RAP1A_HUMAN
ID RAP1A_HUMAN Reviewed; 184 AA.
AC P62834; P10113;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Ras-related protein Rap-1A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61224};
DE AltName: Full=C21KG;
DE AltName: Full=G-22K;
DE AltName: Full=GTP-binding protein smg p21A;
DE AltName: Full=Ras-related protein Krev-1;
DE Flags: Precursor;
GN Name=RAP1A; Synonyms=KREV1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3045729;
RA Pizon V., Chardin P., Lerosey I., Olofsson B., Tavitian A.;
RT "Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode
RT proteins closely related to ras in the 'effector' region.";
RL Oncogene 3:201-204(1988).
RN [2]
RP SEQUENCE REVISION TO 3.
RA Pizon V.;
RL Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Platelet;
RX PubMed=2507536; DOI=10.1016/s0021-9258(18)71450-6;
RA Nagata K., Itoh H., Katada T., Takenaka K., Ui M., Kaziro Y., Nozawa Y.;
RT "Purification, identification, and characterization of two GTP-binding
RT proteins with molecular weights of 25,000 and 21,000 in human platelet
RT cytosol. One is the rap1/smg21/Krev-1 protein and the other is a novel GTP-
RT binding protein.";
RL J. Biol. Chem. 264:17000-17005(1989).
RN [7]
RP PROTEIN SEQUENCE OF 1-35.
RX PubMed=3141412; DOI=10.1016/s0021-9258(18)37454-4;
RA Bokoch G.M., Parkos C.A., Mumby S.M.;
RT "Purification and characterization of the 22,000-dalton GTP-binding protein
RT substrate for ADP-ribosylation by botulinum toxin, G22K.";
RL J. Biol. Chem. 263:16744-16749(1988).
RN [8]
RP PROTEIN SEQUENCE OF 1-5; 17-24; 32-42 AND 152-168.
RX PubMed=3144274; DOI=10.1016/s0006-291x(88)80302-4;
RA Ohmori T., Kikuchi A., Yamamoto K., Kawata M., Kondo J., Takai Y.;
RT "Identification of a platelet Mr 22,000 GTP-binding protein as the novel
RT smg-21 gene product having the same putative effector domain as the ras
RT gene products.";
RL Biochem. Biophys. Res. Commun. 157:670-676(1988).
RN [9]
RP ISOPRENYLATION AT CYS-181, AND METHYLATION AT CYS-181.
RX PubMed=1899909; DOI=10.1128/mcb.11.3.1523-1530.1991;
RA Buss J.E., Quilliam L.A., Kato K., Casey P.J., Solski P.A., Wong G.,
RA Clark R., McCormick F., Bokoch G.M., Der C.J.;
RT "The COOH-terminal domain of the Rap1A (Krev-1) protein is isoprenylated
RT and supports transformation by an H-Ras:Rap1A chimeric protein.";
RL Mol. Cell. Biol. 11:1523-1530(1991).
RN [10]
RP INTERACTION WITH RAPGEF2.
RX PubMed=10608844; DOI=10.1074/jbc.274.53.37815;
RA Liao Y., Kariya K., Hu C.-D., Shibatohge M., Goshima M., Okada T.,
RA Watari Y., Gao X., Jin T.-G., Yamawaki-Kataoka Y., Kataoka T.;
RT "RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a
RT Ras/Rap1A-associating domain, is conserved between nematode and humans.";
RL J. Biol. Chem. 274:37815-37820(1999).
RN [11]
RP INTERACTION WITH PLCE1.
RX PubMed=11022048; DOI=10.1074/jbc.m008324200;
RA Song C., Hu C.-D., Masago M., Kariya K., Yamawaki-Kataoka Y.,
RA Shibatohge M., Wu D., Satoh T., Kataoka T.;
RT "Regulation of a novel human phospholipase C, PLCepsilon, through membrane
RT targeting by Ras.";
RL J. Biol. Chem. 276:2752-2757(2001).
RN [12]
RP INTERACTION WITH RAPGEF2, AND SUBCELLULAR LOCATION.
RX PubMed=11359771; DOI=10.1074/jbc.m101737200;
RA Liao Y., Satoh T., Gao X., Jin T.G., Hu C.D., Kataoka T.;
RT "RA-GEF-1, a guanine nucleotide exchange factor for Rap1, is activated by
RT translocation induced by association with Rap1*GTP and enhances Rap1-
RT dependent B-Raf activation.";
RL J. Biol. Chem. 276:28478-28483(2001).
RN [13]
RP INTERACTION WITH PLCE1.
RX PubMed=12444546; DOI=10.1038/sj.onc.1206003;
RA Song C., Satoh T., Edamatsu H., Wu D., Tadano M., Gao X., Kataoka T.;
RT "Differential roles of Ras and Rap1 in growth factor-dependent activation
RT of phospholipase C epsilon.";
RL Oncogene 21:8105-8113(2002).
RN [14]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH ITGB1BP1 AND KRIT1, AND
RP INTERACTION WITH KRIT1.
RX PubMed=17916086; DOI=10.1111/j.1742-4658.2007.06068.x;
RA Beraud-Dufour S., Gautier R., Albiges-Rizo C., Chardin P., Faurobert E.;
RT "Krit 1 interactions with microtubules and membranes are regulated by Rap1
RT and integrin cytoplasmic domain associated protein-1.";
RL FEBS J. 274:5518-5532(2007).
RN [15]
RP INTERACTION WITH RADIL.
RX PubMed=17704304; DOI=10.1101/gad.1561507;
RA Smolen G.A., Schott B.J., Stewart R.A., Diederichs S., Muir B.,
RA Provencher H.L., Look A.T., Sgroi D.C., Peterson R.T., Haber D.A.;
RT "A Rap GTPase interactor, RADIL, mediates migration of neural crest
RT precursors.";
RL Genes Dev. 21:2131-2136(2007).
RN [16]
RP INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
RX PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT "Identification of three novel proteins (SGSM1, 2, 3) which modulate small
RT G protein (RAP and RAB)-mediated signaling pathway.";
RL Genomics 90:249-260(2007).
RN [17]
RP INTERACTION WITH RAP1GDS1.
RX PubMed=20709748; DOI=10.1074/jbc.m110.129916;
RA Berg T.J., Gastonguay A.J., Lorimer E.L., Kuhnmuench J.R., Li R.,
RA Fields A.P., Williams C.L.;
RT "Splice variants of SmgGDS control small GTPase prenylation and membrane
RT localization.";
RL J. Biol. Chem. 285:35255-35266(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP FUNCTION.
RX PubMed=21840392; DOI=10.1016/j.cellsig.2011.07.022;
RA Pannekoek W.J., van Dijk J.J., Chan O.Y., Huveneers S., Linnemann J.R.,
RA Spanjaard E., Brouwer P.M., van der Meer A.J., Zwartkruis F.J., Rehmann H.,
RA de Rooij J., Bos J.L.;
RT "Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction
RT control.";
RL Cell. Signal. 23:2056-2064(2011).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-167 IN COMPLEX WITH GTP.
RX PubMed=7791872; DOI=10.1038/375554a0;
RA Nassar N., Horn G., Herrmann C., Scherer A., McCormick F., Wittinghofer A.;
RT "The 2.2 A crystal structure of the Ras-binding domain of the
RT serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue.";
RL Nature 375:554-560(1995).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-167 IN COMPLEX WITH GTP ANALOG.
RX PubMed=8756332; DOI=10.1038/nsb0896-723;
RA Nassar N., Horn G., Herrmann C., Block C., Janknecht R., Wittinghofer A.;
RT "Ras/Rap effector specificity determined by charge reversal.";
RL Nat. Struct. Biol. 3:723-729(1996).
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. {ECO:0000269|PubMed:17916086,
CC ECO:0000269|PubMed:21840392}.
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 -!- SUBUNIT: Found in a complex, at least composed of ITGB1BP1, KRIT1 and
CC RAP1A (PubMed:17916086). Interacts (active GTP-bound form
CC preferentially) with KRIT1 (via C-terminus FERM domain); the
CC interaction does not induce the opening conformation of KRIT1
CC (PubMed:17916086). In its GTP-bound form interacts with PLCE1 and RADIL
CC (PubMed:11022048, PubMed:12444546, PubMed:17704304). Interacts with
CC SGSM1, SGSM2 and SGSM3 (PubMed:17509819). Interacts (via GTP-bound
CC active form) with RAPGEF2 (via Ras-associating domain)
CC (PubMed:11359771, PubMed:10608844). Interacts with TBC1D21 (By
CC similarity). Interacts with RAP1GDS1 (PubMed:20709748).
CC {ECO:0000250|UniProtKB:P62835, ECO:0000269|PubMed:10608844,
CC ECO:0000269|PubMed:11022048, ECO:0000269|PubMed:11359771,
CC ECO:0000269|PubMed:12444546, ECO:0000269|PubMed:17509819,
CC ECO:0000269|PubMed:17704304, ECO:0000269|PubMed:17916086,
CC ECO:0000269|PubMed:20709748}.
CC -!- INTERACTION:
CC P62834; P04049: RAF1; NbExp=2; IntAct=EBI-491414, EBI-365996;
CC P62834; Q8WWW0-2: RASSF5; NbExp=3; IntAct=EBI-491414, EBI-960502;
CC P62834; Q5EBH1: Rassf5; Xeno; NbExp=3; IntAct=EBI-491414, EBI-960530;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11359771};
CC Lipid-anchor {ECO:0000269|PubMed:11359771}. Cytoplasm
CC {ECO:0000269|PubMed:11359771}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11359771}. Cell junction {ECO:0000250}. Early
CC endosome {ECO:0000250}. Note=Recruited from early endosome to late
CC endosome compartment after nerve growth factor (NGF) stimulation.
CC Localized with RAPGEF2 at cell-cell junctions (By similarity).
CC Colocalized with RAPGEF2 in the perinuclear region. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RAP1AID272.html";
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DR EMBL; X12533; CAA31051.1; -; mRNA.
DR EMBL; M22995; AAA36150.1; -; mRNA.
DR EMBL; AF493912; AAM12626.1; -; mRNA.
DR EMBL; AL049557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014086; AAH14086.1; -; mRNA.
DR CCDS; CCDS840.1; -.
DR PIR; A32342; A32342.
DR RefSeq; NP_001010935.1; NM_001010935.2.
DR RefSeq; NP_001278825.1; NM_001291896.1.
DR RefSeq; NP_002875.1; NM_002884.3.
DR RefSeq; XP_016857451.1; XM_017001962.1.
DR RefSeq; XP_016857452.1; XM_017001963.1.
DR RefSeq; XP_016857453.1; XM_017001964.1.
DR PDB; 1C1Y; X-ray; 1.90 A; A=1-167.
DR PDB; 1GUA; X-ray; 2.00 A; A=1-167.
DR PDB; 3KUC; X-ray; 1.92 A; A=1-167.
DR PDB; 4KVG; X-ray; 1.65 A; A/C=1-167.
DR PDBsum; 1C1Y; -.
DR PDBsum; 1GUA; -.
DR PDBsum; 3KUC; -.
DR PDBsum; 4KVG; -.
DR AlphaFoldDB; P62834; -.
DR SMR; P62834; -.
DR BioGRID; 111841; 152.
DR CORUM; P62834; -.
DR DIP; DIP-29106N; -.
DR IntAct; P62834; 44.
DR MINT; P62834; -.
DR STRING; 9606.ENSP00000358723; -.
DR BindingDB; P62834; -.
DR ChEMBL; CHEMBL1255139; -.
DR GlyGen; P62834; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62834; -.
DR PhosphoSitePlus; P62834; -.
DR SwissPalm; P62834; -.
DR BioMuta; RAP1A; -.
DR DMDM; 51338607; -.
DR OGP; P62834; -.
DR EPD; P62834; -.
DR jPOST; P62834; -.
DR MassIVE; P62834; -.
DR MaxQB; P62834; -.
DR PaxDb; P62834; -.
DR PeptideAtlas; P62834; -.
DR PRIDE; P62834; -.
DR ProteomicsDB; 57431; -.
DR TopDownProteomics; P62834; -.
DR Antibodypedia; 4330; 468 antibodies from 37 providers.
DR DNASU; 5906; -.
DR Ensembl; ENST00000356415.5; ENSP00000348786.1; ENSG00000116473.15.
DR Ensembl; ENST00000369709.4; ENSP00000358723.3; ENSG00000116473.15.
DR Ensembl; ENST00000687939.1; ENSP00000509234.1; ENSG00000116473.15.
DR GeneID; 5906; -.
DR KEGG; hsa:5906; -.
DR MANE-Select; ENST00000369709.4; ENSP00000358723.3; NM_002884.4; NP_002875.1.
DR UCSC; uc001ebi.4; human.
DR CTD; 5906; -.
DR DisGeNET; 5906; -.
DR GeneCards; RAP1A; -.
DR HGNC; HGNC:9855; RAP1A.
DR HPA; ENSG00000116473; Low tissue specificity.
DR MIM; 179520; gene.
DR neXtProt; NX_P62834; -.
DR OpenTargets; ENSG00000116473; -.
DR PharmGKB; PA34217; -.
DR VEuPathDB; HostDB:ENSG00000116473; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000160251; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P62834; -.
DR OMA; NVPMVIV; -.
DR PhylomeDB; P62834; -.
DR TreeFam; TF313014; -.
DR PathwayCommons; P62834; -.
DR Reactome; R-HSA-170968; Frs2-mediated activation.
DR Reactome; R-HSA-170984; ARMS-mediated activation.
DR Reactome; R-HSA-354192; Integrin signaling.
DR Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-HSA-392517; Rap1 signalling.
DR Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR SignaLink; P62834; -.
DR SIGNOR; P62834; -.
DR BioGRID-ORCS; 5906; 33 hits in 1045 CRISPR screens.
DR ChiTaRS; RAP1A; human.
DR EvolutionaryTrace; P62834; -.
DR GeneWiki; RAP1A; -.
DR GenomeRNAi; 5906; -.
DR Pharos; P62834; Tchem.
DR PRO; PR:P62834; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P62834; protein.
DR Bgee; ENSG00000116473; Expressed in blood vessel layer and 212 other tissues.
DR ExpressionAtlas; P62834; baseline and differential.
DR Genevisible; P62834; HS.
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; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
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; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IBA:GO_Central.
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; IDA:GO_Central.
DR GO; GO:0032486; P:Rap protein signal transduction; IMP:UniProtKB.
DR GO; GO:1901888; P:regulation of cell junction assembly; IMP:UniProtKB.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
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 3D-structure; Cell junction; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Endosome; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Neurogenesis; Nucleotide-binding; Prenylation;
KW Reference proteome; Tumor suppressor.
FT CHAIN 1..181
FT /note="Ras-related protein Rap-1A"
FT /id="PRO_0000030199"
FT PROPEP 182..184
FT /note="Removed in mature form"
FT /id="PRO_0000030200"
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:0000269|PubMed:7791872,
FT ECO:0000269|PubMed:8756332"
FT BINDING 29..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:7791872,
FT ECO:0000269|PubMed:8756332"
FT BINDING 60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:7791872,
FT ECO:0000269|PubMed:8756332"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:7791872,
FT ECO:0000269|PubMed:8756332"
FT MOD_RES 181
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:1899909"
FT LIPID 181
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1899909"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:4KVG"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:4KVG"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1GUA"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:4KVG"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:4KVG"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:4KVG"
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
