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 02-NOV-2016, entry version 119. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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; RA Winge P., Brembu T., Kristensen R., Bones A.M.; RT "Genetic structure and evolution of RAC-GTPases in Arabidopsis RT 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., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA 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., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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., RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., RA Shibata K., 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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 RT pollen 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 RT morphogenesis 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 CC actin-dependent tip growth of pollen tubes. CC {ECO:0000269|PubMed:10209027, ECO:0000269|PubMed:9765526}. CC -!- FUNCTION: Inactive GDP-bound Rho GTPases reside in the cytosol, CC are found in a complex with Rho GDP-dissociation inhibitors (Rho CC GDIs), and are released from the GDI protein in order to CC translocate to membranes upon activation. {ECO:0000250}. CC -!- SUBUNIT: Interacts with SPK1. {ECO:0000269|PubMed:17267444, CC ECO:0000269|PubMed:18308939}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. CC Note=Associated with the 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_119762.3. DR UniGene; At.2216; -. DR PDB; 3BWD; X-ray; 1.53 A; D=1-180. DR PDBsum; 3BWD; -. DR ProteinModelPortal; Q9SBJ6; -. DR SMR; Q9SBJ6; -. DR BioGrid; 15032; 29. DR DIP; DIP-29821N; -. DR IntAct; Q9SBJ6; 5. DR STRING; 3702.AT4G35950.1; -. DR PaxDb; Q9SBJ6; -. DR EnsemblPlants; AT4G35950.1; AT4G35950.1; AT4G35950. DR GeneID; 829750; -. DR Gramene; AT4G35950.1; AT4G35950.1; AT4G35950. DR KEGG; ath:AT4G35950; -. DR TAIR; AT4G35950; -. DR eggNOG; KOG0393; Eukaryota. DR eggNOG; COG1100; LUCA. DR HOGENOM; HOG000233974; -. DR InParanoid; Q9SBJ6; -. DR KO; K04392; -. DR OMA; FENYNSS; -. DR OrthoDB; EOG09360LB1; -. DR PhylomeDB; Q9SBJ6; -. DR Reactome; R-ATH-194840; Rho GTPase cycle. DR Reactome; R-ATH-198203; PI3K/AKT activation. DR Reactome; R-ATH-392451; G beta:gamma signalling through PI3Kgamma. DR Reactome; R-ATH-5666185; RHO GTPases Activate Rhotekin and Rhophilins. DR Reactome; R-ATH-5689896; Ovarian tumor domain proteases. DR EvolutionaryTrace; Q9SBJ6; -. DR PRO; PR:Q9SBJ6; -. DR Proteomes; UP000006548; Chromosome 4. DR Genevisible; Q9SBJ6; AT. DR GO; GO:0005737; C:cytoplasm; IDA:TAIR. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. 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 Pfam; PF00071; Ras; 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; Complete proteome; Cytoplasm; GTP-binding; Lipoprotein; KW Membrane; Methylation; Nucleotide-binding; Prenylation; KW Reference proteome. FT CHAIN 1 194 Rac-like GTP-binding protein ARAC6. FT /FTId=PRO_0000198920. FT PROPEP 195 197 Removed in mature form. {ECO:0000255}. FT /FTId=PRO_0000227585. FT NP_BIND 13 20 GTP. {ECO:0000244|PDB:3BWD}. FT NP_BIND 60 64 GTP. {ECO:0000250}. FT NP_BIND 118 121 GTP. {ECO:0000244|PDB:3BWD}. FT MOTIF 35 43 Effector region. {ECO:0000255}. FT COMPBIAS 182 189 Poly-Lys. FT BINDING 160 160 GDP; via amide nitrogen. FT {ECO:0000244|PDB:3BWD}. FT MOD_RES 194 194 Cysteine methyl ester. {ECO:0000255}. FT LIPID 194 194 S-geranylgeranyl cysteine. {ECO:0000255}. FT STRAND 8 12 {ECO:0000244|PDB:3BWD}. FT HELIX 19 28 {ECO:0000244|PDB:3BWD}. FT STRAND 57 59 {ECO:0000244|PDB:3BWD}. FT TURN 66 70 {ECO:0000244|PDB:3BWD}. FT HELIX 71 75 {ECO:0000244|PDB:3BWD}. FT STRAND 79 86 {ECO:0000244|PDB:3BWD}. FT HELIX 90 98 {ECO:0000244|PDB:3BWD}. FT HELIX 100 107 {ECO:0000244|PDB:3BWD}. FT STRAND 113 118 {ECO:0000244|PDB:3BWD}. FT HELIX 120 123 {ECO:0000244|PDB:3BWD}. FT HELIX 126 131 {ECO:0000244|PDB:3BWD}. FT HELIX 140 150 {ECO:0000244|PDB:3BWD}. FT STRAND 153 157 {ECO:0000244|PDB:3BWD}. FT TURN 160 162 {ECO:0000244|PDB:3BWD}. FT HELIX 166 177 {ECO:0000244|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 //