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Protein

Rho GDP-dissociation inhibitor 1

Gene

ARHGDIA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-BTA-193634. Axonal growth inhibition (RHOA activation).
R-BTA-194840. Rho GTPase cycle.
R-BTA-209563. Axonal growth stimulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GDP-dissociation inhibitor 1
Short name:
Rho GDI 1
Alternative name(s):
Rho-GDI alpha
Gene namesi
Name:ARHGDIA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 204203Rho GDP-dissociation inhibitor 1PRO_0000219011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei43 – 431N6-acetyllysineBy similarity
Modified residuei47 – 471PhosphoserineBy similarity
Modified residuei101 – 1011Phosphoserine; by PKASequence analysis
Modified residuei105 – 1051N6-acetyllysineBy similarity
Modified residuei115 – 1151Phosphoserine; by PKCSequence analysis
Modified residuei127 – 1271N6-acetyllysineBy similarity
Modified residuei141 – 1411N6-acetyllysine; alternateBy similarity
Modified residuei141 – 1411N6-succinyllysine; alternateBy similarity
Modified residuei178 – 1781N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP19803.
PRIDEiP19803.

Expressioni

Tissue specificityi

Brain, lung, thymus, spleen, small intestine, and kidney, and weakly in heart and liver.

Gene expression databases

ExpressionAtlasiP19803. baseline.

Interactioni

Subunit structurei

Monomer. Interacts with FER. Interacts with PLXNB3 (By similarity). Forms a heterodimer with RAC1. Interacts with RHOA, the affinity is increased by three orders of magnitude when RHOA is prenylated. Interacts with PSMD10; the interaction increases ARHGDIA association with RHOA, leading to ARHGDIA-mediated inactivation of RHOA and ROCK and prolonged AKT activation (By similarity). Interacts with RHOC and CDC42 (By similarity).By similarity

Protein-protein interaction databases

MINTiMINT-121946.
STRINGi9913.ENSBTAP00000040280.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 145Combined sources
Beta strandi16 – 205Combined sources
Helixi35 – 406Combined sources
Turni41 – 444Combined sources
Helixi46 – 5611Combined sources
Beta strandi74 – 785Combined sources
Beta strandi80 – 845Combined sources
Beta strandi87 – 893Combined sources
Helixi95 – 995Combined sources
Beta strandi102 – 1054Combined sources
Beta strandi109 – 1168Combined sources
Beta strandi123 – 13412Combined sources
Beta strandi137 – 14913Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi160 – 1645Combined sources
Helixi169 – 1713Combined sources
Beta strandi173 – 18210Combined sources
Beta strandi183 – 1875Combined sources
Beta strandi190 – 20112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJWNMR-A60-204[»]
1DOAX-ray2.60B1-204[»]
1GDFNMR-A60-204[»]
5FR1X-ray2.75B1-204[»]
5FR2X-ray3.35B1-204[»]
ProteinModelPortaliP19803.
SMRiP19803. Positions 5-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19803.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 8318HydrophobicAdd
BLAST

Sequence similaritiesi

Belongs to the Rho GDI family.Curated

Phylogenomic databases

eggNOGiKOG3205. Eukaryota.
ENOG4111K44. LUCA.
GeneTreeiENSGT00390000006233.
HOGENOMiHOG000175765.
HOVERGENiHBG000206.
InParanoidiP19803.
KOiK12462.
OMAiQMSESSI.
OrthoDBiEOG72JWH9.
TreeFamiTF105387.

Family and domain databases

Gene3Di2.70.50.30. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR000406. Rho_GDI.
IPR024792. RhoGDI_domain.
[Graphical view]
PANTHERiPTHR10980. PTHR10980. 1 hit.
PfamiPF02115. Rho_GDI. 1 hit.
[Graphical view]
PRINTSiPR00492. RHOGDI.
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P19803-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEQEPTAEQ LAQIAAENEE DEHSVNYKPP AQKSIQEIQE LDKDDESLRK
60 70 80 90 100
YKEALLGRVA VSADPNVPNV VVTRLTLVCS TAPGPLELDL TGDLESFKKQ
110 120 130 140 150
SFVLKEGVEY RIKISFRVNR EIVSGMKYIQ HTYRKGVKID KTDYMVGSYG
160 170 180 190 200
PRAEEYEFLT PMEEAPKGML ARGSYNIKSR FTDDDRTDHL SWEWNLTIKK

EWKD
Length:204
Mass (Da):23,421
Last modified:January 23, 2007 - v3
Checksum:i49CE7DEB05D271CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52689 mRNA. Translation: CAA36916.1.
BC103465 mRNA. Translation: AAI03466.1.
PIRiS12121.
RefSeqiNP_788823.1. NM_176650.3.
XP_005221068.2. XM_005221011.3.
UniGeneiBt.48750.

Genome annotation databases

EnsembliENSBTAT00000042645; ENSBTAP00000040280; ENSBTAG00000030209.
GeneIDi338054.
KEGGibta:338054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52689 mRNA. Translation: CAA36916.1.
BC103465 mRNA. Translation: AAI03466.1.
PIRiS12121.
RefSeqiNP_788823.1. NM_176650.3.
XP_005221068.2. XM_005221011.3.
UniGeneiBt.48750.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJWNMR-A60-204[»]
1DOAX-ray2.60B1-204[»]
1GDFNMR-A60-204[»]
5FR1X-ray2.75B1-204[»]
5FR2X-ray3.35B1-204[»]
ProteinModelPortaliP19803.
SMRiP19803. Positions 5-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-121946.
STRINGi9913.ENSBTAP00000040280.

Proteomic databases

PaxDbiP19803.
PRIDEiP19803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000042645; ENSBTAP00000040280; ENSBTAG00000030209.
GeneIDi338054.
KEGGibta:338054.

Organism-specific databases

CTDi396.

Phylogenomic databases

eggNOGiKOG3205. Eukaryota.
ENOG4111K44. LUCA.
GeneTreeiENSGT00390000006233.
HOGENOMiHOG000175765.
HOVERGENiHBG000206.
InParanoidiP19803.
KOiK12462.
OMAiQMSESSI.
OrthoDBiEOG72JWH9.
TreeFamiTF105387.

Enzyme and pathway databases

ReactomeiR-BTA-193634. Axonal growth inhibition (RHOA activation).
R-BTA-194840. Rho GTPase cycle.
R-BTA-209563. Axonal growth stimulation.

Miscellaneous databases

EvolutionaryTraceiP19803.

Gene expression databases

ExpressionAtlasiP19803. baseline.

Family and domain databases

Gene3Di2.70.50.30. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR000406. Rho_GDI.
IPR024792. RhoGDI_domain.
[Graphical view]
PANTHERiPTHR10980. PTHR10980. 1 hit.
PfamiPF02115. Rho_GDI. 1 hit.
[Graphical view]
PRINTSiPR00492. RHOGDI.
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a novel type of regulatory protein (GDI) for the rho proteins, ras p21-like small GTP-binding proteins."
    Fukumoto Y., Kaibuchi K., Hori Y., Fujioka H., Araki S., Ueda T., Kikuchi A., Takai Y.
    Oncogene 5:1321-1328(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
    Tissue: Brain.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Uterus.
  3. "C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases."
    Gosser Y.Q., Nomanbhoy T.K., Aghazadeh B., Manor D., Combs C., Cerione R.A., Rosen M.K.
    Nature 387:814-819(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 60-204, FUNCTION.

Entry informationi

Entry nameiGDIR1_BOVIN
AccessioniPrimary (citable) accession number: P19803
Secondary accession number(s): Q3ZBA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.