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Protein

Rac-like GTP-binding protein ARAC1

Gene

ARAC1

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

Functioni

Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation.By similarity

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

  • abscisic acid-activated signaling pathway Source: TAIR
  • auxin-activated signaling pathway Source: TAIR
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-ATH-194840. Rho GTPase cycle.
R-ATH-198203. PI3K/AKT activation.
R-ATH-392451. G beta:gamma signalling through PI3Kgamma.
R-ATH-5666185. RHO GTPases Activate Rhotekin and Rhophilins.

Names & Taxonomyi

Protein namesi
Recommended name:
Rac-like GTP-binding protein ARAC1
Alternative name(s):
GTPase protein ROP3
Gene namesi
Name:ARAC1
Synonyms:ATGP2, ROP3
Ordered Locus Names:At2g17800
ORF Names:T17A5.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G17800.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: TAIR
  • nucleus Source: TAIR
  • phragmoplast Source: TAIR
  • plasma membrane Source: TAIR
  • spindle Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Rac-like GTP-binding protein ARAC1PRO_0000198915Add
BLAST
Propeptidei195 – 1973Removed in mature formSequence analysisPRO_0000227580

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941Cysteine methyl esterSequence analysis
Lipidationi194 – 1941S-geranylgeranyl cysteineSequence analysis

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiQ38902.
PRIDEiQ38902.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

GenevisibleiQ38902. AT.

Interactioni

Subunit structurei

Interacts with SPK1.1 Publication

Protein-protein interaction databases

BioGridi1647. 3 interactions.
DIPiDIP-29819N.
STRINGi3702.AT2G17800.1.

Structurei

3D structure databases

ProteinModelPortaliQ38902.
SMRiQ38902. Positions 4-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi182 – 1898Poly-Lys

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
HOGENOMiHOG000233974.
InParanoidiQ38902.
KOiK04392.
OMAiNPIIYPQ.
PhylomeDBiQ38902.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q38902-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASRFIKCV TVGDGAVGKT CLLISYTSNT FPTDYVPTVF DNFSANVVVN
60 70 80 90 100
GATVNLGLWD TAGQEDYNRL RPLSYRGADV FILAFSLISK ASYENVSKKW
110 120 130 140 150
IPELKHYAPG VPIVLVGTKL DLRDDKQFFI DHPGAVPITT AQGEELKKLI
160 170 180 190
GAPAYIECSS KTQENVKGVF DAAIRVVLQP PKQKKKKSKA QKACSIL
Length:197
Mass (Da):21,530
Last modified:November 1, 1997 - v1
Checksum:iC566CFC0C4390632
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64919 mRNA. Translation: AAD00113.1.
U41295 mRNA. Translation: AAC49851.1.
AF115466 Genomic DNA. Translation: AAF40237.1.
CP002685 Genomic DNA. Translation: AEC06689.1.
CP002685 Genomic DNA. Translation: AEC06690.1.
AY093046 mRNA. Translation: AAM13045.1.
BT000393 mRNA. Translation: AAN15712.1.
PIRiT08857.
RefSeqiNP_001077910.1. NM_001084441.1.
NP_179371.1. NM_127334.3.
UniGeneiAt.23460.

Genome annotation databases

EnsemblPlantsiAT2G17800.1; AT2G17800.1; AT2G17800.
AT2G17800.2; AT2G17800.2; AT2G17800.
GeneIDi816290.
GrameneiAT2G17800.1; AT2G17800.1; AT2G17800.
AT2G17800.2; AT2G17800.2; AT2G17800.
KEGGiath:AT2G17800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64919 mRNA. Translation: AAD00113.1.
U41295 mRNA. Translation: AAC49851.1.
AF115466 Genomic DNA. Translation: AAF40237.1.
CP002685 Genomic DNA. Translation: AEC06689.1.
CP002685 Genomic DNA. Translation: AEC06690.1.
AY093046 mRNA. Translation: AAM13045.1.
BT000393 mRNA. Translation: AAN15712.1.
PIRiT08857.
RefSeqiNP_001077910.1. NM_001084441.1.
NP_179371.1. NM_127334.3.
UniGeneiAt.23460.

3D structure databases

ProteinModelPortaliQ38902.
SMRiQ38902. Positions 4-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1647. 3 interactions.
DIPiDIP-29819N.
STRINGi3702.AT2G17800.1.

Proteomic databases

PaxDbiQ38902.
PRIDEiQ38902.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G17800.1; AT2G17800.1; AT2G17800.
AT2G17800.2; AT2G17800.2; AT2G17800.
GeneIDi816290.
GrameneiAT2G17800.1; AT2G17800.1; AT2G17800.
AT2G17800.2; AT2G17800.2; AT2G17800.
KEGGiath:AT2G17800.

Organism-specific databases

TAIRiAT2G17800.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
HOGENOMiHOG000233974.
InParanoidiQ38902.
KOiK04392.
OMAiNPIIYPQ.
PhylomeDBiQ38902.

Enzyme and pathway databases

ReactomeiR-ATH-194840. Rho GTPase cycle.
R-ATH-198203. PI3K/AKT activation.
R-ATH-392451. G beta:gamma signalling through PI3Kgamma.
R-ATH-5666185. RHO GTPases Activate Rhotekin and Rhophilins.

Miscellaneous databases

PROiQ38902.

Gene expression databases

GenevisibleiQ38902. 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. "Identification and isoprenylation of plant GTP-binding proteins."
    Biermann B.J., Randall S.K., Crowell D.N.
    Plant Mol. Biol. 31:1021-1028(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and characterization of rac-like cDNAs from Arabidopsis thaliana."
    Winge P., Brembu T., Bones A.M.
    Plant Mol. Biol. 35:483-495(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  3. "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 [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Arabidopsis Rho-related GTPases: differential gene expression in pollen and polar localization in fission yeast."
    Li H., Wu G., Ware D., Davis K.R., Yang Z.
    Plant Physiol. 118:407-417(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "A SPIKE1 signaling complex controls actin-dependent cell morphogenesis through the heteromeric WAVE and ARP2/3 complexes."
    Basu D., Le J., Zakharova T., Mallery E.L., Szymanski D.B.
    Proc. Natl. Acad. Sci. U.S.A. 105:4044-4049(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPK1.
    Strain: cv. Columbia.

Entry informationi

Entry nameiRAC1_ARATH
AccessioniPrimary (citable) accession number: Q38902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 125 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.