ID   RAC1_LOTJA              Reviewed;         197 AA.
AC   O04369;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Rac-like GTP-binding protein RAC1;
DE   Flags: Precursor;
GN   Name=RAC1;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
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; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Gifu / B-129; TISSUE=Root nodule;
RX   PubMed=9076991; DOI=10.1046/j.1365-313x.1997.11020237.x;
RA   Borg S., Brandstrup B., Jensen T.J., Poulsen C.;
RT   "Identification of new protein species among 33 different small GTP-binding
RT   proteins encoded by cDNAs from Lotus japonicus, and expression of
RT   corresponding mRNAs in developing root nodules.";
RL   Plant J. 11:237-250(1997).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=Associated with the
CC       membrane when activated.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
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DR   EMBL; Z73961; CAA98189.1; -; mRNA.
DR   AlphaFoldDB; O04369; -.
DR   SMR; O04369; -.
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 RAC1"
FT                   /id="PRO_0000198929"
FT   PROPEP          195..197
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000227591"
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;  21619 MW;  364359A00D061FB6 CRC64;
     MSASRFIKCV TVGDGAVGKT CLLISYTSNT FPTDYVPTVF DNFSANVVVD GSTVNLGLWD
     TAGQEDYNRL RPLSYRGADV FILAFSLISK ASYENIAKKW IPELRHYAPG VPIILVGTKL
     DLRDDKHFLA DHPGAVPITT AQGEELRKLI GAPAYIECSS KTQQNVKAVF DAAIKVVLQP
     PKQKKKKREA QKSCSIL