ID CDC42_CANAL Reviewed; 191 AA. AC P0CY33; A0A1D8PED3; O14426; Q59QC8; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 66. DE RecName: Full=Cell division control protein 42 homolog; DE Flags: Precursor; GN Name=CDC42; OrderedLocusNames=CAALFM_C108450CA; GN ORFNames=CaO19.390, CaO19.8020; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). CC -!- FUNCTION: Involved in hyphal formation, virulence, morphogenesis. 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}. 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; CP017623; AOW26483.1; -; Genomic_DNA. DR RefSeq; XP_711878.1; XM_706785.2. DR AlphaFoldDB; P0CY33; -. DR BMRB; P0CY33; -. DR SMR; P0CY33; -. DR BioGRID; 1229572; 7. DR IntAct; P0CY33; 1. DR MINT; P0CY33; -. DR STRING; 237561.P0CY33; -. DR EnsemblFungi; C1_08450C_A-T; C1_08450C_A-T-p1; C1_08450C_A. DR GeneID; 3646488; -. DR KEGG; cal:CAALFM_C108450CA; -. DR CGD; CAL0000192612; CDC42. DR VEuPathDB; FungiDB:C1_08450C_A; -. DR eggNOG; KOG0393; Eukaryota. DR HOGENOM; CLU_041217_21_3_1; -. DR InParanoid; P0CY33; -. DR OMA; RRLGCFK; -. DR OrthoDB; 5480056at2759; -. DR PRO; PR:P0CY33; -. DR Proteomes; UP000000559; Chromosome 1. DR GO; GO:0030428; C:cell septum; NAS:CGD. DR GO; GO:0005935; C:cellular bud neck; IDA:CGD. DR GO; GO:0005934; C:cellular bud tip; IDA:CGD. DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD. DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi. DR GO; GO:0001411; C:hyphal tip; IDA:CGD. DR GO; GO:0031562; C:hyphal tip polarisome; IDA:CGD. DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi. DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi. DR GO; GO:0016020; C:membrane; IMP:CGD. DR GO; GO:0031965; C:nuclear membrane; IEA:EnsemblFungi. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005940; C:septin ring; IEA:EnsemblFungi. DR GO; GO:0031521; C:spitzenkorper; IDA:CGD. DR GO; GO:0005525; F:GTP binding; IDA:CGD. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. 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; IEA:EnsemblFungi. DR GO; GO:0007119; P:budding cell isotropic bud growth; IEA:EnsemblFungi. DR GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central. DR GO; GO:0007114; P:cell budding; IMP:CGD. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0036187; P:cell growth mode switching, budding to filamentous; IMP:CGD. DR GO; GO:0000902; P:cell morphogenesis; IMP:CGD. DR GO; GO:0000747; P:conjugation with cellular fusion; IEA:EnsemblFungi. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR GO; GO:0030010; P:establishment of cell polarity; IMP:CGD. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central. DR GO; GO:0030447; P:filamentous growth; IMP:CGD. DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD. DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD. DR GO; GO:0030448; P:hyphal growth; IMP:CGD. DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi. DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi. DR GO; GO:0045921; P:positive regulation of exocytosis; IEA:EnsemblFungi. DR GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD. DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IEA:EnsemblFungi. DR GO; GO:0001558; P:regulation of cell growth; IMP:CGD. DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:EnsemblFungi. DR GO; GO:0007096; P:regulation of exit from mitosis; IEA:EnsemblFungi. DR GO; GO:0060178; P:regulation of exocyst localization; IEA:EnsemblFungi. DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IEA:EnsemblFungi. DR GO; GO:0031106; P:septin ring organization; IEA:EnsemblFungi. DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:CGD. DR CDD; cd01874; Cdc42; 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_dom. DR InterPro; IPR001806; Small_GTPase. DR InterPro; IPR003578; Small_GTPase_Rho. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24072:SF192; CELL DIVISION CONTROL PROTEIN 42 HOMOLOG; 1. DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 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 3: Inferred from homology; KW Cell cycle; Cell division; Cell membrane; GTP-binding; Lipoprotein; KW Membrane; Methylation; Nucleotide-binding; Prenylation; Reference proteome; KW Virulence. FT CHAIN 1..188 FT /note="Cell division control protein 42 homolog" FT /id="PRO_0000198952" FT PROPEP 189..191 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000281282" FT MOTIF 32..40 FT /note="Effector region" FT /evidence="ECO:0000250" 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 188 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250" FT LIPID 188 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" SQ SEQUENCE 191 AA; 21263 MW; 6F92C17659AD0AD9 CRC64; MQTIKCVVVG DGAVGKTCLL ISYTTSKFPA DYVPTVFDNY AVTVMIGDEP FTLGLFDTAG QEDYDRLRPL SYPSTDVFLV CFSVISPASF ENVKEKWFPE VHHHCPGVPI IIVGTQTDLR NDDVILQRLH RQKLSPITQE QGEKLAKELR AVKYVECSAL TQRGLKTVFD EAIVAALEPP VIKKSKKCTI L //