RAPA_DICDI
ID RAPA_DICDI Reviewed; 186 AA.
AC P18613; Q54EV9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ras-related protein rapA;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P10114};
DE AltName: Full=Ras-related protein rap-1;
DE Flags: Precursor;
GN Name=rapA; Synonyms=rap1; ORFNames=DDB_G0291237;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX2;
RX PubMed=2205839; DOI=10.1093/nar/18.17.5265;
RA Robbins S.M., Suttorp V.V., Weeks G., Spiegelman G.B.;
RT "A ras-related gene from the lower eukaryote Dictyostelium that is highly
RT conserved relative to the human rap genes.";
RL Nucleic Acids Res. 18:5265-5269(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF GLY-12.
RX PubMed=9950684; DOI=10.1091/mbc.10.2.393;
RA Seastone D.J., Zhang L., Buczynski G., Rebstein P., Weeks G.,
RA Spiegelman G., Cardelli J.;
RT "The small Mr Ras-like GTPase Rap1 and the phospholipase C pathway act to
RT regulate phagocytosis in Dictyostelium discoideum.";
RL Mol. Biol. Cell 10:393-406(1999).
RN [4]
RP DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-12, FUNCTION, AND INTERACTION WITH
RP RALGDS.
RX PubMed=12186953; DOI=10.1242/jcs.00039;
RA Kang R., Kae H., Ip H., Spiegelman G.B., Weeks G.;
RT "Evidence for a role for the Dictyostelium Rap1 in cell viability and the
RT response to osmotic stress.";
RL J. Cell Sci. 115:3675-3682(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
RN [6]
RP INTERACTION WITH GFLB, AND FUNCTION.
RX PubMed=27237792; DOI=10.1016/j.devcel.2016.05.001;
RA Liu Y., Lacal J., Veltman D.M., Fusetti F., van Haastert P.J., Firtel R.A.,
RA Kortholt A.;
RT "A Galpha-Stimulated RapGEF Is a Receptor-Proximal Regulator of
RT Dictyostelium Chemotaxis.";
RL Dev. Cell 37:458-472(2016).
CC -!- FUNCTION: G protein of the Ras family that positively regulates
CC phagocytosis and negatively regulates macropinocytosis
CC (PubMed:9950684). May be involved in the activation of guanylyl cyclase
CC during the response to hyperosmotic conditions (PubMed:12186953).
CC Overexpressing cells generate alterations in cell shape and contractile
CC responses (PubMed:12186953). Involved in chemotaxis via regulation of
CC the balance of Ras and Rap signaling at the leading edge of chemotaxing
CC cells (PubMed:27237792). {ECO:0000269|PubMed:12186953,
CC ECO:0000269|PubMed:27237792, ECO:0000269|PubMed:9950684}.
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:P10114};
CC -!- SUBUNIT: Interacts with ralGDS (only when rapA is in its GTP-bound
CC state) (PubMed:12186953). Interacts with the Rap guanine nucleotide
CC exchange factor glfB (PubMed:27237792). {ECO:0000269|PubMed:12186953,
CC ECO:0000269|PubMed:27237792}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: This protein is expressed at all stages during
CC development but is expressed maximally during the aggregation and
CC culmination periods.
CC -!- DISRUPTION PHENOTYPE: Null cells exhibit reduced viability in response
CC to osmotic shock, reduced accumulation of cGMP in response to osmotic
CC shock and decrease in growth rate. {ECO:0000269|PubMed:12186953}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; X54291; CAA38185.1; -; mRNA.
DR EMBL; AAFI02000177; EAL61602.1; -; Genomic_DNA.
DR PIR; S11229; S11229.
DR RefSeq; XP_635131.1; XM_630039.1.
DR AlphaFoldDB; P18613; -.
DR SMR; P18613; -.
DR IntAct; P18613; 1.
DR STRING; 44689.DDB0216229; -.
DR PaxDb; P18613; -.
DR ABCD; P18613; 5 sequenced antibodies.
DR EnsemblProtists; EAL61602; EAL61602; DDB_G0291237.
DR GeneID; 8628077; -.
DR KEGG; ddi:DDB_G0291237; -.
DR dictyBase; DDB_G0291237; rapA.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P18613; -.
DR OMA; CYRKQWV; -.
DR PhylomeDB; P18613; -.
DR Reactome; R-DDI-170968; Frs2-mediated activation.
DR Reactome; R-DDI-354192; Integrin signaling.
DR Reactome; R-DDI-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-DDI-392517; Rap1 signalling.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:P18613; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0060187; C:cell pole; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0031256; C:leading edge membrane; IDA:dictyBase.
DR GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR GO; GO:0140220; C:pathogen-containing vacuole; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0031982; C:vesicle; IDA:dictyBase.
DR GO; GO:0003925; F:G protein activity; IDA:dictyBase.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:dictyBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0030250; F:guanylate cyclase activator activity; IMP:dictyBase.
DR GO; GO:0031267; F:small GTPase binding; IDA:dictyBase.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:dictyBase.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:dictyBase.
DR GO; GO:0071321; P:cellular response to cGMP; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0006972; P:hyperosmotic response; IMP:dictyBase.
DR GO; GO:1902850; P:microtubule cytoskeleton organization involved in mitosis; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:dictyBase.
DR GO; GO:0048550; P:negative regulation of pinocytosis; IMP:dictyBase.
DR GO; GO:0006997; P:nucleus organization; IMP:dictyBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEP:dictyBase.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:1904515; P:positive regulation of TORC2 signaling; IGI:dictyBase.
DR GO; GO:0032486; P:Rap protein signal transduction; IEA:InterPro.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:dictyBase.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IGI:dictyBase.
DR GO; GO:0043520; P:regulation of myosin II filament assembly; IMP:dictyBase.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IDA:dictyBase.
DR GO; GO:0009409; P:response to cold; IEP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
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 membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..183
FT /note="Ras-related protein rapA"
FT /id="PRO_0000082684"
FT PROPEP 184..186
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281327"
FT MOTIF 34..42
FT /note="Effector region"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 183
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 183
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 12
FT /note="G->T: Enhanced phagocytosis."
FT /evidence="ECO:0000269|PubMed:12186953,
FT ECO:0000269|PubMed:9950684"
FT MUTAGEN 12
FT /note="G->V: Exhibits severely reduced chemotaxis towards
FT cAMP and enhanced accumulation of cGMP."
FT /evidence="ECO:0000269|PubMed:12186953,
FT ECO:0000269|PubMed:9950684"
SQ SEQUENCE 186 AA; 21006 MW; 3A992CD956AB2192 CRC64;
MPLREFKIVV LGSGGVGKSA LTVQFVQGIF VEKYDPTIED SYRKQVEVDS NQCMLEILDT
AGTEQFTAMR DLYMKNGQGF VLVYSIISNS TFNELPDLRE QILRVKDCED VPMVLVGNKC
DLHDQRVIST EQGEELARKF GDCYFLEASA KNKVNVEQIF YNLIRQINRK NPVGPPSKAK
SKCALL
