RAP1A_BOVIN
ID RAP1A_BOVIN Reviewed; 184 AA.
AC P62833; A4IFG1; P10113;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ras-related protein Rap-1A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61224};
DE AltName: Full=GTP-binding protein smg p21A;
DE Flags: Precursor;
GN Name=RAP1A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=3143720; DOI=10.1016/s0021-9258(18)37376-9;
RA Kawata M., Matsui Y., Kondo J., Hishida T., Teranishi Y., Takai Y.;
RT "A novel small molecular weight GTP-binding protein with the same putative
RT effector domain as the ras proteins in bovine brain membranes.
RT Purification, determination of primary structure, and characterization.";
RL J. Biol. Chem. 263:18965-18971(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 130-145 AND 169-173.
RX PubMed=1646988;
RA Kawata M., Kawahara Y., Sunako M., Araki S., Koide M., Tsuda T.,
RA Fukuzaki H., Takai Y.;
RT "The molecular heterogeneity of the smg-21/Krev-1/rap1 proteins, a GTP-
RT binding protein having the same effector domain as ras p21s, in bovine
RT aortic smooth muscle membranes.";
RL Oncogene 6:841-848(1991).
CC -!- FUNCTION: Induces morphological reversion of a cell line transformed by
CC a Ras oncogene. Counteracts the mitogenic function of Ras, at least
CC partly because it can interact with Ras GAPs and RAF in a competitive
CC manner. Together with ITGB1BP1, regulates KRIT1 localization to
CC microtubules and membranes. Plays a role in nerve growth factor (NGF)-
CC induced neurite outgrowth. Plays a role in the regulation of embryonic
CC blood vessel formation. Involved in the establishment of basal
CC endothelial barrier function. May be involved in the regulation of the
CC vascular endothelial growth factor receptor KDR expression at
CC endothelial cell-cell junctions (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 -!- ACTIVITY REGULATION: Activated by guanine nucleotide-exchange factors
CC (GEF) EPAC and EPAC2 in a cAMP-dependent manner, and GFR.
CC {ECO:0000250}.
CC -!- SUBUNIT: Found in a complex, at least composed of ITGB1BP1, KRIT1 and
CC RAP1A. Interacts (active GTP-bound form preferentially) with KRIT1 (via
CC C-terminus FERM domain); the interaction does not induce the opening
CC conformation of KRIT1. In its GTP-bound form interacts with PLCE1 and
CC RADIL. Interacts with SGSM1, SGSM2 and SGSM3. Interacts (via GTP-bound
CC active form) with RAPGEF2 (via Ras-associating domain) (By similarity).
CC Interacts with TBC1D21 (By similarity). Interacts with RAP1GDS1 (By
CC similarity). {ECO:0000250|UniProtKB:P62834,
CC ECO:0000250|UniProtKB:P62835}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cytoplasm.
CC Cytoplasm, perinuclear region {ECO:0000250}. Cell junction
CC {ECO:0000250}. Early endosome {ECO:0000250}. Note=Recruited from early
CC endosome to late endosome compartment after nerve growth factor (NGF)
CC stimulation. Localized with RAPGEF2 at cell-cell junctions. Colocalized
CC with RAPGEF2 in the perinuclear region (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; J04196; AAA30415.1; -; mRNA.
DR EMBL; BC134566; AAI34567.1; -; mRNA.
DR PIR; A31961; A31961.
DR RefSeq; NP_776873.1; NM_174448.4.
DR RefSeq; XP_010801456.1; XM_010803154.1.
DR AlphaFoldDB; P62833; -.
DR SMR; P62833; -.
DR STRING; 9913.ENSBTAP00000019575; -.
DR PaxDb; P62833; -.
DR PeptideAtlas; P62833; -.
DR PRIDE; P62833; -.
DR Ensembl; ENSBTAT00000068678; ENSBTAP00000062154; ENSBTAG00000050904.
DR GeneID; 282031; -.
DR KEGG; bta:282031; -.
DR CTD; 5906; -.
DR VEuPathDB; HostDB:ENSBTAG00000050904; -.
DR VGNC; VGNC:33715; RAP1A.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000160251; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P62833; -.
DR OMA; NVPMVIV; -.
DR OrthoDB; 1353024at2759; -.
DR TreeFam; TF313014; -.
DR Reactome; R-BTA-170968; Frs2-mediated activation.
DR Reactome; R-BTA-170984; ARMS-mediated activation.
DR Reactome; R-BTA-354192; Integrin signaling.
DR Reactome; R-BTA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-BTA-392517; Rap1 signalling.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000050904; Expressed in trachea and 103 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
DR GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
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:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:Ensembl.
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 Cell junction; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Neurogenesis; Nucleotide-binding; Prenylation; Reference proteome;
KW Tumor suppressor.
FT CHAIN 1..181
FT /note="Ras-related protein Rap-1A"
FT /id="PRO_0000030197"
FT PROPEP 182..184
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030198"
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:P62834"
FT BINDING 29..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62834"
FT BINDING 60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62834"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62834"
FT MOD_RES 181
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62834"
FT LIPID 181
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62834"
SQ SEQUENCE 184 AA; 20987 MW; 42C39290C98E0A92 CRC64;
MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDCQQ CMLEILDTAG
TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTEDVP MILVGNKCDL
EDERVVGKEQ GQNLARQWCN CAFLESSAKS KINVNEIFYD LVRQINRKTP VEKKKPKKKS
CLLL
