ID   RHO1_PEA                Reviewed;         197 AA.
AC   Q35638;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Rac-like GTP-binding protein RHO1;
DE   AltName: Full=GTPase protein ROP1;
DE   Flags: Precursor;
GN   Name=RHO1;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Alaska;
RX   PubMed=8378356; DOI=10.1073/pnas.90.18.8732;
RA   Yang Z., Watson J.C.;
RT   "Molecular cloning and characterization of rho, a ras-related small GTP-
RT   binding protein from the garden pea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:8732-8736(1993).
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12239385; DOI=10.2307/3870272;
RA   Lin Y., Wang Y., Zhu J.-K., Yang Z.;
RT   "Localization of a Rho GTPase implies a role in tip growth and movement of
RT   the generative cell in pollen tubes.";
RL   Plant Cell 8:293-303(1996).
CC   -!- FUNCTION: Inactive GDP-bound Rho GTPases reside in the cytosol, are
CC       found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and
CC       are released from the GDI protein in order to translocate to membranes
CC       upon activation (By similarity). May be involved in cell polarity
CC       control during the actin-dependent tip growth of pollen tubes.
CC       {ECO:0000250, ECO:0000269|PubMed:12239385}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=Associated with the
CC       membrane when activated.
CC   -!- TISSUE SPECIFICITY: Expressed at the tip of pollen tubes.
CC       {ECO:0000269|PubMed:12239385}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
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DR   EMBL; L19093; AAA96980.1; -; mRNA.
DR   PIR; A47525; A47525.
DR   AlphaFoldDB; Q35638; -.
DR   SMR; Q35638; -.
DR   EnsemblPlants; Psat4g102000.1; Psat4g102000.1.cds; Psat4g102000.
DR   EnsemblPlants; Psat4g102000.2; Psat4g102000.2.cds; Psat4g102000.
DR   EnsemblPlants; Psat4g102000.3; Psat4g102000.3.cds; Psat4g102000.
DR   Gramene; Psat4g102000.1; Psat4g102000.1.cds; Psat4g102000.
DR   Gramene; Psat4g102000.2; Psat4g102000.2.cds; Psat4g102000.
DR   Gramene; Psat4g102000.3; Psat4g102000.3.cds; Psat4g102000.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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   Cytoplasm; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation.
FT   CHAIN           1..194
FT                   /note="Rac-like GTP-binding protein RHO1"
FT                   /id="PRO_0000198931"
FT   PROPEP          195..197
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000227593"
FT   MOTIF           35..43
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
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         194
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           194
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   197 AA;  21630 MW;  A9A511501A7E5969 CRC64;
     MSASRFIKCV TVGDGAVGKT CLLISYTSNT FPTDYVPTVF DNFSANVVVN GSTVNLGLWD
     TAGQEDYNRL RPLSYRGADV FILAFSLISK ASYENVSKKW IPELKHYAPG VPIILVGTKL
     DLRDDKQFFV DHPGAVPITT AQGEELRKLI NAPAYIECSS KSQQNVKAVF DAAIRVVLQP
     PKQKKKKSKA QKACSIL