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RAP1B_PANTR
ID   RAP1B_PANTR             Reviewed;         184 AA.
AC   A5A6J7;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 111.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA   Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA   Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT   "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT   large potential divergence of the transcriptome.";
RL   Gene 399:1-10(2007).
CC   -!- FUNCTION: GTP-binding protein that possesses intrinsic GTPase activity.
CC       Contributes to the polarizing activity of KRIT1 and CDH5 in the
CC       establishment and maintenance of correct endothelial cell polarity and
CC       vascular lumen. Required for the localization of phosphorylated PRKCZ,
CC       PARD3 and TIAM1 to the cell junction. Plays a role in the establishment
CC       of basal endothelial barrier function (By similarity).
CC       {ECO:0000250|UniProtKB:P61224}.
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   -!- ACTIVITY REGULATION: Activated by guanine nucleotide-exchange factor
CC       (GEF) EPAC2 in a cAMP-dependent manner. {ECO:0000250|UniProtKB:P61224}.
CC   -!- SUBUNIT: Heterodimer with RAP1GAP (By similarity). Interacts with EPAC2
CC       (By similarity). Interacts with SGSM1 (By similarity). Interacts with
CC       SGSM2 (By similarity). Interacts with SGSM3 (By similarity). Interacts
CC       with KRIT1 (By similarity). Interacts with RAP1GDS1 (By similarity).
CC       {ECO:0000250|UniProtKB:P61224}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61224}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61224}. Cell junction
CC       {ECO:0000250|UniProtKB:P61224}. Note=May shuttle between plasma
CC       membrane and cytosol (By similarity). Presence of KRIT1 and CDH5 is
CC       required for its localization to the cell junction (By similarity).
CC       {ECO:0000250|UniProtKB:P61224}.
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DR   EMBL; AB222125; BAF62370.1; -; mRNA.
DR   RefSeq; NP_001092015.1; NM_001098545.1.
DR   RefSeq; XP_009424050.1; XM_009425775.2.
DR   RefSeq; XP_016778071.1; XM_016922582.1.
DR   AlphaFoldDB; A5A6J7; -.
DR   SMR; A5A6J7; -.
DR   STRING; 9598.ENSPTRP00000008828; -.
DR   PaxDb; A5A6J7; -.
DR   Ensembl; ENSPTRT00000110714; ENSPTRP00000070769; ENSPTRG00000005197.
DR   GeneID; 452065; -.
DR   KEGG; ptr:452065; -.
DR   CTD; 5908; -.
DR   VGNC; VGNC:10515; RAP1B.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000154429; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; A5A6J7; -.
DR   OMA; CYRKQWV; -.
DR   OrthoDB; 1353024at2759; -.
DR   TreeFam; TF313014; -.
DR   Proteomes; UP000002277; Chromosome 12.
DR   Bgee; ENSPTRG00000005197; Expressed in fibroblast and 21 other tissues.
DR   GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR   GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
DR   GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IBA:GO_Central.
DR   GO; GO:0033625; P:positive regulation of integrin activation; IEA:Ensembl.
DR   GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR   GO; GO:1901888; P:regulation of cell junction assembly; ISS:UniProtKB.
DR   GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
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   ADP-ribosylation; Cell junction; Cell membrane; Cytoplasm; GTP-binding;
KW   Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Prenylation; Reference proteome.
FT   CHAIN           1..181
FT                   /note="Ras-related protein Rap-1b"
FT                   /id="PRO_0000295277"
FT   PROPEP          182..184
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000295278"
FT   REGION          25..67
FT                   /note="Interaction with KRIT1"
FT                   /evidence="ECO:0000250|UniProtKB:P61224"
FT   MOTIF           32..40
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   BINDING         10..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61224"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61224"
FT   BINDING         116..119
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61224"
FT   BINDING         147..149
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61224"
FT   MOD_RES         39
FT                   /note="ADP-ribosylserine; by botulinum toxin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         179
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P61224"
FT   MOD_RES         181
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P61224"
FT   LIPID           181
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P61224"
SQ   SEQUENCE   184 AA;  20825 MW;  CE976895E5965224 CRC64;
     MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDAQQ CMLEILDTAG
     TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MILVGNKCDL
     EDERVVGKEQ GQNLARQWNN CAFLESSAKS KINVNEIFYD LVRQINRKTP VPGKARKKSS
     CQLL
 
 
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