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RAP1B_RAT
ID   RAP1B_RAT               Reviewed;         184 AA.
AC   Q62636; Q6J167;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Ras-related protein Rap-1b;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P61224};
DE   AltName: Full=GTP-binding protein smg p21B;
DE   Flags: Precursor;
GN   Name=Rap1b;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Rishi A.K., Gulamhussein A.I., Steele M.P.;
RT   "Cloning and sequencing of rat Ras like Rap1B cDNA.";
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Thyroid;
RA   Tsygankova O.M., Meinkoth J.L.;
RT   "Sequence of Rap1b from Wistar rat thyroid cells.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; U07795; AAA92787.1; -; mRNA.
DR   EMBL; AY607847; AAT37620.1; -; mRNA.
DR   EMBL; BC081731; AAH81731.1; -; mRNA.
DR   RefSeq; NP_599173.2; NM_134346.3.
DR   RefSeq; XP_008763599.1; XM_008765377.2.
DR   PDB; 3X1W; X-ray; 1.20 A; A=1-167.
DR   PDB; 3X1X; X-ray; 1.00 A; A=1-167.
DR   PDB; 3X1Y; X-ray; 1.17 A; A=1-167.
DR   PDB; 3X1Z; X-ray; 1.25 A; A/B=1-167.
DR   PDBsum; 3X1W; -.
DR   PDBsum; 3X1X; -.
DR   PDBsum; 3X1Y; -.
DR   PDBsum; 3X1Z; -.
DR   AlphaFoldDB; Q62636; -.
DR   SMR; Q62636; -.
DR   BioGRID; 251189; 1.
DR   IntAct; Q62636; 1.
DR   STRING; 10116.ENSRNOP00000009511; -.
DR   iPTMnet; Q62636; -.
DR   PhosphoSitePlus; Q62636; -.
DR   jPOST; Q62636; -.
DR   PaxDb; Q62636; -.
DR   PRIDE; Q62636; -.
DR   Ensembl; ENSRNOT00000113270; ENSRNOP00000078778; ENSRNOG00000007048.
DR   GeneID; 171337; -.
DR   KEGG; rno:171337; -.
DR   UCSC; RGD:620577; rat.
DR   CTD; 5908; -.
DR   RGD; 620577; Rap1b.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000154429; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; Q62636; -.
DR   OMA; CYRKQWV; -.
DR   OrthoDB; 1353024at2759; -.
DR   PhylomeDB; Q62636; -.
DR   TreeFam; TF313014; -.
DR   Reactome; R-RNO-354192; Integrin signaling.
DR   Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR   Reactome; R-RNO-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-RNO-392517; Rap1 signalling.
DR   Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-8875555; MET activates RAP1 and RAC1.
DR   PRO; PR:Q62636; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000007048; Expressed in spleen and 19 other tissues.
DR   Genevisible; Q62636; RN.
DR   GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005811; C:lipid droplet; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR   GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR   GO; GO:0097211; P:cellular response to gonadotropin-releasing hormone; IEP:RGD.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:RGD.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:RGD.
DR   GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
DR   GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; ISO:RGD.
DR   GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; ISO:RGD.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR   GO; GO:0033625; P:positive regulation of integrin activation; ISO:RGD.
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   GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD.
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   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Cell junction; Cell membrane; Cytoplasm;
KW   GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome.
FT   CHAIN           1..181
FT                   /note="Ras-related protein Rap-1b"
FT                   /id="PRO_0000030213"
FT   PROPEP          182..184
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000030214"
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"
FT   CONFLICT        58
FT                   /note="T -> A (in Ref. 1; AAA92787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75
FT                   /note="G -> E (in Ref. 1; AAA92787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86..90
FT                   /note="AQSTF -> TQIDC (in Ref. 1; AAA92787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="D -> G (in Ref. 1; AAA92787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="G -> P (in Ref. 1; AAA92787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174..175
FT                   /note="KA -> NR (in Ref. 1; AAA92787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="S -> P (in Ref. 1; AAA92787)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   HELIX           16..25
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   STRAND          39..46
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   STRAND          49..57
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   HELIX           68..74
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   STRAND          76..83
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   HELIX           87..104
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   STRAND          111..116
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   HELIX           128..137
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   TURN            148..151
FT                   /evidence="ECO:0007829|PDB:3X1X"
FT   HELIX           154..165
FT                   /evidence="ECO:0007829|PDB:3X1X"
SQ   SEQUENCE   184 AA;  20798 MW;  37A76895E58DD80C CRC64;
     MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDAQQ CMLEILDTAG
     TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MILVGNKCDL
     EDERVVGKEQ GQNLARQWSN CAFLESSAKS KINVNEIFYD LVRQINRKTP VPGKARKKSS
     CQLL
 
 
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