RHO1_SCHPO
ID RHO1_SCHPO Reviewed; 202 AA.
AC Q09914;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=GTP-binding protein rho1;
DE Flags: Precursor;
GN Name=rho1; ORFNames=SPAC1F7.04;
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 [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=9372443; DOI=10.1242/jcs.110.20.2547;
RA Arellano M., Duran A., Perez P.;
RT "Localisation of the Schizosaccharomyces pombe rho1p GTPase and its
RT involvement in the organisation of the actin cytoskeleton.";
RL J. Cell Sci. 110:2547-2555(1997).
CC -!- FUNCTION: Involved in the regulation of cell wall growth and actin
CC cytoskeleton organization. Activates (1,3)-beta-D-glucan synthase.
CC {ECO:0000269|PubMed:9372443}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9372443};
CC Lipid-anchor {ECO:0000269|PubMed:9372443}. 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; D38180; BAA07377.1; -; mRNA.
DR EMBL; CU329670; CAA91951.1; -; Genomic_DNA.
DR PIR; JC4044; JC4044.
DR RefSeq; NP_594490.1; NM_001019919.2.
DR AlphaFoldDB; Q09914; -.
DR SMR; Q09914; -.
DR BioGRID; 278109; 40.
DR IntAct; Q09914; 1.
DR STRING; 4896.SPAC1F7.04.1; -.
DR MaxQB; Q09914; -.
DR PaxDb; Q09914; -.
DR PRIDE; Q09914; -.
DR EnsemblFungi; SPAC1F7.04.1; SPAC1F7.04.1:pep; SPAC1F7.04.
DR GeneID; 2541612; -.
DR KEGG; spo:SPAC1F7.04; -.
DR PomBase; SPAC1F7.04; rho1.
DR VEuPathDB; FungiDB:SPAC1F7.04; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q09914; -.
DR OMA; APEVNHY; -.
DR PhylomeDB; Q09914; -.
DR Reactome; R-SPO-198203; PI3K/AKT activation.
DR Reactome; R-SPO-392451; G beta:gamma signalling through PI3Kgamma.
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-8980692; RHOA GTPase cycle.
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:Q09914; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0098753; C:anchored component of the cytoplasmic side of the plasma membrane; NAS:PomBase.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:1902716; C:cell cortex of growing cell tip; 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:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0035838; C:growing cell tip; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0140453; C:protein aggregate center; 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:0035591; F:signaling adaptor activity; IPI:PomBase.
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:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0060635; P:positive regulation of (1->3)-beta-D-glucan biosynthetic process; IMP:PomBase.
DR GO; GO:1905758; P:positive regulation of primary cell septum biogenesis; IMP:PomBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0090334; P:regulation of cell wall (1->3)-beta-D-glucan biosynthetic process; TAS:PomBase.
DR GO; GO:0032955; P:regulation of division septum assembly; IMP:PomBase.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:PomBase.
DR GO; GO:2000769; P:regulation of establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0070610; P:regulation of fungal-type cell wall (1->3)-alpha-glucan biosynthetic process; IMP:PomBase.
DR GO; GO:0032995; P:regulation of fungal-type cell wall biogenesis; IGI:PomBase.
DR GO; GO:1903471; P:regulation of mitotic actomyosin contractile ring contraction; 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 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..199
FT /note="GTP-binding protein rho1"
FT /id="PRO_0000198940"
FT PROPEP 200..202
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281270"
FT MOTIF 35..43
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 199
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 199
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 202 AA; 22523 MW; 21B625E0B9098CB1 CRC64;
MATELRRKLV IVGDGACGKT CLLIVFSKGT FPEVYVPTVF ENYVADVEVD GRHVELALWD
TAGQEDYDRL RPLSYPDSHV ILICFAVDSP DSLDNVQEKW ISEVLHFCSS LPILLVACKA
DLRNDPKIIE ELSKTNQHPV TTEEGQAVAQ KIGAYKYLEC SAKTNEGVRE VFESATRAAM
LKHKPKVKPS SGTKKKKRCI LL
