ID   RAP1B_CYPCA             Reviewed;         184 AA.
AC   Q9YH37;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Ras-related protein Rap-1b;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P61224};
DE   Flags: Precursor;
GN   Name=rap1b;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chang M.S., Chang Y., Chang G.D., Huang F.L., Huang C.-J.;
RT   "Molecular cloning and sequencing of two carp cDNAs encoding ras-related
RT   proteins.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable GTP-binding protein that possesses GTPase activity.
CC       May play a role in endothelial cell polarity and endothelial barrier
CC       function (By similarity). {ECO:0000250}.
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:0000250}. Cytoplasm, cytosol
CC       {ECO:0000250}. Cell junction {ECO:0000250}. Note=May shuttle between
CC       plasma membrane and cytosol. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; U53783; AAD10840.1; -; mRNA.
DR   AlphaFoldDB; Q9YH37; -.
DR   SMR; Q9YH37; -.
DR   Proteomes; UP000694384; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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 junction; Cell membrane; Cytoplasm; GTP-binding; Hydrolase;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW   Reference proteome.
FT   CHAIN           1..181
FT                   /note="Ras-related protein Rap-1b"
FT                   /id="PRO_0000366911"
FT   PROPEP          182..184
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000366912"
FT   MOTIF           32..40
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..119
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         181
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           181
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   184 AA;  20780 MW;  CDD75E1FFF1D6903 CRC64;
     MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDGQQ CMLEILDTAG
     TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTDDVP IILVGNKCDL
     EDERVVGKEQ GQNLARQWNS CAFLESSAKS KINVNEIFYD LVRQINRKTP VPGKARKKST
     CQLL