RAC2_ARATH
ID RAC2_ARATH Reviewed; 201 AA.
AC Q38903;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Rac-like GTP-binding protein ARAC2;
DE AltName: Full=GTPase protein ROP7;
DE Flags: Precursor;
GN Name=ARAC2; Synonyms=ROP7; OrderedLocusNames=At5g45970; ORFNames=MCL19.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9349271; DOI=10.1023/a:1005804508902;
RA Winge P., Brembu T., Bones A.M.;
RT "Cloning and characterization of rac-like cDNAs from Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 35:483-495(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11102387; DOI=10.1093/genetics/156.4.1959;
RA Winge P., Brembu T., Kristensen R., Bones A.M.;
RT "Genetic structure and evolution of RAC-GTPases in Arabidopsis thaliana.";
RL Genetics 156:1959-1971(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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 -!- TISSUE SPECIFICITY: Expressed exclusively in the root, hypocotyl and
CC stem.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; U43026; AAC49852.1; -; mRNA.
DR EMBL; AF115469; AAF40241.1; -; Genomic_DNA.
DR EMBL; AB006698; BAB08242.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95321.1; -; Genomic_DNA.
DR PIR; T48862; T48862.
DR RefSeq; NP_199409.1; NM_123965.2.
DR PDB; 2WBL; X-ray; 2.90 A; C/D=1-180.
DR PDBsum; 2WBL; -.
DR AlphaFoldDB; Q38903; -.
DR SMR; Q38903; -.
DR BioGRID; 19886; 3.
DR IntAct; Q38903; 1.
DR STRING; 3702.AT5G45970.1; -.
DR PaxDb; Q38903; -.
DR PRIDE; Q38903; -.
DR ProteomicsDB; 236451; -.
DR EnsemblPlants; AT5G45970.1; AT5G45970.1; AT5G45970.
DR GeneID; 834637; -.
DR Gramene; AT5G45970.1; AT5G45970.1; AT5G45970.
DR KEGG; ath:AT5G45970; -.
DR Araport; AT5G45970; -.
DR TAIR; locus:2161343; AT5G45970.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q38903; -.
DR OMA; SSHKMCT; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q38903; -.
DR EvolutionaryTrace; Q38903; -.
DR PRO; PR:Q38903; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38903; baseline and differential.
DR Genevisible; Q38903; AT.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
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:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
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: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 3D-structure; Cytoplasm; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..198
FT /note="Rac-like GTP-binding protein ARAC2"
FT /id="PRO_0000198916"
FT PROPEP 199..201
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000227581"
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 198
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 198
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:2WBL"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:2WBL"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:2WBL"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:2WBL"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2WBL"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:2WBL"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2WBL"
FT TURN 120..124
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:2WBL"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2WBL"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:2WBL"
SQ SEQUENCE 201 AA; 22393 MW; B3E73F55BDBB8028 CRC64;
MSTARFIKCV TVGDGAVGKT CMLISYTSNT FPTDYVPTVF DNFSANVVVD GSTVNLGLWD
TAGQEDYNRL RPLSYRGADV FLLAFSLISK ASYENIHKKW LPELKHYAPG IPIVLVGTKL
DLRDDKQFLK DHPGAASITT AQGEELRKMI GAVRYLECSS KTQQNVKAVF DTAIRVALRP
PKAKKKIKPL KTKRSRICFF L
