RAC8_ARATH
ID RAC8_ARATH Reviewed; 208 AA.
AC Q9SU67; O82482;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Rac-like GTP-binding protein ARAC8;
DE AltName: Full=GTPase protein ROP10;
GN Name=ARAC8; Synonyms=ROP10; OrderedLocusNames=At3g48040;
GN ORFNames=T17F15.90;
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, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
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 [6]
RP PALMITOYLATION AT CYS-199 AND CYS-205, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-199 AND CYS-205.
RX PubMed=12368496; DOI=10.1105/tpc.005561;
RA Lavy M., Bracha-Drori K., Sternberg H., Yalovsky S.;
RT "A cell-specific, prenylation-independent mechanism regulates targeting of
RT type II RACs.";
RL Plant Cell 14:2431-2450(2002).
RN [7]
RP FUNCTION.
RX PubMed=12417701; DOI=10.1105/tpc.005611;
RA Zheng Z.-L., Nafisi M., Tam A., Li H., Crowell D.N., Chary S.N.,
RA Schroeder J.I., Shen J., Yang Z.;
RT "Plasma membrane-associated ROP10 small GTPase is a specific negative
RT regulator of abscisic acid responses in Arabidopsis.";
RL Plant Cell 14:2787-2797(2002).
RN [8]
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 [9]
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: Acts as a negative regulator of abscisic acid (ABA)
CC responses. {ECO:0000269|PubMed:12417701}.
CC -!- SUBUNIT: Interacts with ICR1 (PubMed:17493810). Binds to SPK1
CC (PubMed:18308939). {ECO:0000269|PubMed:17493810,
CC ECO:0000269|PubMed:18308939}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12368496}; Lipid-
CC anchor {ECO:0000269|PubMed:12368496}.
CC -!- PTM: Although this sequence has a C-terminal -CXXX, it is palmitoylated
CC at Cys-205, rather than prenylated. {ECO:0000269|PubMed:12368496}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41135.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF079486; AAC63015.1; -; mRNA.
DR EMBL; AF115475; AAF40247.1; -; Genomic_DNA.
DR EMBL; AL049658; CAB41135.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78359.1; -; Genomic_DNA.
DR EMBL; AK117324; BAC41995.1; -; mRNA.
DR EMBL; BT005228; AAO63292.1; -; mRNA.
DR PIR; T06679; T06679.
DR PIR; T48860; T48860.
DR RefSeq; NP_566897.1; NM_114673.3.
DR AlphaFoldDB; Q9SU67; -.
DR SMR; Q9SU67; -.
DR BioGRID; 9278; 29.
DR DIP; DIP-29823N; -.
DR IntAct; Q9SU67; 30.
DR STRING; 3702.AT3G48040.1; -.
DR SwissPalm; Q9SU67; -.
DR PaxDb; Q9SU67; -.
DR PRIDE; Q9SU67; -.
DR ProteomicsDB; 236399; -.
DR EnsemblPlants; AT3G48040.1; AT3G48040.1; AT3G48040.
DR GeneID; 823959; -.
DR Gramene; AT3G48040.1; AT3G48040.1; AT3G48040.
DR KEGG; ath:AT3G48040; -.
DR Araport; AT3G48040; -.
DR TAIR; locus:2097905; AT3G48040.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q9SU67; -.
DR OMA; RIMHTRR; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q9SU67; -.
DR PRO; PR:Q9SU67; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SU67; baseline and differential.
DR Genevisible; Q9SU67; 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:0005829; C:cytosol; HDA:TAIR.
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; ISS:TAIR.
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: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:0009788; P:negative regulation of abscisic acid-activated signaling pathway; TAS:TAIR.
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 Abscisic acid signaling pathway; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Palmitate; Reference proteome.
FT CHAIN 1..208
FT /note="Rac-like GTP-binding protein ARAC8"
FT /id="PRO_0000198922"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 199
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12368496"
FT LIPID 205
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12368496"
FT MUTAGEN 199
FT /note="C->S: Affects the membrane location."
FT /evidence="ECO:0000269|PubMed:12368496"
FT MUTAGEN 205
FT /note="C->S: Affects the membrane location."
FT /evidence="ECO:0000269|PubMed:12368496"
SQ SEQUENCE 208 AA; 23069 MW; 4029C5063A936CD4 CRC64;
MASSASKFIK CVTVGDGAVG KTCMLICYTS NKFPTDYIPT VFDNFSVNVV VEGITVNLGL
WDTAGQEDYN RLRPLSYRGA DVFVLAFSLI SRASYENVFK KWIPELQHFA PGVPIVLVGT
KMDLREDRHY LSDHPGLSPV TTSQGEELRK HIGATYYIEC SSKTQQNVKA VFDAAIKVVI
KPAVKQKEKK KKQKPRSGCL SNILCGKN
