RSU1_BOVIN
ID RSU1_BOVIN Reviewed; 277 AA.
AC Q5E9C0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ras suppressor protein 1;
DE Short=Rsu-1;
GN Name=RSU1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Potentially plays a role in the Ras signal transduction
CC pathway. Capable of suppressing v-Ras transformation in vitro (By
CC similarity). {ECO:0000250}.
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DR EMBL; BT021000; AAX09017.1; -; mRNA.
DR EMBL; BC102118; AAI02119.1; -; mRNA.
DR RefSeq; NP_001035691.1; NM_001040601.2.
DR AlphaFoldDB; Q5E9C0; -.
DR SMR; Q5E9C0; -.
DR STRING; 9913.ENSBTAP00000039209; -.
DR PaxDb; Q5E9C0; -.
DR PRIDE; Q5E9C0; -.
DR Ensembl; ENSBTAT00000039415; ENSBTAP00000039209; ENSBTAG00000027446.
DR GeneID; 617534; -.
DR KEGG; bta:617534; -.
DR CTD; 6251; -.
DR VEuPathDB; HostDB:ENSBTAG00000027446; -.
DR VGNC; VGNC:57022; RSU1.
DR eggNOG; KOG0617; Eukaryota.
DR GeneTree; ENSGT00940000158676; -.
DR HOGENOM; CLU_000288_18_15_1; -.
DR InParanoid; Q5E9C0; -.
DR OMA; RHMQGGR; -.
DR OrthoDB; 1382533at2759; -.
DR TreeFam; TF314790; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000027446; Expressed in myometrium and 105 other tissues.
DR ExpressionAtlas; Q5E9C0; baseline and differential.
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; 7.
DR PROSITE; PS51450; LRR; 7.
PE 2: Evidence at transcript 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..276
FT /note="Ras suppressor protein 1"
FT /id="PRO_0000273968"
FT REPEAT 41..63
FT /note="LRR 1"
FT REPEAT 64..85
FT /note="LRR 2"
FT REPEAT 87..109
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; 31537 MW; 4094EABC0D75999C CRC64;
MSKSLKKLVE ESREKNQPEV DMSDRGISNM LDINGLFTLS HITQLVLSHN KLTTVPPNIA
ELKNLEVLNF FNNQIEELPT QISSLQKLKH LNLGMNRLNT LPRGFGSLPA LEVLDLTYNN
LNENSLPGNF FYLTTLRALY LSDNDFEILP PDIGKLTKLQ ILSLRDNDLI SLPKEIGELT
QLKELHIQGN RLTVLPPELG NLDLTGQKQI FKAENNPWVT PIADQFQLGV SHVFEYIRSE
TYKYLYGRHM QANPEPPKKN NDKSKKISRK PLAAKNK