Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Rac-like GTP-binding protein ARAC6

Gene

ARAC6

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

Functioni

May be involved in cell polarity control during the actin-dependent tip growth of pollen tubes.2 Publications
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei160 – 1601GDP; via amide nitrogenCombined sources

Regions

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

GO - Molecular functioni

GO - Biological processi

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 ARAC6
Alternative name(s):
GTPase protein ROP5
Gene namesi
Name:ARAC6
Synonyms:RAC2, ROP5
Ordered Locus Names:At4g35950
ORF Names:F4B14_220, T19K4.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G35950.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: TAIR
  • membrane Source: UniProtKB-SubCell
  • nucleus 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 ARAC6PRO_0000198920Add
BLAST
Propeptidei195 – 1973Removed in mature formSequence analysisPRO_0000227585

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

PaxDbiQ9SBJ6.

Expressioni

Tissue specificityi

Ubiquitous. Preferentially expressed in mature pollen and pollen tubes.2 Publications

Gene expression databases

GenevisibleiQ9SBJ6. AT.

Interactioni

Subunit structurei

Interacts with SPK1.2 Publications

Protein-protein interaction databases

BioGridi15032. 28 interactions.
DIPiDIP-29821N.
IntActiQ9SBJ6. 5 interactions.
STRINGi3702.AT4G35950.1.

Structurei

Secondary structure

1
197
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Helixi19 – 2810Combined sources
Beta strandi57 – 593Combined sources
Turni66 – 705Combined sources
Helixi71 – 755Combined sources
Beta strandi79 – 868Combined sources
Helixi90 – 989Combined sources
Helixi100 – 1078Combined sources
Beta strandi113 – 1186Combined sources
Helixi120 – 1234Combined sources
Helixi126 – 1316Combined sources
Helixi140 – 15011Combined sources
Beta strandi153 – 1575Combined sources
Turni160 – 1623Combined sources
Helixi166 – 17712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BWDX-ray1.53D1-180[»]
ProteinModelPortaliQ9SBJ6.
SMRiQ9SBJ6. Positions 4-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SBJ6.

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.
InParanoidiQ9SBJ6.
KOiK04392.
OMAiKERRFQP.
PhylomeDBiQ9SBJ6.

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.

Q9SBJ6-1 [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 VQGEELKKLI
160 170 180 190
GAPAYIECSS KSQENVKGVF DAAIRVVLQP PKQKKKKNKA QKACSIL
Length:197
Mass (Da):21,571
Last modified:August 31, 2004 - v2
Checksum:iD26BE6D3827C1632
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF107663 mRNA. Translation: AAD17999.1.
AF079487 mRNA. Translation: AAC29480.1.
AF115473 Genomic DNA. Translation: AAF40245.1.
AL022373 Genomic DNA. Translation: CAA18489.1.
AL031986 Genomic DNA. Translation: CAA21481.1.
AL161588 Genomic DNA. Translation: CAB81504.1.
CP002687 Genomic DNA. Translation: AEE86595.1.
AK117209 mRNA. Translation: BAC41885.1.
BT005217 mRNA. Translation: AAO63281.1.
AY087336 mRNA. Translation: AAM64886.1.
AF031429 Genomic DNA. Translation: AAB87673.1.
PIRiT04705.
RefSeqiNP_195320.1. NM_119762.3.
UniGeneiAt.2216.

Genome annotation databases

EnsemblPlantsiAT4G35950.1; AT4G35950.1; AT4G35950.
GeneIDi829750.
GrameneiAT4G35950.1; AT4G35950.1; AT4G35950.
KEGGiath:AT4G35950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF107663 mRNA. Translation: AAD17999.1.
AF079487 mRNA. Translation: AAC29480.1.
AF115473 Genomic DNA. Translation: AAF40245.1.
AL022373 Genomic DNA. Translation: CAA18489.1.
AL031986 Genomic DNA. Translation: CAA21481.1.
AL161588 Genomic DNA. Translation: CAB81504.1.
CP002687 Genomic DNA. Translation: AEE86595.1.
AK117209 mRNA. Translation: BAC41885.1.
BT005217 mRNA. Translation: AAO63281.1.
AY087336 mRNA. Translation: AAM64886.1.
AF031429 Genomic DNA. Translation: AAB87673.1.
PIRiT04705.
RefSeqiNP_195320.1. NM_119762.3.
UniGeneiAt.2216.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BWDX-ray1.53D1-180[»]
ProteinModelPortaliQ9SBJ6.
SMRiQ9SBJ6. Positions 4-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15032. 28 interactions.
DIPiDIP-29821N.
IntActiQ9SBJ6. 5 interactions.
STRINGi3702.AT4G35950.1.

Proteomic databases

PaxDbiQ9SBJ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G35950.1; AT4G35950.1; AT4G35950.
GeneIDi829750.
GrameneiAT4G35950.1; AT4G35950.1; AT4G35950.
KEGGiath:AT4G35950.

Organism-specific databases

TAIRiAT4G35950.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
HOGENOMiHOG000233974.
InParanoidiQ9SBJ6.
KOiK04392.
OMAiKERRFQP.
PhylomeDBiQ9SBJ6.

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

EvolutionaryTraceiQ9SBJ6.
PROiQ9SBJ6.

Gene expression databases

GenevisibleiQ9SBJ6. 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. "Rac homologues and compartmentalized phosphatidylinositol 4, 5-bisphosphate act in a common pathway to regulate polar pollen tube growth."
    Kost B., Lemichez E., Spielhofer P., Hong Y., Tolias K., Carpenter C., Chua N.-H.
    J. Cell Biol. 145:317-330(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  2. "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 and cv. Landsberg erecta.
  3. "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.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99, FUNCTION, TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  9. "The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell morphogenesis."
    Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M., Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.
    Development 134:967-977(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPK1.
  10. "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.
  11. "Crystal structure of the plant Rho protein ROP5."
    Thomas C., Berken A.
    Submitted (JAN-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 1-180 IN COMPLEX WITH GDP.

Entry informationi

Entry nameiRAC6_ARATH
AccessioniPrimary (citable) accession number: Q9SBJ6
Secondary accession number(s): O65632
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: June 8, 2016
This is version 115 of the entry and version 2 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.