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
