ID   RSU1_MOUSE              Reviewed;         277 AA.
AC   Q01730;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Ras suppressor protein 1;
DE            Short=RSP-1;
DE            Short=Rsu-1;
GN   Name=Rsu1; Synonyms=Rsp1;
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=NIH Swiss; TISSUE=Fibroblast;
RX   PubMed=1508180; DOI=10.1128/mcb.12.9.3750-3756.1992;
RA   Cutler M.L., Bassin R.H., Zanoni L., Talbot N.;
RT   "Isolation of rsp-1, a novel cDNA capable of suppressing v-Ras
RT   transformation.";
RL   Mol. Cell. Biol. 12:3750-3756(1992).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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: Potentially plays a role in the Ras signal transduction
CC       pathway. Capable of suppressing v-Ras transformation in vitro.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X63039; CAA44765.1; -; mRNA.
DR   CCDS; CCDS15693.1; -.
DR   PIR; S25770; S25770.
DR   AlphaFoldDB; Q01730; -.
DR   SMR; Q01730; -.
DR   IntAct; Q01730; 2.
DR   MINT; Q01730; -.
DR   STRING; 10090.ENSMUSP00000028059; -.
DR   iPTMnet; Q01730; -.
DR   PhosphoSitePlus; Q01730; -.
DR   EPD; Q01730; -.
DR   jPOST; Q01730; -.
DR   MaxQB; Q01730; -.
DR   PaxDb; Q01730; -.
DR   PeptideAtlas; Q01730; -.
DR   PRIDE; Q01730; -.
DR   ProteomicsDB; 262716; -.
DR   TopDownProteomics; Q01730; -.
DR   MGI; MGI:103040; Rsu1.
DR   eggNOG; KOG0617; Eukaryota.
DR   InParanoid; Q01730; -.
DR   PhylomeDB; Q01730; -.
DR   Reactome; R-MMU-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR   ChiTaRS; Rsu1; mouse.
DR   PRO; PR:Q01730; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q01730; protein.
DR   GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IGI:MGI.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IGI:MGI.
DR   GO; GO:0007265; P:Ras protein signal transduction; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00369; LRR_TYP; 6.
DR   PROSITE; PS51450; LRR; 7.
PE   1: Evidence at protein level;
KW   Acetylation; Leucine-rich repeat; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q15404"
FT   CHAIN           2..277
FT                   /note="Ras suppressor protein 1"
FT                   /id="PRO_0000097500"
FT   REPEAT          41..63
FT                   /note="LRR 1"
FT   REPEAT          64..85
FT                   /note="LRR 2"
FT   REPEAT          87..108
FT                   /note="LRR 3"
FT   REPEAT          110..133
FT                   /note="LRR 4"
FT   REPEAT          135..156
FT                   /note="LRR 5"
FT   REPEAT          158..179
FT                   /note="LRR 6"
FT   REPEAT          181..202
FT                   /note="LRR 7"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15404"
SQ   SEQUENCE   277 AA;  31550 MW;  0D12705A39872F2E CRC64;
     MSKSLKKLVE ESREKNQPEV DMSDRGISSM LDVNGLFSLA HITQLVLSHN KLTTVPPNVA
     ELKNLEVLNF FNNQIEELPT QISSLQKLKH LNLGMNRLNT LPRGFGSSRL LEVLELTYNN
     LNEHSLPGNF FYLTTLRALY LSDNDFEILP PDIGKLTKLQ ILSLRDNDLI SLPKEIGELT
     QLKELHIQGN RLTVLPPELG NLDLTGQKQV FKAENNPWVT PIADQFQLGV SHVFEYIRSE
     TYKYLYGRHM QANPEPPKKN NDKSKKISRK PLAAKNK