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 27-MAR-2024, entry version 153. 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}. 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; CAD86931.2; -; Genomic_DNA. DR RefSeq; NP_001018257.1; NM_001019469.2. DR AlphaFoldDB; Q874R1; -. DR SMR; Q874R1; -. DR BioGRID; 280552; 32. DR STRING; 284812.Q874R1; -. DR MaxQB; Q874R1; -. DR PaxDb; 4896-SPAC16A10-04-1; -. 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; PTVFERH; -. DR PhylomeDB; Q874R1; -. DR Reactome; R-SPO-6798695; Neutrophil degranulation. 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:0009898; C:cytoplasmic side of plasma membrane; NAS:PomBase. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000935; C:division septum; IDA: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:0000917; P:division septum assembly; IMP:PomBase. 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:0008104; P:protein localization; IMP:PomBase. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR CDD; cd04132; Rho4_like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24072:SF181; GTP-BINDING PROTEIN RHO4; 1. DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 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 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 //