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
