CDC42_ASHGO
ID CDC42_ASHGO Reviewed; 191 AA.
AC Q9HF56;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cell division control protein 42;
DE Flags: Precursor;
GN Name=CDC42; OrderedLocusNames=AGL093W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11156982; DOI=10.1093/genetics/157.2.601;
RA Wendland J., Philippsen P.;
RT "Cell polarity and hyphal morphogenesis are controlled by multiple rho-
RT protein modules in the filamentous ascomycete Ashbya gossypii.";
RL Genetics 157:601-610(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Involved in development of cell polarity during the cell
CC division cycle. Required for the establishment of actin polarization in
CC germ cells. {ECO:0000269|PubMed:11156982}.
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; AF210627; AAG41247.1; -; Genomic_DNA.
DR EMBL; AE016820; AAS54397.1; -; Genomic_DNA.
DR RefSeq; NP_986573.1; NM_211635.1.
DR AlphaFoldDB; Q9HF56; -.
DR SMR; Q9HF56; -.
DR STRING; 33169.AAS54397; -.
DR EnsemblFungi; AAS54397; AAS54397; AGOS_AGL093W.
DR GeneID; 4622872; -.
DR KEGG; ago:AGOS_AGL093W; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q9HF56; -.
DR OMA; ITHHQQK; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0031965; C:nuclear membrane; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005940; C:septin ring; IEA:EnsemblFungi.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
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; IEA:EnsemblFungi.
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; 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:2000222; P:positive regulation of pseudohyphal growth; IEA:EnsemblFungi.
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:0031384; P:regulation of initiation of mating projection growth; 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 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 3: Inferred from homology;
KW Cell cycle; Cell division; Cell membrane; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..188
FT /note="Cell division control protein 42"
FT /id="PRO_0000198951"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281281"
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; 21470 MW; E73389C1847CD5B9 CRC64;
MQTLKCVVVG DGAVGKTCLL ISYTTNQFPA DYVPTVFDNY AVTVMIGDEP YTLGLFDTAG
QEDYDRLRPL SYPSTDVFLV CFSVVSPPSF ENVKEKWFPE VHHHCPGVPC LIVGTQIDLR
ENKMVIEKLQ RQRLRPITPE QGEKFARELR AVKYVECSAL TQRGLKNVFD EAIVAALEPP
VIKKSKKCTI L
