ID S9PU32_SCHOY Unreviewed; 192 AA.
AC S9PU32;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Cell division control protein 42 homolog {ECO:0000256|RuleBase:RU367141};
DE EC=3.6.5.2 {ECO:0000256|RuleBase:RU367141};
GN ORFNames=SOCG_00374 {ECO:0000313|EMBL:EPX72611.1};
OS Schizosaccharomyces octosporus (strain yFS286) (Fission yeast)
OS (Octosporomyces octosporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=483514 {ECO:0000313|EMBL:EPX72611.1};
RN [1] {ECO:0000313|EMBL:EPX72611.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YFS286 {ECO:0000313|EMBL:EPX72611.1};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [2] {ECO:0000313|EMBL:EPX72611.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YFS286 {ECO:0000313|EMBL:EPX72611.1};
RG The Broad Institute Genome Sequencing Platform;
RA Nusbaum C., Russ C., Rhind N., Niki H., Allshire R., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Birren B.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC an active GTP-bound and an inactive GDP-bound state.
CC {ECO:0000256|RuleBase:RU367141}.
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:0000256|RuleBase:RU367141};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367141};
CC Lipid-anchor {ECO:0000256|RuleBase:RU367141}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42
CC subfamily. {ECO:0000256|ARBA:ARBA00008112,
CC ECO:0000256|RuleBase:RU367141}.
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DR EMBL; KE503207; EPX72611.1; -; Genomic_DNA.
DR RefSeq; XP_013018248.1; XM_013162794.1.
DR AlphaFoldDB; S9PU32; -.
DR EnsemblFungi; EPX72611; EPX72611; SOCG_00374.
DR GeneID; 25029358; -.
DR VEuPathDB; FungiDB:SOCG_00374; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR OMA; ANIRSKW; -.
DR OrthoDB; 5480056at2759; -.
DR Proteomes; UP000016088; Unassembled WGS sequence.
DR GO; GO:0071521; C:Cdc42 GTPase complex; IEA:EnsemblFungi.
DR GO; GO:1902716; C:cell cortex of growing cell tip; IEA:EnsemblFungi.
DR GO; GO:0032154; C:cleavage furrow; IEA:EnsemblFungi.
DR GO; GO:0090726; C:cortical dynamic polarity patch; IEA:EnsemblFungi.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0070382; C:exocytic vesicle; IEA:EnsemblFungi.
DR GO; GO:0097575; C:lateral cell cortex; IEA:EnsemblFungi.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IEA:EnsemblFungi.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:EnsemblFungi.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IEA:EnsemblFungi.
DR GO; GO:1902917; P:positive regulation of mating projection assembly; IEA:EnsemblFungi.
DR GO; GO:0032951; P:regulation of beta-glucan biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0032955; P:regulation of division septum assembly; IEA:EnsemblFungi.
DR GO; GO:2001135; P:regulation of endocytic recycling; IEA:EnsemblFungi.
DR GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IEA:EnsemblFungi.
DR GO; GO:0017157; P:regulation of exocytosis; IEA:EnsemblFungi.
DR GO; GO:0033157; P:regulation of intracellular protein transport; IEA:EnsemblFungi.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
DR PROSITE; PS51420; RHO; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367141};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU367141};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU367141};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367141};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367141};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289, ECO:0000256|RuleBase:RU367141}.
SQ SEQUENCE 192 AA; 21408 MW; E81A07BDF7EE0888 CRC64;
MPTIKCVVVG DGAVGKTCLL ISYTTNKFPS DYVPTVFDNY AVTVMIGDEP YTLGLFDTAG
QEDYDRLRPL SYPQTDVFLV CFSVTSPASF ENVKEKWFPE VHHHCPGVPC LIVGTQIDLR
DDPSVQQKLA RQHKHTLTHE QGERLARELG AVKYVECSAL TQRGLKNVFD EAIVAALDPP
VPHKKKTKCL IM
//
