RHO3_SCHPO
ID RHO3_SCHPO Reviewed; 205 AA.
AC O13928;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=GTP-binding protein rho3;
DE Flags: Precursor;
GN Name=rho3; ORFNames=SPAC23C4.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, INTERACTION WITH FOR3, AND SUBCELLULAR LOCATION.
RX PubMed=12415007; DOI=10.1242/jcs.00150;
RA Nakano K., Imai J., Arai R., Toh-e A., Matsui Y., Mabuchi I.;
RT "The small GTPase Rho3 and the diaphanous/formin For3 function in polarized
RT cell growth in fission yeast.";
RL J. Cell Sci. 115:4629-4639(2002).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-25 AND THR-27.
RX PubMed=12930742; DOI=10.1093/genetics/164.4.1323;
RA Wang H., Tang X., Balasubramanian M.K.;
RT "Rho3p regulates cell separation by modulating exocyst function in
RT Schizosaccharomyces pombe.";
RL Genetics 164:1323-1331(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PALMITOYLATION.
RX PubMed=23843742; DOI=10.1371/journal.pbio.1001597;
RA Zhang M.M., Wu P.Y., Kelly F.D., Nurse P., Hang H.C.;
RT "Quantitative control of protein S-palmitoylation regulates meiotic entry
RT in fission yeast.";
RL PLoS Biol. 11:e1001597-e1001597(2013).
CC -!- FUNCTION: Involved in controlling cell shape and septation
CC (PubMed:12415007). Regulates cell separation by modulating the function
CC of the exocyst complex (PubMed:12930742). Involved in post-Golgi
CC vesicle transport (PubMed:12930742). Involved in driving sexual
CC development in a palmitoylation-dependent manner (PubMed:23843742).
CC {ECO:0000269|PubMed:12415007, ECO:0000269|PubMed:12930742,
CC ECO:0000269|PubMed:23843742}.
CC -!- SUBUNIT: Interacts with for3. {ECO:0000269|PubMed:12415007}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12415007,
CC ECO:0000269|PubMed:12930742}; Lipid-anchor
CC {ECO:0000269|PubMed:12415007, ECO:0000269|PubMed:12930742,
CC ECO:0000269|PubMed:23843742}. Note=Found at the cell periphery and the
CC growing tips of interphase cells. Localized to the division site during
CC cell division.
CC -!- DEVELOPMENTAL STAGE: Expressed during meiosis (at protein level).
CC {ECO:0000269|PubMed:23843742}.
CC -!- PTM: Palmitoylated by the erf2-erf4 complex.
CC {ECO:0000269|PubMed:23843742}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {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; CU329670; CAD86888.1; -; Genomic_DNA.
DR PIR; T38263; T38263.
DR RefSeq; NP_001018193.1; NM_001018576.2.
DR AlphaFoldDB; O13928; -.
DR SMR; O13928; -.
DR BioGRID; 280587; 50.
DR STRING; 4896.SPAC23C4.08.1; -.
DR SwissPalm; O13928; -.
DR MaxQB; O13928; -.
DR PaxDb; O13928; -.
DR EnsemblFungi; SPAC23C4.08.1; SPAC23C4.08.1:pep; SPAC23C4.08.
DR GeneID; 3361511; -.
DR KEGG; spo:SPAC23C4.08; -.
DR PomBase; SPAC23C4.08; rho3.
DR VEuPathDB; FungiDB:SPAC23C4.08; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; O13928; -.
DR OMA; MPLCGGS; -.
DR PhylomeDB; O13928; -.
DR Reactome; R-SPO-416482; G alpha (12/13) signalling events.
DR Reactome; R-SPO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-9013026; RHOB GTPase cycle.
DR Reactome; R-SPO-9013106; RHOC GTPase cycle.
DR Reactome; R-SPO-9013405; RHOD GTPase cycle.
DR Reactome; R-SPO-9035034; RHOF GTPase cycle.
DR Reactome; R-SPO-9696264; RND3 GTPase cycle.
DR Reactome; R-SPO-9696270; RND2 GTPase cycle.
DR Reactome; R-SPO-9696273; RND1 GTPase cycle.
DR PRO; PR:O13928; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; IDA:PomBase.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:PomBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; TAS:PomBase.
DR GO; GO:0010590; P:regulation of septum digestion after cytokinesis; IMP:PomBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
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; Cell shape; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome.
FT CHAIN 1..202
FT /note="GTP-binding protein rho3"
FT /id="PRO_0000198942"
FT PROPEP 203..205
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT /id="PRO_0000281272"
FT MOTIF 42..50
FT /note="Effector region"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20171"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT MOD_RES 202
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT LIPID 202
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT MUTAGEN 25
FT /note="G->V: Abnormal cell wall deposition."
FT /evidence="ECO:0000269|PubMed:12930742"
FT MUTAGEN 27
FT /note="T->N: Defective in cell separation."
FT /evidence="ECO:0000269|PubMed:12930742"
SQ SEQUENCE 205 AA; 22502 MW; 947CB98094841D25 CRC64;
MSSCFGSKKK PIYRKIVILG DGAAGKTSLL NVFTKGYFPQ VYEPTIFENY IHDIFVDGNS
IELSLWDTAG QEEYDQLRSL SYSDTHVIMI CFAVDSRDSL ENVITKWLPE VSSNCPGVKL
VLVALKCDLR GADEEQVDHS KIIDYEEGLA AAKKINAVRY LECSAKLNRG VNEAFTEAAR
VALAAQPRGT KDGADESHGT GCIIA
