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Protein

Rac-like GTP-binding protein ARAC7

Gene

ARAC7

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a negative regulator of abscisic acid (ABA) responses.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 208GTPBy similarity
Nucleotide bindingi60 – 645GTPBy similarity
Nucleotide bindingi118 – 1214GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Abscisic acid signaling pathway

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Rac-like GTP-binding protein ARAC7
Alternative name(s):
GTPase protein ROP9
Gene namesi
Name:ARAC7
Synonyms:ROP9
Ordered Locus Names:At4g28950
ORF Names:F25O24.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G28950.

Subcellular locationi

  • Membrane 1 Publication; Lipid-anchor 1 Publication

GO - Cellular componenti

  • intracellular Source: InterPro
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi196 – 1961C → S: Affects the membrane location. 1 Publication
Mutagenesisi203 – 2031C → S: Affects the membrane location. 1 Publication
Mutagenesisi206 – 2061C → S: Affects the membrane location. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 209209Rac-like GTP-binding protein ARAC7PRO_0000198921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi196 – 1961S-palmitoyl cysteine1 Publication
Lipidationi203 – 2031S-palmitoyl cysteine1 Publication
Lipidationi206 – 2061S-palmitoyl cysteine1 Publication

Post-translational modificationi

Although this sequence has a C-terminal -CXXX, it is palmitoylated at Cys-206, rather than prenylated.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiO82480.
PRIDEiO82480.

Expressioni

Gene expression databases

ExpressionAtlasiO82480. baseline and differential.
GenevisibleiO82480. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G28950.1.

Structurei

Secondary structure

1
209
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 149Combined sources
Helixi19 – 2810Combined sources
Beta strandi43 – 486Combined sources
Beta strandi53 – 597Combined sources
Helixi73 – 753Combined sources
Beta strandi79 – 868Combined sources
Helixi90 – 989Combined sources
Helixi100 – 1078Combined sources
Beta strandi113 – 1186Combined sources
Helixi120 – 1234Combined sources
Helixi126 – 1316Combined sources
Helixi138 – 14811Combined sources
Beta strandi151 – 1555Combined sources
Turni158 – 1603Combined sources
Helixi164 – 17613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0VX-ray1.78A/B/C/D1-209[»]
ProteinModelPortaliO82480.
SMRiO82480. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO82480.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi35 – 439Effector regionSequence analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
HOGENOMiHOG000233974.
InParanoidiO82480.
KOiK04392.
OMAiDDKGYLA.
PhylomeDBiO82480.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O82480-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASKFIKCV TVGDGAVGKT CMLICYTSNK FPTDYIPTVF DNFSANVAVD
60 70 80 90 100
GQIVNLGLWD TAGQEDYSRL RPLSYRGADI FVLAFSLISK ASYENVLKKW
110 120 130 140 150
MPELRRFAPN VPIVLVGTKL DLRDDKGYLA DHTNVITSTQ GEELRKQIGA
160 170 180 190 200
AAYIECSSKT QQNVKAVFDT AIKVVLQPPR RKEVPRRRKN HRRSGCSIAS

IVCGGCTAA
Length:209
Mass (Da):23,043
Last modified:November 1, 1998 - v1
Checksum:iFA0087A6A7650CB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079484 mRNA. Translation: AAC63013.1.
AF115474 Genomic DNA. Translation: AAF40246.1.
AL078469 Genomic DNA. Translation: CAB43909.1.
AL161574 Genomic DNA. Translation: CAB79653.1.
CP002687 Genomic DNA. Translation: AEE85566.1.
PIRiT08950.
RefSeqiNP_194624.1. NM_119039.2.
UniGeneiAt.3402.

Genome annotation databases

EnsemblPlantsiAT4G28950.1; AT4G28950.1; AT4G28950.
GeneIDi829016.
GrameneiAT4G28950.1; AT4G28950.1; AT4G28950.
KEGGiath:AT4G28950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079484 mRNA. Translation: AAC63013.1.
AF115474 Genomic DNA. Translation: AAF40246.1.
AL078469 Genomic DNA. Translation: CAB43909.1.
AL161574 Genomic DNA. Translation: CAB79653.1.
CP002687 Genomic DNA. Translation: AEE85566.1.
PIRiT08950.
RefSeqiNP_194624.1. NM_119039.2.
UniGeneiAt.3402.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0VX-ray1.78A/B/C/D1-209[»]
ProteinModelPortaliO82480.
SMRiO82480. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G28950.1.

Proteomic databases

PaxDbiO82480.
PRIDEiO82480.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G28950.1; AT4G28950.1; AT4G28950.
GeneIDi829016.
GrameneiAT4G28950.1; AT4G28950.1; AT4G28950.
KEGGiath:AT4G28950.

Organism-specific databases

TAIRiAT4G28950.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
HOGENOMiHOG000233974.
InParanoidiO82480.
KOiK04392.
OMAiDDKGYLA.
PhylomeDBiO82480.

Miscellaneous databases

EvolutionaryTraceiO82480.
PROiO82480.

Gene expression databases

ExpressionAtlasiO82480. baseline and differential.
GenevisibleiO82480. AT.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic structure and evolution of RAC-GTPases in Arabidopsis thaliana."
    Winge P., Brembu T., Kristensen R., Bones A.M.
    Genetics 156:1959-1971(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "A cell-specific, prenylation-independent mechanism regulates targeting of type II RACs."
    Lavy M., Bracha-Drori K., Sternberg H., Yalovsky S.
    Plant Cell 14:2431-2450(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-196; CYS-203 AND CYS-206, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-196; CYS-203 AND CYS-206.
  5. "Plasma membrane-associated ROP10 small GTPase is a specific negative regulator of abscisic acid responses in Arabidopsis."
    Zheng Z.-L., Nafisi M., Tam A., Li H., Crowell D.N., Chary S.N., Schroeder J.I., Shen J., Yang Z.
    Plant Cell 14:2787-2797(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiRAC7_ARATH
AccessioniPrimary (citable) accession number: O82480
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.