RAC1A_DICDI
ID RAC1A_DICDI Reviewed; 194 AA.
AC P34144; Q54YK6; Q9GPU0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Rho-related protein rac1A;
DE Flags: Precursor;
GN Name=rac1A; ORFNames=DDB_G0277869;
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=AX3;
RX PubMed=8294042; DOI=10.1016/0378-1119(93)90448-c;
RA Bush J.M. IV, Franek K., Cardelli J.A.;
RT "Cloning and characterization of seven novel Dictyostelium discoideum rac-
RT related genes belonging to the rho family of GTPases.";
RL Gene 136:61-68(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=11222756; DOI=10.1093/nar/29.5.1068;
RA Rivero F., Dislich H., Gloeckner G., Noegel A.A.;
RT "The Dictyostelium discoideum family of Rho-related proteins.";
RL Nucleic Acids Res. 29:1068-1079(2001).
RN [3]
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 [4]
RP INTERACTION WITH LIME.
RX PubMed=9487125; DOI=10.1091/mbc.9.3.545;
RA Prassler J., Murr A., Stocker S., Faix J., Murphy J., Marriott G.;
RT "DdLIM is a cytoskeleton-associated protein involved in the protrusion of
RT lamellipodia in Dictyostelium.";
RL Mol. Biol. Cell 9:545-559(1998).
RN [5]
RP INTERACTION WITH RGAA.
RX PubMed=9739079; DOI=10.1242/jcs.111.20.3059;
RA Faix J., Clougherty C., Konzok A., Mintert U., Murphy J., Albrecht R.,
RA Muhlbauer B., Kuhlmann J.;
RT "The IQGAP-related protein DGAP1 interacts with Rac and is involved in the
RT modulation of the F-actin cytoskeleton and control of cell motility.";
RL J. Cell Sci. 111:3059-3071(1998).
RN [6]
RP INTERACTION WITH RGAA, AND FUNCTION.
RX PubMed=10825297; DOI=10.1242/jcs.113.12.2253;
RA Dumontier M., Hoecht P., Mintert U., Faix J.;
RT "Rac1 GTPases control filopodia formation, cell motility, endocytosis,
RT cytokinesis and development in Dictyostelium.";
RL J. Cell Sci. 113:2253-2265(2000).
RN [7]
RP INTERACTION WITH PAKB.
RX PubMed=15509655; DOI=10.1091/mbc.e04-06-0534;
RA de la Roche M., Mahasneh A., Lee S.-F., Rivero F., Cote G.P.;
RT "Cellular distribution and functions of wild-type and constitutively
RT activated Dictyostelium PakB.";
RL Mol. Biol. Cell 16:238-247(2005).
RN [8]
RP INTERACTION WITH FORH.
RC STRAIN=AX2;
RX PubMed=15908944; DOI=10.1038/ncb1266;
RA Schirenbeck A., Bretschneider T., Arasada R., Schleicher M., Faix J.;
RT "The Diaphanous-related formin dDia2 is required for the formation and
RT maintenance of filopodia.";
RL Nat. Cell Biol. 7:619-625(2005).
RN [9]
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).
CC -!- FUNCTION: Overexpression promotes the formation of filopodia and
CC membrane ruffles. {ECO:0000269|PubMed:10825297}.
CC -!- SUBUNIT: Interacts with forH. Interacts with pakB. May interact with
CC limE. Interacts (in GTP-bound form) with rgaA.
CC {ECO:0000269|PubMed:10825297, ECO:0000269|PubMed:15509655,
CC ECO:0000269|PubMed:15908944, ECO:0000269|PubMed:9487125,
CC ECO:0000269|PubMed:9739079}.
CC -!- INTERACTION:
CC P34144; Q54N00: forH; NbExp=2; IntAct=EBI-1808643, EBI-1808560;
CC P34144; Q54K32: rgaA; NbExp=4; IntAct=EBI-1808643, EBI-1808670;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; L11588; AAC37391.1; -; mRNA.
DR EMBL; AF309947; AAG45106.1; -; Genomic_DNA.
DR EMBL; AAFI02000023; EAL68107.1; -; Genomic_DNA.
DR RefSeq; XP_642196.1; XM_637104.1.
DR AlphaFoldDB; P34144; -.
DR SMR; P34144; -.
DR IntAct; P34144; 7.
DR STRING; 44689.DDB0214822; -.
DR SWISS-2DPAGE; P34144; -.
DR PaxDb; P34144; -.
DR EnsemblProtists; EAL68107; EAL68107; DDB_G0277869.
DR GeneID; 8621403; -.
DR KEGG; ddi:DDB_G0277869; -.
DR dictyBase; DDB_G0277869; rac1A.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P34144; -.
DR OMA; ITHHQQK; -.
DR PhylomeDB; P34144; -.
DR Reactome; R-DDI-193648; NRAGE signals death through JNK.
DR Reactome; R-DDI-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DDI-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-DDI-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DDI-445144; Signal transduction by L1.
DR Reactome; R-DDI-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-DDI-5627123; RHO GTPases activate PAKs.
DR Reactome; R-DDI-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DDI-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013406; RHOQ GTPase cycle.
DR Reactome; R-DDI-9013407; RHOH GTPase cycle.
DR Reactome; R-DDI-9013409; RHOJ GTPase cycle.
DR Reactome; R-DDI-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DDI-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-DDI-9706019; RHOBTB3 ATPase cycle.
DR Reactome; R-DDI-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P34144; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:1904269; C:cell leading edge cell cortex; IDA:dictyBase.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031254; C:cell trailing edge; IDA:dictyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:dictyBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; 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:0019901; F:protein kinase binding; IPI:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:dictyBase.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:dictyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:2000145; P:regulation of cell motility; IMP:dictyBase.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IMP:dictyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..191
FT /note="Rho-related protein rac1A"
FT /id="PRO_0000198895"
FT PROPEP 192..194
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281246"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 191
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 162
FT /note="Q -> E (in Ref. 1; AAC37391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 21572 MW; 718E2BDE338E0005 CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP INLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSIISPSSF ENVNGKWHPE ICHHAPNVPI ILVGTKLDMR
EDKETQDRLK EKKLYPISYE QGLAKMKEIN AVKYLECSAL TQKGLKTVFD EAIRAVINPP
LSKKKKSSGG CNIL
