Q38937 (RAC5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rac-like GTP-binding protein ARAC5

Alternative name(s):
GTPase protein ROP4

Gene names

Name:	ARAC5
Synonyms:	ATGP3, ROP4
Ordered Locus Names:	At1g75840
ORF Names:	T4O12.8

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in cell polarity control during the actin-dependent tip growth of root hairs. Ref.9 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. Ref.9
Subunit structure	Interacts with GDI1 and ROPGEF8 homodimer. Ref.8 Ref.10 Ref.11
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein. Note: Associated with the membrane when activated. Ref.8
Tissue specificity	Ubiquitous. Preferentially expressed at the tip of root hairs. Ref.3 Ref.9
Sequence similarities	Belongs to the small GTPase superfamily. Rho family.
Sequence caution	The sequence AAF26755.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleolus Inferred from direct assay PubMed 15469496. Source: TAIR phragmoplast Inferred from direct assay PubMed 15469496. Source: TAIR plasma membrane Inferred from direct assay PubMed 18088316. Source: UniProtKB
Molecular_function	GTP binding Inferred from direct assay Ref.10. Source: UniProtKB GTPase activity Inferred from sequence or structural similarity Ref.9. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GDI1	Q9SFC6	2	EBI-1751308,EBI-1751328

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 193

193

Rac-like GTP-binding protein ARAC5

PRO_0000198919

Propeptide

194 – 196

3

Removed in mature form Potential

PRO_0000227584

Regions

Nucleotide binding

16 – 21

6

GTP

Nucleotide binding

119 – 121

3

GTP

Nucleotide binding

159 – 161

3

GTP

Motif

35 – 43

9

Effector region Potential

Compositional bias

182 – 190

9

Poly-Lys

Amino acid modifications

Modified residue

193

1

Cysteine methyl ester Potential

Lipidation

193

1

S-geranylgeranyl cysteine Potential

Experimental info

Mutagenesis

65

1

E → A: Strongly impairs GEF-dependent nucleotide exchange. Ref.10

Sequence conflict

22

1

M → I in AAC78242. Ref.3

Sequence conflict

88 – 89

2

IS → YC in AAD00114. Ref.1

Sequence conflict

95

1

N → H in AAC78242. Ref.3

Sequence conflict

189 – 195

7

NKNRCVF → TKAQKACSI in AAD00114. Ref.1

Secondary structure

1

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196

Helix Strand Turn

Details...

Beta strand

6 – 13

8

Helix

19 – 28

10

Beta strand

43 – 49

7

Beta strand

52 – 59

8

Turn

62 – 65

4

Beta strand

79 – 86

8

Helix

90 – 98

9

Helix

100 – 107

8

Beta strand

113 – 118

6

Helix

120 – 122

3

Helix

126 – 131

6

Helix

140 – 149

10

Beta strand

155 – 157

3

Turn

160 – 162

3

Helix

166 – 177

12

Sequences

	Sequence		Length	Mass (Da)
	Q38937 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 631317F3DA441A35	FASTA	196	21,777
	10 20 30 40 50 60 MSASRFIKCV TVGDGAVGKT CMLISYTSNT FPTDYVPTVF DNFSANVVVD GNTVNLGLWD 70 80 90 100 110 120 TAGQEDYNRL RPLSYRGADV FILAFSLISK ASYENVAKKW IPELRHYAPG VPIILVGTKL 130 140 150 160 170 180 DLRDDKQFFI DHPGAVPITT NQGEELKKLI GSPIYIECSS KTQQNVKAVF DAAIKVVLQP 190 PKQKKKKKNK NRCVFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00547065.

PIR

T48865.

RefSeq

NP_177712.1. NM_106234.2.

UniGene

At.25499.
At.49319.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NTY	X-ray	3.10	C/D	1-180	[»]

ProteinModelPortal

Q38937.

SMR

Q38937. Positions 4-179.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29820N.

IntAct

Q38937. 1 interaction.

Proteomic databases

PaxDb

Q38937.

PRIDE

Q38937.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT1G75840.1; AT1G75840.1; AT1G75840.

GeneID

843917.

KEGG

ath:AT1G75840.

Organism-specific databases

GeneFarm

4163. 421.

TAIR

At1g75840.

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233974.

InParanoid

Q38937.

KO

K07975.

OMA

QGLQMMK.

PhylomeDB

Q38937.

ProtClustDB

CLSN2682707.

Gene expression databases

Genevestigator

Q38937.

GermOnline

AT1G75840. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00174. RHO. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51420. RHO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q38937.

Entry information

Entry name

RAC5_ARATH

Accession

Primary (citable) accession number: Q38937
Secondary accession number(s): O48545, Q9LQT0, Q9ZRD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program