CDC42_YEAST
ID CDC42_YEAST Reviewed; 191 AA.
AC P19073; D6VYN1; Q05978;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Cell division control protein 42;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P60953};
DE AltName: Full=Suppressor of RHO3 protein 2;
DE Flags: Precursor;
GN Name=CDC42; Synonyms=SRO2; OrderedLocusNames=YLR229C; ORFNames=L8083.13;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2164028; DOI=10.1083/jcb.111.1.143;
RA Johnson D.I., Pringle J.R.;
RT "Molecular characterization of CDC42, a Saccharomyces cerevisiae gene
RT involved in the development of cell polarity.";
RL J. Cell Biol. 111:143-152(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP INTERACTION WITH BEM4.
RX PubMed=8754839; DOI=10.1128/mcb.16.8.4387;
RA Mack D., Nishimura K., Dennehey B.K., Arbogast T., Parkinson J., Toh-e A.,
RA Pringle J.R., Bender A., Matsui Y.;
RT "Identification of the bud emergence gene BEM4 and its interactions with
RT rho-type GTPases in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:4387-4395(1996).
RN [6]
RP MUTAGENESIS.
RX PubMed=9178507;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<561::aid-yea114>3.0.co;2-x;
RA Miller P.J., Johnson D.I.;
RT "Characterization of the Saccharomyces cerevisiae cdc42-1ts allele and new
RT temperature-conditional-lethal cdc42 alleles.";
RL Yeast 13:561-572(1997).
RN [7]
RP INTERACTION WITH RGA1.
RX PubMed=7498791; DOI=10.1101/gad.9.23.2949;
RA Stevenson B.J., Ferguson B., de Virgilio C., Bi E., Pringle J.R.,
RA Ammerer G., Sprague G.F. Jr.;
RT "Mutation of RGA1, which encodes a putative GTPase-activating protein for
RT the polarity-establishment protein Cdc42p, activates the pheromone-response
RT pathway in the yeast Saccharomyces cerevisiae.";
RL Genes Dev. 9:2949-2963(1995).
RN [8]
RP FUNCTION, AND INTERACTION WITH AXL2.
RX PubMed=17460121; DOI=10.1091/mbc.e06-09-0822;
RA Gao X.D., Sperber L.M., Kane S.A., Tong Z., Tong A.H., Boone C., Bi E.;
RT "Sequential and distinct roles of the cadherin domain-containing protein
RT Axl2p in cell polarization in yeast cell cycle.";
RL Mol. Biol. Cell 18:2542-2560(2007).
CC -!- FUNCTION: Involved in development of cell polarity during the cell
CC division cycle, and essential for bud emergence. Affects signaling in
CC the pheromone-response pathway through the STE20 protein kinase.
CC Negatively regulated by the GTPase-activating proteins RGA1, BEM3, and
CC BEM4. {ECO:0000269|PubMed:17460121}.
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:P60953};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P60953};
CC -!- SUBUNIT: Interacts with BEM4; the interaction is direct
CC (PubMed:8754839). Interacts with AXL2 (PubMed:17460121). Interacts with
CC RGA1 (PubMed:7498791). {ECO:0000269|PubMed:17460121,
CC ECO:0000269|PubMed:7498791, ECO:0000269|PubMed:8754839}.
CC -!- INTERACTION:
CC P19073; Q99299: AIM44; NbExp=4; IntAct=EBI-4274, EBI-29423;
CC P19073; P29366: BEM1; NbExp=4; IntAct=EBI-4274, EBI-3508;
CC P19073; P11433: CDC24; NbExp=4; IntAct=EBI-4274, EBI-4220;
CC P19073; Q12434: RDI1; NbExp=2; IntAct=EBI-4274, EBI-7525;
CC P19073; Q03497: STE20; NbExp=6; IntAct=EBI-4274, EBI-18285;
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. CDC42
CC subfamily. {ECO:0000305}.
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DR EMBL; X51906; CAA36186.1; -; Genomic_DNA.
DR EMBL; U19027; AAB67416.1; -; Genomic_DNA.
DR EMBL; AY557933; AAS56259.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09547.1; -; Genomic_DNA.
DR PIR; S51452; S51452.
DR RefSeq; NP_013330.1; NM_001182116.1.
DR AlphaFoldDB; P19073; -.
DR SMR; P19073; -.
DR BioGRID; 31499; 325.
DR DIP; DIP-862N; -.
DR IntAct; P19073; 23.
DR MINT; P19073; -.
DR STRING; 4932.YLR229C; -.
DR iPTMnet; P19073; -.
DR MaxQB; P19073; -.
DR PaxDb; P19073; -.
DR PRIDE; P19073; -.
DR EnsemblFungi; YLR229C_mRNA; YLR229C; YLR229C.
DR GeneID; 850930; -.
DR KEGG; sce:YLR229C; -.
DR SGD; S000004219; CDC42.
DR VEuPathDB; FungiDB:YLR229C; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000153675; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P19073; -.
DR OMA; ITHHQQK; -.
DR BioCyc; YEAST:G3O-32343-MON; -.
DR Reactome; R-SCE-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-SCE-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-SCE-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-SCE-5627123; RHO GTPases activate PAKs.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-9013148; CDC42 GTPase cycle.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P19073; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P19073; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005940; C:septin ring; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0007119; P:budding cell isotropic bud growth; IMP:SGD.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:SGD.
DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IMP:SGD.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:AgBase.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD.
DR GO; GO:0060178; P:regulation of exocyst localization; IMP:SGD.
DR GO; GO:0031384; P:regulation of initiation of mating projection growth; IMP:SGD.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IMP:SGD.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:SGD.
DR GO; GO:0031106; P:septin ring organization; IMP:SGD.
DR CDD; cd01874; Cdc42; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR037874; Cdc42.
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 cycle; Cell division; Cell membrane; GTP-binding; Hydrolase;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Pheromone response;
KW Prenylation; Reference proteome.
FT CHAIN 1..188
FT /note="Cell division control protein 42"
FT /id="PRO_0000198955"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281285"
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|UniProtKB:P61586"
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|UniProtKB:P61586"
FT MOD_RES 188
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT LIPID 188
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT MUTAGEN 12
FT /note="G->V: Enhances interaction with RGA1."
FT /evidence="ECO:0000269|PubMed:9178507"
FT MUTAGEN 58
FT /note="T->A: Temperature-sensitive mutant."
FT /evidence="ECO:0000269|PubMed:9178507"
FT MUTAGEN 61
FT /note="Q->L: Enhances interaction with RGA1."
FT /evidence="ECO:0000269|PubMed:9178507"
FT MUTAGEN 71
FT /note="S->P: Temperature-sensitive mutant."
FT /evidence="ECO:0000269|PubMed:9178507"
FT MUTAGEN 97
FT /note="W->R: Temperature-sensitive mutant."
FT /evidence="ECO:0000269|PubMed:9178507"
FT MUTAGEN 118
FT /note="D->A: Dramatically reduces interaction with RGA1."
FT /evidence="ECO:0000269|PubMed:9178507"
FT MUTAGEN 142
FT /note="G->S: In CDC42-1; temperature-sensitive mutant."
FT /evidence="ECO:0000269|PubMed:9178507"
FT MUTAGEN 188
FT /note="C->S: Enhances interaction with RGA1."
FT /evidence="ECO:0000269|PubMed:9178507"
FT CONFLICT 189
FT /note="A -> T (in Ref. 1; CAA36186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 21323 MW; 30BD644BA9836B2C CRC64;
MQTLKCVVVG DGAVGKTCLL ISYTTNQFPA DYVPTVFDNY AVTVMIGDEP YTLGLFDTAG
QEDYDRLRPL SYPSTDVFLV CFSVISPPSF ENVKEKWFPE VHHHCPGVPC LVVGTQIDLR
DDKVIIEKLQ RQRLRPITSE QGSRLARELK AVKYVECSAL TQRGLKNVFD EAIVAALEPP
VIKKSKKCAI L
