RAC7_ARATH
ID RAC7_ARATH Reviewed; 209 AA.
AC O82480;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Rac-like GTP-binding protein ARAC7;
DE AltName: Full=GTPase protein ROP9;
GN Name=ARAC7; Synonyms=ROP9; OrderedLocusNames=At4g28950; ORFNames=F25O24.70;
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;
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=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 [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 PALMITOYLATION AT CYS-196; CYS-203 AND CYS-206, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-196; CYS-203 AND CYS-206.
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 [5]
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).
CC -!- FUNCTION: Acts as a negative regulator of abscisic acid (ABA)
CC responses. {ECO:0000269|PubMed:12417701}.
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-206, rather than prenylated. {ECO:0000269|PubMed:12368496}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AF079484; AAC63013.1; -; mRNA.
DR EMBL; AF115474; AAF40246.1; -; Genomic_DNA.
DR EMBL; AL078469; CAB43909.1; -; Genomic_DNA.
DR EMBL; AL161574; CAB79653.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85566.1; -; Genomic_DNA.
DR PIR; T08950; T08950.
DR RefSeq; NP_194624.1; NM_119039.3.
DR PDB; 2J0V; X-ray; 1.78 A; A/B/C/D=1-209.
DR PDBsum; 2J0V; -.
DR AlphaFoldDB; O82480; -.
DR SMR; O82480; -.
DR STRING; 3702.AT4G28950.1; -.
DR PaxDb; O82480; -.
DR PRIDE; O82480; -.
DR ProteomicsDB; 236691; -.
DR EnsemblPlants; AT4G28950.1; AT4G28950.1; AT4G28950.
DR GeneID; 829016; -.
DR Gramene; AT4G28950.1; AT4G28950.1; AT4G28950.
DR KEGG; ath:AT4G28950; -.
DR Araport; AT4G28950; -.
DR TAIR; locus:2123548; AT4G28950.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; O82480; -.
DR OMA; ITHHQQK; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; O82480; -.
DR EvolutionaryTrace; O82480; -.
DR PRO; PR:O82480; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O82480; baseline and differential.
DR Genevisible; O82480; 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: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; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
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; Abscisic acid signaling pathway; GTP-binding; Lipoprotein;
KW Membrane; Nucleotide-binding; Palmitate; Reference proteome.
FT CHAIN 1..209
FT /note="Rac-like GTP-binding protein ARAC7"
FT /id="PRO_0000198921"
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 LIPID 196
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:12368496"
FT LIPID 203
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:12368496"
FT LIPID 206
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:12368496"
FT MUTAGEN 196
FT /note="C->S: Affects the membrane location."
FT /evidence="ECO:0000269|PubMed:12368496"
FT MUTAGEN 203
FT /note="C->S: Affects the membrane location."
FT /evidence="ECO:0000269|PubMed:12368496"
FT MUTAGEN 206
FT /note="C->S: Affects the membrane location."
FT /evidence="ECO:0000269|PubMed:12368496"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:2J0V"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:2J0V"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2J0V"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:2J0V"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2J0V"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:2J0V"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:2J0V"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:2J0V"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2J0V"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:2J0V"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:2J0V"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:2J0V"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:2J0V"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:2J0V"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:2J0V"
SQ SEQUENCE 209 AA; 23043 MW; FA0087A6A7650CB5 CRC64;
MSASKFIKCV TVGDGAVGKT CMLICYTSNK FPTDYIPTVF DNFSANVAVD GQIVNLGLWD
TAGQEDYSRL RPLSYRGADI FVLAFSLISK ASYENVLKKW MPELRRFAPN VPIVLVGTKL
DLRDDKGYLA DHTNVITSTQ GEELRKQIGA AAYIECSSKT QQNVKAVFDT AIKVVLQPPR
RKEVPRRRKN HRRSGCSIAS IVCGGCTAA
