; baseline and differential.
DR Genevisible; O35626; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
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; ISO:MGI.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; ISO:MGI.
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_0000082718"
FT PROPEP 278..280
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281373"
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"
SQ SEQUENCE 280 AA; 31684 MW; E551203197FCF9D5 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 IREKTSVGSQ AKDKERCVIS
