RHO2_SCHPO
ID RHO2_SCHPO Reviewed; 200 AA.
AC Q10133;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=GTP-binding protein rho2;
DE Flags: Precursor;
GN Name=rho2; ORFNames=SPAC16.01;
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 [MRNA].
RC STRAIN=JY450;
RX PubMed=7698654; DOI=10.1016/0378-1119(94)00917-h;
RA Nakano K., Mabuchi I.;
RT "Isolation and sequencing of two cDNA clones encoding Rho proteins from the
RT fission yeast Schizosaccharomyces pombe.";
RL Gene 155:119-122(1995).
RN [2]
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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9405296; DOI=10.1242/jcs.111.2.149;
RA Hirata D., Nakano K., Fukui M., Takenaka H., Miyakawa T., Mabuchi I.;
RT "Genes that cause aberrant cell morphology by overexpression in fission
RT yeast: a role of a small GTP-binding protein Rho2 in cell morphogenesis.";
RL J. Cell Sci. 111:149-159(1998).
RN [4]
RP FUNCTION, AND INTERACTION WITH PCK2.
RX PubMed=11102532; DOI=10.1091/mbc.11.12.4393;
RA Calonge T.M., Nakano K., Arellano M., Arai R., Katayama S., Toda T.,
RA Mabuchi I., Perez P.;
RT "Schizosaccharomyces pombe rho2p GTPase regulates cell wall alpha-glucan
RT biosynthesis through the protein kinase pck2p.";
RL Mol. Biol. Cell 11:4393-4401(2000).
CC -!- FUNCTION: Involved in cell morphogenesis, the maintenance of growth
CC direction, control of polarity and of cell wall integrity. Regulates
CC the synthesis of alpha-D-glucan through activation of pck2.
CC {ECO:0000269|PubMed:11102532, ECO:0000269|PubMed:9405296}.
CC -!- SUBUNIT: Interacts with pck2. {ECO:0000269|PubMed:11102532}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9405296};
CC Lipid-anchor {ECO:0000269|PubMed:9405296}. Note=Found at the growing
CC tips of interphase cells and at the septum prior to cytokinesis.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; D38181; BAA07378.1; -; mRNA.
DR EMBL; CU329670; CAB57399.1; -; Genomic_DNA.
DR PIR; JC4045; JC4045.
DR RefSeq; NP_594569.1; NM_001019998.3.
DR AlphaFoldDB; Q10133; -.
DR SMR; Q10133; -.
DR BioGRID; 279222; 41.
DR STRING; 4896.SPAC16.01.1; -.
DR SwissPalm; Q10133; -.
DR MaxQB; Q10133; -.
DR PaxDb; Q10133; -.
DR EnsemblFungi; SPAC16.01.1; SPAC16.01.1:pep; SPAC16.01.
DR GeneID; 2542773; -.
DR KEGG; spo:SPAC16.01; -.
DR PomBase; SPAC16.01; rho2.
DR VEuPathDB; FungiDB:SPAC16.01; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q10133; -.
DR OMA; NDNVMRR; -.
DR PhylomeDB; Q10133; -.
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:Q10133; -.
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:0035841; C:new growing cell tip; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035840; C:old growing cell tip; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:PomBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; 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:0070610; P:regulation of fungal-type cell wall (1->3)-alpha-glucan biosynthetic process; IGI: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 membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..197
FT /note="GTP-binding protein rho2"
FT /id="PRO_0000198941"
FT PROPEP 198..200
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281271"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 197
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 197
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 200 AA; 22253 MW; 9200015082FC5EA2 CRC64;
MLQSQPIRRK LVVVGDGACG KTSLLSVFTL GYFPTEYVPT VFENYVSDCR VDGKSVQLAL
WDTAGQEEYE RLRPMSYAKA HIILVGFAID SPDSLENVST KWIEEINTLC PNVPFILVGM
KADLRSDPVA IEEMRRRNQN FVKSQQAELV AQRIGARKYM ECSSLTGDGV DDVFEAATRA
ALTVRDSEND KSSTKCCIIS
