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 ARAC5

Gene

ARAC5

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 root hairs.1 Publication
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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 216GTP
Nucleotide bindingi119 – 1213GTP
Nucleotide bindingi159 – 1613GTP

GO - Molecular functioni

  • GTPase activity Source: TAIR
  • GTP binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G75840-MONOMER.
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 ARAC5
Alternative name(s):
GTPase protein ROP4
Gene namesi
Name:ARAC5
Synonyms:ATGP3, ROP4
Ordered Locus Names:At1g75840
ORF Names:T4O12.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G75840.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651E → A: Strongly impairs GEF-dependent nucleotide exchange. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193193Rac-like GTP-binding protein ARAC5PRO_0000198919Add
BLAST
Propeptidei194 – 1963Removed in mature formSequence analysisPRO_0000227584

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931Cysteine methyl esterSequence analysis
Lipidationi193 – 1931S-geranylgeranyl cysteineSequence analysis

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiQ38937.
PRIDEiQ38937.

Expressioni

Tissue specificityi

Ubiquitous. Preferentially expressed at the tip of root hairs.2 Publications

Gene expression databases

GenevisibleiQ38937. AT.

Interactioni

Subunit structurei

Interacts with GDI1 and ROPGEF8 homodimer (PubMed:10798620, PubMed:17218277, PubMed:19335195). Binds to SPK1 (PubMed:18308939).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GDI1Q9SFC62EBI-1751308,EBI-1751328

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi29136. 6 interactions.
DIPiDIP-29820N.
IntActiQ38937. 1 interaction.
STRINGi3702.AT1G75840.1.

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 138Combined sources
Helixi19 – 2810Combined sources
Beta strandi43 – 497Combined sources
Beta strandi52 – 598Combined sources
Turni62 – 654Combined sources
Beta strandi79 – 868Combined sources
Helixi90 – 989Combined sources
Helixi100 – 1078Combined sources
Beta strandi113 – 1186Combined sources
Helixi120 – 1223Combined sources
Helixi126 – 1316Combined sources
Helixi140 – 14910Combined sources
Beta strandi155 – 1573Combined sources
Turni160 – 1623Combined sources
Helixi166 – 17712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NTYX-ray3.10C/D1-180[»]
ProteinModelPortaliQ38937.
SMRiQ38937. Positions 4-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ38937.

Family & Domainsi

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi182 – 1909Poly-Lys

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
HOGENOMiHOG000233974.
InParanoidiQ38937.
KOiK04392.
OMAiRGDTETH.
PhylomeDBiQ38937.

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.

Q38937-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASRFIKCV TVGDGAVGKT CMLISYTSNT FPTDYVPTVF DNFSANVVVD
60 70 80 90 100
GNTVNLGLWD TAGQEDYNRL RPLSYRGADV FILAFSLISK ASYENVAKKW
110 120 130 140 150
IPELRHYAPG VPIILVGTKL DLRDDKQFFI DHPGAVPITT NQGEELKKLI
160 170 180 190
GSPIYIECSS KTQQNVKAVF DAAIKVVLQP PKQKKKKKNK NRCVFL
Length:196
Mass (Da):21,777
Last modified:November 1, 1997 - v1
Checksum:i631317F3DA441A35
GO

Sequence cautioni

The sequence AAF26755.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221M → I in AAC78242 (PubMed:9765526).Curated
Sequence conflicti88 – 892IS → YC in AAD00114 (PubMed:8843944).Curated
Sequence conflicti95 – 951N → H in AAC78242 (PubMed:9765526).Curated
Sequence conflicti189 – 1957NKNRCVF → TKAQKACSI in AAD00114 (PubMed:8843944).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64920 mRNA. Translation: AAD00114.1.
U52350 mRNA. Translation: AAC49855.1.
AF031428 mRNA. Translation: AAC78242.1.
AF115472 Genomic DNA. Translation: AAF40244.1.
AC007396 Genomic DNA. Translation: AAF26755.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE35764.1.
AY062800 mRNA. Translation: AAL32878.1.
AY081600 mRNA. Translation: AAM10162.1.
PIRiT48865.
RefSeqiNP_177712.1. NM_106234.2.
UniGeneiAt.25499.
At.49319.

Genome annotation databases

EnsemblPlantsiAT1G75840.1; AT1G75840.1; AT1G75840.
GeneIDi843917.
GrameneiAT1G75840.1; AT1G75840.1; AT1G75840.
KEGGiath:AT1G75840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64920 mRNA. Translation: AAD00114.1.
U52350 mRNA. Translation: AAC49855.1.
AF031428 mRNA. Translation: AAC78242.1.
AF115472 Genomic DNA. Translation: AAF40244.1.
AC007396 Genomic DNA. Translation: AAF26755.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE35764.1.
AY062800 mRNA. Translation: AAL32878.1.
AY081600 mRNA. Translation: AAM10162.1.
PIRiT48865.
RefSeqiNP_177712.1. NM_106234.2.
UniGeneiAt.25499.
At.49319.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NTYX-ray3.10C/D1-180[»]
ProteinModelPortaliQ38937.
SMRiQ38937. Positions 4-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi29136. 6 interactions.
DIPiDIP-29820N.
IntActiQ38937. 1 interaction.
STRINGi3702.AT1G75840.1.

Proteomic databases

PaxDbiQ38937.
PRIDEiQ38937.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G75840.1; AT1G75840.1; AT1G75840.
GeneIDi843917.
GrameneiAT1G75840.1; AT1G75840.1; AT1G75840.
KEGGiath:AT1G75840.

Organism-specific databases

TAIRiAT1G75840.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
HOGENOMiHOG000233974.
InParanoidiQ38937.
KOiK04392.
OMAiRGDTETH.
PhylomeDBiQ38937.

Enzyme and pathway databases

BioCyciARA:AT1G75840-MONOMER.
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

EvolutionaryTraceiQ38937.
PROiQ38937.

Gene expression databases

GenevisibleiQ38937. 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. "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 [MRNA], TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  4. "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.
  5. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  6. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  7. "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.
  8. "Localization of AtROP4 and AtROP6 and interaction with the guanine nucleotide dissociation inhibitor AtRhoGDI1 from Arabidopsis."
    Bischoff F., Vahlkamp L., Molendijk A.J., Palme K.
    Plant Mol. Biol. 42:515-530(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RHO GDI-1.
  9. "Arabidopsis thaliana Rop GTPases are localized to tips of root hairs and control polar growth."
    Molendijk A.J., Bischoff F., Rajendrakumar C.S.V., Friml J., Braun M., Gilroy S., Palme K.
    EMBO J. 20:2779-2788(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  10. "Structural evidence for a common intermediate in small G protein-GEF reactions."
    Thomas C., Fricke I., Scrima A., Berken A., Wittinghofer A.
    Mol. Cell 25:141-149(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-180 IN COMPLEX WITH GDP, INTERACTION WITH ROPGEF8, MUTAGENESIS OF GLU-65.
  11. "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.
  12. "3D structure of a binary ROP-PRONE complex: the final intermediate for a complete set of molecular snapshots of the RopGEF reaction."
    Thomas C., Fricke I., Weyand M., Berken A.
    Biol. Chem. 390:427-435(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 76-440, INTERACTION WITH ROPGEF8.

Entry informationi

Entry nameiRAC5_ARATH
AccessioniPrimary (citable) accession number: Q38937
Secondary accession number(s): O48545, Q9LQT0, Q9ZRD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 139 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.