RAC3_ARATH
ID RAC3_ARATH Reviewed; 198 AA.
AC Q38912; P92989; Q84W42;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Rac-like GTP-binding protein ARAC3 {ECO:0000303|PubMed:9349271};
DE Short=AtRAC1 {ECO:0000303|PubMed:11102387};
DE AltName: Full=GTPase protein ROP6 {ECO:0000303|PubMed:10798620};
DE Flags: Precursor;
GN Name=ARAC3 {ECO:0000303|PubMed:9349271};
GN Synonyms=RAC1 {ECO:0000303|PubMed:11102387},
GN ROP6 {ECO:0000303|PubMed:10798620};
GN OrderedLocusNames=At4g35020 {ECO:0000312|Araport:AT4G35020};
GN ORFNames=M4E13.80 {ECO:0000312|EMBL:CAA17767.1};
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].
RX PubMed=8893552; DOI=10.1046/j.1365-313x.1996.10040761.x;
RA Xia G., Ramachandran S., Hong Y., Chan Y.-S., Simanis V., Chua N.-H.;
RT "Identification of plant cytoskeletal, cell cycle-related and polarity-
RT related proteins using Schizosaccharomyces pombe.";
RL Plant J. 10:761-769(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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RHO GDI-1.
RX PubMed=10798620; DOI=10.1023/a:1006341210147;
RA Bischoff F., Vahlkamp L., Molendijk A.J., Palme K.;
RT "Localization of AtROP4 and AtROP6 and interaction with the guanine
RT nucleotide dissociation inhibitor AtRhoGDI1 from Arabidopsis.";
RL Plant Mol. Biol. 42:515-530(2000).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11387211; DOI=10.1093/emboj/20.11.2779;
RA Molendijk A.J., Bischoff F., Rajendrakumar C.S.V., Friml J., Braun M.,
RA Gilroy S., Palme K.;
RT "Arabidopsis thaliana Rop GTPases are localized to tips of root hairs and
RT control polar growth.";
RL EMBO J. 20:2779-2788(2001).
RN [10]
RP INTERACTION WITH ICR1.
RX PubMed=17493810; DOI=10.1016/j.cub.2007.04.038;
RA Lavy M., Bloch D., Hazak O., Gutman I., Poraty L., Sorek N., Sternberg H.,
RA Yalovsky S.;
RT "A Novel ROP/RAC effector links cell polarity, root-meristem maintenance,
RT and vesicle trafficking.";
RL Curr. Biol. 17:947-952(2007).
RN [11]
RP RETRACTED PAPER.
RX PubMed=17242203; DOI=10.1128/mcb.02347-06;
RA Sorek N., Poraty L., Sternberg H., Bar E., Lewinsohn E., Yalovsky S.;
RT "Activation status-coupled transient S acylation determines membrane
RT partitioning of a plant Rho-related GTPase.";
RL Mol. Cell. Biol. 27:2144-2154(2007).
RN [12]
RP RETRACTION NOTICE OF PUBMED:17242203.
RX PubMed=28754775; DOI=10.1128/mcb.00321-17;
RA Sorek N., Poraty L., Sternberg H., Bar E., Lewinsohn E., Yalovsky S.;
RL Mol. Cell. Biol. 37:0-0(2017).
RN [13]
RP FUNCTION, AND INTERACTION WITH SPK1.
RX PubMed=22683260; DOI=10.1016/j.cub.2012.05.019;
RA Lin D., Nagawa S., Chen J., Cao L., Chen X., Xu T., Li H., Dhonukshe P.,
RA Yamamuro C., Friml J., Scheres B., Fu Y., Yang Z.;
RT "A ROP GTPase-dependent auxin signaling pathway regulates the subcellular
RT distribution of PIN2 in Arabidopsis roots.";
RL Curr. Biol. 22:1319-1325(2012).
RN [14]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27251533; DOI=10.1038/nplants.2015.162;
RA Stanislas T., Hueser A., Barbosa I.C.R., Kiefer C.S., Brackmann K.,
RA Pietra S., Gustavsson A., Zourelidou M., Schwechheimer C., Grebe M.;
RT "Arabidopsis D6PK is a lipid domain-dependent mediator of root epidermal
RT planar polarity.";
RL Nat. Plants 1:15162-15162(2015).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=30770391; DOI=10.1242/dev.168559;
RA Gendre D., Baral A., Dang X., Esnay N., Boutte Y., Stanislas T., Vain T.,
RA Claverol S., Gustavsson A., Lin D., Grebe M., Bhalerao R.P.;
RT "Rho-of-plant activated root hair formation requires Arabidopsis YIP4a/b
RT gene function.";
RL Development 146:0-0(2019).
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. Involved in cell polarity control during the actin-
CC dependent tip growth of root hairs, thus regulating root hair length
CC and root hair initiation (PubMed:11387211, PubMed:30770391). SPK1-
CC dependent activation is required for auxin-mediated inhibition of PIN2
CC internalization during gravitropic responses (PubMed:22683260).
CC {ECO:0000269|PubMed:11387211, ECO:0000269|PubMed:22683260,
CC ECO:0000269|PubMed:30770391}.
CC -!- SUBUNIT: Interacts with Rho GDP-dissociation inhibitor 1 and ICR1
CC (PubMed:10798620, PubMed:17493810). Binds to SPK1 when in the inactive
CC GDP-bound form (PubMed:22683260). {ECO:0000269|PubMed:10798620,
CC ECO:0000269|PubMed:17493810, ECO:0000269|PubMed:22683260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q38937}. Cell
CC membrane {ECO:0000269|PubMed:10798620, ECO:0000269|PubMed:27251533};
CC Peripheral membrane protein {ECO:0000255}. Note=The localization to the
CC plasma membrane requires YIP4A and YIP4B (By similarity). Accumulates
CC in a sterol-enriched, polar membrane domain during root hair initiation
CC (PubMed:27251533). {ECO:0000250|UniProtKB:Q38919,
CC ECO:0000269|PubMed:27251533}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed at the tip of
CC root hairs. {ECO:0000269|PubMed:11387211, ECO:0000269|PubMed:9765526}.
CC -!- DEVELOPMENTAL STAGE: In root trichoblasts, accumulates into patches at
CC the basal end of the cell before a hair bulge is visible and remain
CC concentrated at the tip of the bulge and in the growing hair.
CC {ECO:0000269|PubMed:30770391}.
CC -!- DISRUPTION PHENOTYPE: Fewer and shorter root hairs.
CC {ECO:0000269|PubMed:30770391}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC -!- CAUTION: An article reported S-acylation of Cys residues that regulates
CC localization to membranes; however, this paper was later retracted.
CC {ECO:0000305|PubMed:17242203, ECO:0000305|PubMed:28754775}.
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DR EMBL; U62746; AAB38780.1; -; mRNA.
DR EMBL; U43501; AAC49853.1; -; Genomic_DNA.
DR EMBL; AF031427; AAC78241.1; -; mRNA.
DR EMBL; AF115470; AAF40242.1; -; Genomic_DNA.
DR EMBL; AL022023; CAA17767.1; -; Genomic_DNA.
DR EMBL; AL161586; CAB80219.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86447.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86448.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86449.1; -; Genomic_DNA.
DR EMBL; BT004252; AAO42256.1; -; mRNA.
DR PIR; T05772; T05772.
DR RefSeq; NP_001190916.1; NM_001203987.1.
DR RefSeq; NP_001190917.1; NM_001203988.2.
DR RefSeq; NP_195228.1; NM_119668.6.
DR AlphaFoldDB; Q38912; -.
DR SMR; Q38912; -.
DR BioGRID; 14936; 9.
DR DIP; DIP-29822N; -.
DR IntAct; Q38912; 2.
DR STRING; 3702.AT4G35020.2; -.
DR SwissPalm; Q38912; -.
DR PaxDb; Q38912; -.
DR PRIDE; Q38912; -.
DR ProteomicsDB; 236297; -.
DR EnsemblPlants; AT4G35020.1; AT4G35020.1; AT4G35020.
DR EnsemblPlants; AT4G35020.2; AT4G35020.2; AT4G35020.
DR EnsemblPlants; AT4G35020.3; AT4G35020.3; AT4G35020.
DR GeneID; 829654; -.
DR Gramene; AT4G35020.1; AT4G35020.1; AT4G35020.
DR Gramene; AT4G35020.2; AT4G35020.2; AT4G35020.
DR Gramene; AT4G35020.3; AT4G35020.3; AT4G35020.
DR KEGG; ath:AT4G35020; -.
DR Araport; AT4G35020; -.
DR TAIR; locus:2131606; AT4G35020.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q38912; -.
DR OMA; ENVYTKW; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q38912; -.
DR BioCyc; ARA:AT4G35020-MON; -.
DR PRO; PR:Q38912; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38912; baseline and differential.
DR Genevisible; Q38912; 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:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030427; C:site of polarized growth; IDA:TAIR.
DR GO; GO:0005819; C:spindle; HDA:TAIR.
DR GO; GO:0019003; F:GDP binding; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IDA:TAIR.
DR GO; GO:0003924; F:GTPase activity; IDA:TAIR.
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:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
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:0009958; P:positive gravitropism; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0010928; P:regulation of auxin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0048767; P:root hair elongation; IMP:UniProtKB.
DR GO; GO:0048766; P:root hair initiation; IMP:UniProtKB.
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 Auxin signaling pathway; Cell membrane; Cytoplasm; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Palmitate;
KW Prenylation; Reference proteome.
FT CHAIN 1..195
FT /note="Rac-like GTP-binding protein ARAC3"
FT /id="PRO_0000198917"
FT PROPEP 196..198
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000227582"
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|UniProtKB:P61586"
FT BINDING 16..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 31..38
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT MOD_RES 195
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 158
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 195
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT CONFLICT 124
FT /note="D -> H (in Ref. 1; AAB38780)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="V -> M (in Ref. 7; AAO42256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21728 MW; 154A01D1AAE3A766 CRC64;
MSASRFIKCV TVGDGAVGKT CLLISYTSNT FPTDYVPTVF DNFSANVIVD GNTINLGLWD
TAGQEDYNRL RPLSYRGADV FLLAFSLVSK ASYENVSKKW VPELRHYAPG VPIILVGTKL
DLRDDKQFFA EHPGAVPIST AQGEELKKLI GAPAYIECSA KTQQNVKAVF DAAIKVVLQP
PKNKKKKKRK SQKGCSIL
