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   04-NOV-2026, entry version 229.
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;
GN   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; DOI=10.1038/387s087;
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 + phosphate + H(+); 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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=3; 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; 334.
DR   DIP; DIP-862N; -.
DR   FunCoup; P19073; 1222.
DR   IntAct; P19073; 23.
DR   STRING; 4932.YLR229C; -.
DR   iPTMnet; P19073; -.
DR   PaxDb; 4932-YLR229C; -.
DR   PeptideAtlas; P19073; -.
DR   EnsemblFungi; YLR229C_mRNA; YLR229C; YLR229C.
DR   GeneID; 850930; -.
DR   KEGG; sce:YLR229C; -.
DR   AGR; SGD:S000004219; -.
DR   SGD; S000004219; CDC42.
DR   VEuPathDB; FungiDB:YLR229C; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   HOGENOM; CLU_041217_21_3_1; -.
DR   InParanoid; P19073; -.
DR   OMA; AAYIECK; -.
DR   OrthoDB; 8830751at2759; -.
DR   BioCyc; YEAST:G3O-32343-MONOMER; -.
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-9013406; RHOQ GTPase cycle.
DR   Reactome; R-SCE-9013409; RHOJ 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   BioGRID-ORCS; 850930; 4 hits in 10 CRISPR screens.
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:0005635; C:nuclear envelope; 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:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament 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: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:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR   GO; GO:0071763; P:nuclear membrane organization; IDA: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: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   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd01874; Cdc42; 1.
DR   FunFam; 3.40.50.300:FF:000236; Cell division control protein 42; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR037874; Cdc42.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR24072; RHO FAMILY GTPASE; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell membrane; GTP-binding; Hydrolase;
KW   Lipoprotein; Magnesium; Membrane; Metal-binding; Methylation;
KW   Nucleotide-binding; Pheromone response; 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|UniProtKB:P62745"
FT                   /id="PRO_0000281285"
FT   MOTIF           32..40
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   BINDING         13
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         14
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         15
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         16
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         35
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         60
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         116
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         118
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         159
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   BINDING         160
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   MOD_RES         188
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
FT   LIPID           188
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P60953"
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
//