RAC6_ARATH
ID RAC6_ARATH Reviewed; 197 AA.
AC Q9SBJ6; O65632;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Rac-like GTP-binding protein ARAC6;
DE AltName: Full=GTPase protein ROP5;
DE Flags: Precursor;
GN Name=ARAC6; Synonyms=RAC2, ROP5; OrderedLocusNames=At4g35950;
GN ORFNames=F4B14_220, T19K4.80;
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], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10209027; DOI=10.1083/jcb.145.2.317;
RA Kost B., Lemichez E., Spielhofer P., Hong Y., Tolias K., Carpenter C.,
RA Chua N.-H.;
RT "Rac homologues and compartmentalized phosphatidylinositol 4, 5-
RT bisphosphate act in a common pathway to regulate polar pollen tube
RT growth.";
RL J. Cell Biol. 145:317-330(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia, and 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=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 [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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99, FUNCTION, AND TISSUE
RP 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 [9]
RP INTERACTION WITH SPK1.
RX PubMed=17267444; DOI=10.1242/dev.02792;
RA Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M.,
RA Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.;
RT "The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell
RT morphogenesis.";
RL Development 134:967-977(2007).
RN [10]
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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 1-180 IN COMPLEX WITH GDP.
RA Thomas C., Berken A.;
RT "Crystal structure of the plant Rho protein ROP5.";
RL Submitted (JAN-2008) to the PDB data bank.
CC -!- FUNCTION: May be involved in cell polarity control during the actin-
CC dependent tip growth of pollen tubes. {ECO:0000269|PubMed:10209027,
CC ECO:0000269|PubMed:9765526}.
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:17267444,
CC ECO:0000269|PubMed:18308939}.
CC -!- INTERACTION:
CC Q9SBJ6; Q8SAB7: SPK1; NbExp=2; IntAct=EBI-1548024, EBI-1547917;
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. Preferentially expressed in mature
CC pollen and pollen tubes. {ECO:0000269|PubMed:10209027,
CC ECO:0000269|PubMed:9765526}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AF107663; AAD17999.1; -; mRNA.
DR EMBL; AF079487; AAC29480.1; -; mRNA.
DR EMBL; AF115473; AAF40245.1; -; Genomic_DNA.
DR EMBL; AL022373; CAA18489.1; -; Genomic_DNA.
DR EMBL; AL031986; CAA21481.1; -; Genomic_DNA.
DR EMBL; AL161588; CAB81504.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86595.1; -; Genomic_DNA.
DR EMBL; AK117209; BAC41885.1; -; mRNA.
DR EMBL; BT005217; AAO63281.1; -; mRNA.
DR EMBL; AY087336; AAM64886.1; -; mRNA.
DR EMBL; AF031429; AAB87673.1; -; Genomic_DNA.
DR PIR; T04705; T04705.
DR RefSeq; NP_195320.1; NM_119762.4.
DR PDB; 3BWD; X-ray; 1.53 A; D=1-180.
DR PDBsum; 3BWD; -.
DR AlphaFoldDB; Q9SBJ6; -.
DR SMR; Q9SBJ6; -.
DR BioGRID; 15032; 29.
DR DIP; DIP-29821N; -.
DR IntAct; Q9SBJ6; 6.
DR STRING; 3702.AT4G35950.1; -.
DR PaxDb; Q9SBJ6; -.
DR PRIDE; Q9SBJ6; -.
DR ProteomicsDB; 236398; -.
DR EnsemblPlants; AT4G35950.1; AT4G35950.1; AT4G35950.
DR GeneID; 829750; -.
DR Gramene; AT4G35950.1; AT4G35950.1; AT4G35950.
DR KEGG; ath:AT4G35950; -.
DR Araport; AT4G35950; -.
DR TAIR; locus:2125399; AT4G35950.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q9SBJ6; -.
DR OMA; PWARPAC; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q9SBJ6; -.
DR EvolutionaryTrace; Q9SBJ6; -.
DR PRO; PR:Q9SBJ6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SBJ6; baseline and differential.
DR Genevisible; Q9SBJ6; 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:0005886; C:plasma membrane; IBA:GO_Central.
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..194
FT /note="Rac-like GTP-binding protein ARAC6"
FT /id="PRO_0000198920"
FT PROPEP 195..197
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000227585"
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:0007744|PDB:3BWD"
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:0007744|PDB:3BWD"
FT BINDING 160
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:3BWD"
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"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:3BWD"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:3BWD"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3BWD"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:3BWD"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:3BWD"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:3BWD"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:3BWD"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:3BWD"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3BWD"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:3BWD"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:3BWD"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:3BWD"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3BWD"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:3BWD"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:3BWD"
SQ SEQUENCE 197 AA; 21571 MW; D26BE6D3827C1632 CRC64;
MSASRFIKCV TVGDGAVGKT CLLISYTSNT FPTDYVPTVF DNFSANVVVN GATVNLGLWD
TAGQEDYNRL RPLSYRGADV FILAFSLISK ASYENVSKKW IPELKHYAPG VPIVLVGTKL
DLRDDKQFFI DHPGAVPITT VQGEELKKLI GAPAYIECSS KSQENVKGVF DAAIRVVLQP
PKQKKKKNKA QKACSIL
