RHO4_SCHPO
ID RHO4_SCHPO Reviewed; 203 AA.
AC Q874R1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=GTP-binding protein rho4;
DE Flags: Precursor;
GN Name=rho4; ORFNames=SPAC16A10.04;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-23 AND THR-28.
RX PubMed=12796297; DOI=10.1128/ec.2.3.521-533.2003;
RA Santos B., Gutierrez J., Calonge T.M., Perez P.;
RT "Novel Rho GTPase involved in cytokinesis and cell wall integrity in the
RT fission yeast Schizosaccharomyces pombe.";
RL Eukaryot. Cell 2:521-533(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-23 AND GLN-74.
RX PubMed=12653963; DOI=10.1046/j.1365-2443.2003.00639.x;
RA Nakano K., Mutoh T., Arai R., Mabuchi I.;
RT "The small GTPase Rho4 is involved in controlling cell morphology and
RT septation in fission yeast.";
RL Genes Cells 8:357-370(2003).
RN [3]
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).
CC -!- FUNCTION: Required for cell separation. Involved in the regulation of
CC the septum degradation during cytokinesis and in the organization of F-
CC actin patches and cytoplasmic microtubules.
CC {ECO:0000269|PubMed:12653963, ECO:0000269|PubMed:12796297}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12653963,
CC ECO:0000269|PubMed:12796297}. Note=Membrane-bound. Associates with the
CC septum during mitosis.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAD86931.2; -; Genomic_DNA.
DR RefSeq; NP_001018257.1; NM_001019469.2.
DR AlphaFoldDB; Q874R1; -.
DR SMR; Q874R1; -.
DR BioGRID; 280552; 32.
DR STRING; 4896.SPAC16A10.04.1; -.
DR MaxQB; Q874R1; -.
DR PaxDb; Q874R1; -.
DR PRIDE; Q874R1; -.
DR EnsemblFungi; SPAC16A10.04.1; SPAC16A10.04.1:pep; SPAC16A10.04.
DR GeneID; 3361476; -.
DR KEGG; spo:SPAC16A10.04; -.
DR PomBase; SPAC16A10.04; rho4.
DR VEuPathDB; FungiDB:SPAC16A10.04; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q874R1; -.
DR OMA; NASYIEC; -.
DR PhylomeDB; Q874R1; -.
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:Q874R1; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005938; C:cell cortex; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; EXP: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:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; NAS:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:PomBase.
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:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IMP:PomBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; TAS:PomBase.
DR GO; GO:2001043; P:positive regulation of septum digestion after cytokinesis; EXP:PomBase.
DR GO; GO:0030994; P:primary cell septum disassembly; TAS:PomBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:PomBase.
DR GO; GO:0032955; P:regulation of division septum assembly; 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; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..200
FT /note="GTP-binding protein rho4"
FT /id="PRO_0000198943"
FT PROPEP 201..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281273"
FT MOTIF 43..51
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 200
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 23
FT /note="G->V: Cell lysis during separation."
FT /evidence="ECO:0000269|PubMed:12653963,
FT ECO:0000269|PubMed:12796297"
FT MUTAGEN 28
FT /note="T->N: No cell lysis."
FT /evidence="ECO:0000269|PubMed:12796297"
FT MUTAGEN 74
FT /note="Q->L: Shrunken cells."
FT /evidence="ECO:0000269|PubMed:12653963"
SQ SEQUENCE 203 AA; 22408 MW; 69025B96208649F9 CRC64;
MSAFKKSGSK SETSKKLVVV GDGGCGKTCL LIVFSSGTFP ERYVPTVFEN YITDITYGPN
SKVIELALWD TAGQEEYDRL RPLSYPNSNV ILLCFSIDCP ASLNNVTEKW YPEVQHFCPR
TPIVLVGLKA DLRKDRNATE VLRTQGLTPV TYQQAQSVAL SMNAPYVECS AKENTGVNEV
FQLAVGLTIK KSFSFSKKSC VIL
