RAP1_PHYPO
ID RAP1_PHYPO Reviewed; 188 AA.
AC Q94694;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ras-related protein Rap-1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61224};
DE AltName: Full=Pprap1;
DE Flags: Precursor;
GN Name=RAP1;
OS Physarum polycephalum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX NCBI_TaxID=5791;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=LU352;
RX PubMed=8605245; DOI=10.1016/0167-4781(95)00207-3;
RA Kozlowski P., Trzcinska-Danielewicz J., Toczko K.;
RT "Identification and sequence analysis of a rap gene from the true slime
RT mold Physarum polycephalum.";
RL Biochim. Biophys. Acta 1305:29-33(1996).
RN [2]
RP DEVELOPMENTAL STAGE.
RC STRAIN=CL, LU352, and MCC;
RX PubMed=9344483; DOI=10.1006/cbir.1997.0168;
RA Kozlowski P., Trzcinska-Danielewicz J., Urbanczyk A., Toczko K.;
RT "Ppras1, ppras2 and pprap1 genes, members of a ras gene family from the
RT true slime mold Physarum polycephalum are developmentally regulated.";
RL Cell Biol. Int. 21:441-445(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P61224};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highest levels in fruiting bodies, abundant in
CC amoebae, moderately abundant in CL spherules but barely present in
CC plasmodia and MCC spherules. {ECO:0000269|PubMed:9344483}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; U15594; AAC47511.1; -; mRNA.
DR EMBL; AF000653; AAB58345.1; -; Genomic_DNA.
DR PIR; S65761; S65761.
DR AlphaFoldDB; Q94694; -.
DR SMR; Q94694; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0032486; P:Rap protein signal transduction; IEA:InterPro.
DR CDD; cd04175; Rap1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038851; Rap1.
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 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation.
FT CHAIN 1..185
FT /note="Ras-related protein Rap-1"
FT /id="PRO_0000082685"
FT PROPEP 186..188
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281334"
FT MOTIF 34..42
FT /note="Effector region"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 185
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 185
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 188 AA; 21036 MW; 72B3FC927EB648AE CRC64;
MPLREFKIVV LGSGGVGKSA LTVQFVQGIF VEKYDPTIED SYRKQVEVDG QQCMLEILDT
AGTEQFTAMR DLYMKNGQGF VLVYSIIAMS TFNDLPDLRE QILRVKDCDD VPMVLVGNKC
DLAEQRVIST EQGDELARKF GGCAFLEASA KNKINVEQIF YDLIRQINRK NPGPTNKKEK
KSGGCILL
