RAC1_ARATH
ID RAC1_ARATH Reviewed; 197 AA.
AC Q38902;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Rac-like GTP-binding protein ARAC1;
DE AltName: Full=GTPase protein ROP3;
DE Flags: Precursor;
GN Name=ARAC1; Synonyms=ATGP2, ROP3; OrderedLocusNames=At2g17800;
GN ORFNames=T17A5.14;
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].
RX PubMed=8843944; DOI=10.1007/bf00040720;
RA Biermann B.J., Randall S.K., Crowell D.N.;
RT "Identification and isoprenylation of plant GTP-binding proteins.";
RL Plant Mol. Biol. 31:1021-1028(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=9765526; DOI=10.1104/pp.118.2.407;
RA Li H., Wu G., Ware D., Davis K.R., Yang Z.;
RT "Arabidopsis Rho-related GTPases: differential gene expression in pollen
RT and polar localization in fission yeast.";
RL Plant Physiol. 118:407-417(1998).
RN [8]
RP INTERACTION WITH SPK1.
RC STRAIN=cv. Columbia;
RX PubMed=18308939; DOI=10.1073/pnas.0710294105;
RA Basu D., Le J., Zakharova T., Mallery E.L., Szymanski D.B.;
RT "A SPIKE1 signaling complex controls actin-dependent cell morphogenesis
RT through the heteromeric WAVE and ARP2/3 complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4044-4049(2008).
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 -!- SUBUNIT: Interacts with SPK1. {ECO:0000269|PubMed:18308939}.
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: Ubiquitous. {ECO:0000269|PubMed:9765526}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; U64919; AAD00113.1; -; mRNA.
DR EMBL; U41295; AAC49851.1; -; mRNA.
DR EMBL; AF115466; AAF40237.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06689.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06690.1; -; Genomic_DNA.
DR EMBL; AY093046; AAM13045.1; -; mRNA.
DR EMBL; BT000393; AAN15712.1; -; mRNA.
DR PIR; T08857; T08857.
DR RefSeq; NP_001077910.1; NM_001084441.2.
DR RefSeq; NP_179371.1; NM_127334.4.
DR AlphaFoldDB; Q38902; -.
DR SMR; Q38902; -.
DR BioGRID; 1647; 5.
DR DIP; DIP-29819N; -.
DR IntAct; Q38902; 3.
DR STRING; 3702.AT2G17800.1; -.
DR PaxDb; Q38902; -.
DR PRIDE; Q38902; -.
DR ProteomicsDB; 236448; -.
DR EnsemblPlants; AT2G17800.1; AT2G17800.1; AT2G17800.
DR EnsemblPlants; AT2G17800.2; AT2G17800.2; AT2G17800.
DR GeneID; 816290; -.
DR Gramene; AT2G17800.1; AT2G17800.1; AT2G17800.
DR Gramene; AT2G17800.2; AT2G17800.2; AT2G17800.
DR KEGG; ath:AT2G17800; -.
DR Araport; AT2G17800; -.
DR TAIR; locus:2827916; AT2G17800.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q38902; -.
DR OMA; LICYSIM; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q38902; -.
DR PRO; PR:Q38902; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38902; baseline and differential.
DR Genevisible; Q38902; AT.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
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; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005819; C:spindle; HDA: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:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
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 Cytoplasm; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..194
FT /note="Rac-like GTP-binding protein ARAC1"
FT /id="PRO_0000198915"
FT PROPEP 195..197
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000227580"
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; 21530 MW; C566CFC0C4390632 CRC64;
MSASRFIKCV TVGDGAVGKT CLLISYTSNT FPTDYVPTVF DNFSANVVVN GATVNLGLWD
TAGQEDYNRL RPLSYRGADV FILAFSLISK ASYENVSKKW IPELKHYAPG VPIVLVGTKL
DLRDDKQFFI DHPGAVPITT AQGEELKKLI GAPAYIECSS KTQENVKGVF DAAIRVVLQP
PKQKKKKSKA QKACSIL
