RAC1C_DICDI
ID RAC1C_DICDI Reviewed; 193 AA.
AC P34146; Q54S70; Q9U9S8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Rho-related protein rac1C;
DE Flags: Precursor;
GN Name=rac1C; ORFNames=DDB_G0282365;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RA Dumontier M., Hoecht P., Mintert U., Faix J.;
RT "Full length sequence of Rac1C.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 11-193.
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 [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 FUNCTION, AND INTERACTION WITH RGAA.
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).
CC -!- FUNCTION: Overexpression promotes the formation of filopodia and
CC membrane ruffles. {ECO:0000269|PubMed:10825297}.
CC -!- SUBUNIT: Interacts with pakB. Interacts (in GTP-bound form) with rgaA.
CC {ECO:0000269|PubMed:10825297, ECO:0000269|PubMed:15509655,
CC ECO:0000269|PubMed:9739079}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF310885; AAG45114.1; -; Genomic_DNA.
DR EMBL; AF153328; AAD37805.1; -; mRNA.
DR EMBL; AAFI02000047; EAL66042.1; -; Genomic_DNA.
DR EMBL; L11590; AAC37393.1; -; mRNA.
DR RefSeq; XP_640169.1; XM_635077.1.
DR AlphaFoldDB; P34146; -.
DR SMR; P34146; -.
DR IntAct; P34146; 1.
DR STRING; 44689.DDB0214823; -.
DR PaxDb; P34146; -.
DR EnsemblProtists; EAL66042; EAL66042; DDB_G0282365.
DR GeneID; 8623707; -.
DR KEGG; ddi:DDB_G0282365; -.
DR dictyBase; DDB_G0282365; rac1C.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P34146; -.
DR OMA; AAMYIEC; -.
DR PhylomeDB; P34146; -.
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 PRO; PR:P34146; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
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:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0019953; P:sexual reproduction; IEP:dictyBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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..190
FT /note="Rho-related protein rac1C"
FT /id="PRO_0000198897"
FT PROPEP 191..193
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281248"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 11..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 190
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 190
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 193 AA; 21550 MW; 9BE96E4E9CBDF539 CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP INLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSIISPSSY ENVSGKWGPE VFHHAPNVPI ILVGTKMDMR
EDKETQDRLK EKKLYPVSYE QGLLKMKEIN AFKYLECSAL TQKGLKTVFD EAIRSVINPP
VKKSKSKSGC NIL