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Protein

Rho GDP-dissociation inhibitor 1

Gene

Arhgdia

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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 RAC1.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GDP-dissociation inhibitor 1
Short name:
Rho GDI 1
Alternative name(s):
GDI-1
Rho-GDI alpha
Gene namesi
Name:Arhgdia
Synonyms:C87222, Gdi1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2178103. Arhgdia.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • extracellular exosome Source: MGI
  • extracellular space Source: Ensembl
  • immunological synapse Source: MGI
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

From 1 week to 12 weeks of age, progressive deterioration from mild to massive albuminuria as consequence of renal abnormalities. In kidney, severe podocyte damage, glomerular lesions with focal and segmental sclerosis, along with prominent intratubular casts and luminal dilatation. Tubular epithelial cells show degenerative changes with basement membrane thickening. Increase of apoptotic cells in kidney glomeruli and tubulointerstitium.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi185 – 1851Missing : Loss of interaction with CDC42, RHOA and RAC1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 204203Rho GDP-dissociation inhibitor 1PRO_0000219014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei43 – 431N6-acetyllysineCombined sources
Modified residuei47 – 471PhosphoserineBy similarity
Modified residuei105 – 1051N6-acetyllysineBy similarity
Modified residuei127 – 1271N6-acetyllysineBy similarity
Cross-linki138 – 138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki138 – 138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei141 – 1411N6-acetyllysine; alternateCombined sources
Modified residuei141 – 1411N6-succinyllysine; alternateCombined sources
Cross-linki141 – 141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki141 – 141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei178 – 1781N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ99PT1.
MaxQBiQ99PT1.
PaxDbiQ99PT1.
PeptideAtlasiQ99PT1.
PRIDEiQ99PT1.
TopDownProteomicsiQ99PT1.

2D gel databases

REPRODUCTION-2DPAGEIPI00322312.
Q99PT1.
UCD-2DPAGEQ99PT1.

PTM databases

iPTMnetiQ99PT1.
PhosphoSiteiQ99PT1.
SwissPalmiQ99PT1.

Expressioni

Tissue specificityi

In kidney glomerulus, expressed in podocytes and mesangial cells.2 Publications

Gene expression databases

BgeeiQ99PT1.
CleanExiMM_ARHGDIA.
GenevisibleiQ99PT1. MM.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Rac3P607643EBI-494354,EBI-644949

Protein-protein interaction databases

BioGridi228703. 7 interactions.
IntActiQ99PT1. 5 interactions.
MINTiMINT-1613871.
STRINGi10090.ENSMUSP00000063714.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 144Combined sources
Helixi35 – 406Combined sources
Turni41 – 444Combined sources
Helixi46 – 5611Combined sources
Beta strandi69 – 7810Combined sources
Beta strandi86 – 927Combined sources
Helixi94 – 996Combined sources
Beta strandi101 – 1055Combined sources
Beta strandi109 – 11810Combined sources
Beta strandi123 – 13412Combined sources
Beta strandi137 – 14913Combined sources
Beta strandi152 – 1565Combined sources
Turni169 – 1713Combined sources
Beta strandi173 – 18210Combined sources
Beta strandi190 – 20112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F38X-ray2.80B2-204[»]
ProteinModelPortaliQ99PT1.
SMRiQ99PT1. Positions 5-204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rho GDI family.Curated

Phylogenomic databases

eggNOGiKOG3205. Eukaryota.
ENOG4111K44. LUCA.
GeneTreeiENSGT00390000006233.
HOGENOMiHOG000175765.
HOVERGENiHBG000206.
InParanoidiQ99PT1.
KOiK12462.
OMAiQMSESSI.
OrthoDBiEOG72JWH9.
PhylomeDBiQ99PT1.
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.

Q99PT1-1 [UniParc]FASTAAdd to basket

« Hide

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

EWKD
Length:204
Mass (Da):23,407
Last modified:January 23, 2007 - v3
Checksum:i8ACE6F4456D842D8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551L → P in AAH04732 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055070 mRNA. Translation: BAB21527.1.
AK075656 mRNA. Translation: BAC35881.1.
AK077343 mRNA. Translation: BAC36761.1.
AK143516 mRNA. Translation: BAE25410.1.
AK156819 mRNA. Translation: BAE33865.1.
AK165241 mRNA. Translation: BAE38098.1.
AK170553 mRNA. Translation: BAE41876.1.
AK170718 mRNA. Translation: BAE41976.1.
AK172140 mRNA. Translation: BAE42844.1.
AL663030 Genomic DNA. Translation: CAM27085.1.
BC004732 mRNA. Translation: AAH04732.1.
BC086755 mRNA. Translation: AAH86755.1.
CCDSiCCDS25743.1.
RefSeqiNP_598557.3. NM_133796.7.
XP_006532612.1. XM_006532549.2.
UniGeneiMm.30016.
Mm.456388.
Mm.474783.

Genome annotation databases

EnsembliENSMUST00000067936; ENSMUSP00000063714; ENSMUSG00000025132.
ENSMUST00000106197; ENSMUSP00000101803; ENSMUSG00000025132.
GeneIDi192662.
KEGGimmu:192662.
UCSCiuc007mtj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055070 mRNA. Translation: BAB21527.1.
AK075656 mRNA. Translation: BAC35881.1.
AK077343 mRNA. Translation: BAC36761.1.
AK143516 mRNA. Translation: BAE25410.1.
AK156819 mRNA. Translation: BAE33865.1.
AK165241 mRNA. Translation: BAE38098.1.
AK170553 mRNA. Translation: BAE41876.1.
AK170718 mRNA. Translation: BAE41976.1.
AK172140 mRNA. Translation: BAE42844.1.
AL663030 Genomic DNA. Translation: CAM27085.1.
BC004732 mRNA. Translation: AAH04732.1.
BC086755 mRNA. Translation: AAH86755.1.
CCDSiCCDS25743.1.
RefSeqiNP_598557.3. NM_133796.7.
XP_006532612.1. XM_006532549.2.
UniGeneiMm.30016.
Mm.456388.
Mm.474783.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F38X-ray2.80B2-204[»]
ProteinModelPortaliQ99PT1.
SMRiQ99PT1. Positions 5-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228703. 7 interactions.
IntActiQ99PT1. 5 interactions.
MINTiMINT-1613871.
STRINGi10090.ENSMUSP00000063714.

PTM databases

iPTMnetiQ99PT1.
PhosphoSiteiQ99PT1.
SwissPalmiQ99PT1.

2D gel databases

REPRODUCTION-2DPAGEIPI00322312.
Q99PT1.
UCD-2DPAGEQ99PT1.

Proteomic databases

EPDiQ99PT1.
MaxQBiQ99PT1.
PaxDbiQ99PT1.
PeptideAtlasiQ99PT1.
PRIDEiQ99PT1.
TopDownProteomicsiQ99PT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067936; ENSMUSP00000063714; ENSMUSG00000025132.
ENSMUST00000106197; ENSMUSP00000101803; ENSMUSG00000025132.
GeneIDi192662.
KEGGimmu:192662.
UCSCiuc007mtj.1. mouse.

Organism-specific databases

CTDi396.
MGIiMGI:2178103. Arhgdia.

Phylogenomic databases

eggNOGiKOG3205. Eukaryota.
ENOG4111K44. LUCA.
GeneTreeiENSGT00390000006233.
HOGENOMiHOG000175765.
HOVERGENiHBG000206.
InParanoidiQ99PT1.
KOiK12462.
OMAiQMSESSI.
OrthoDBiEOG72JWH9.
PhylomeDBiQ99PT1.
TreeFamiTF105387.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiArhgdia. mouse.
PROiQ99PT1.
SOURCEiSearch...

Gene expression databases

BgeeiQ99PT1.
CleanExiMM_ARHGDIA.
GenevisibleiQ99PT1. MM.

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. "Mouse cDNA sequence for RhoGDI-1."
    Minamitani T., Matsumoto K.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Pituitary and Spleen.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. Lubec G., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 34-49; 59-98 AND 153-167, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Hippocampus.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease."
    Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H., Miyoshi J., Takai Y., Fujita T.
    Nat. Med. 14:1370-1376(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through RhoGDIalpha-mediated inactivation of Rac1 GTPase."
    Li X., Lee A.Y.
    J. Biol. Chem. 285:32436-32445(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLXNB3.
  10. Cited for: FUNCTION, INTERACTION WITH RHOA; RAC1 AND CDC42, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-185.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43 AND LYS-141, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-204 IN COMPLEX WITH PRENYLATED RHOA, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiGDIR1_MOUSE
AccessioniPrimary (citable) accession number: Q99PT1
Secondary accession number(s): Q5M9P6, Q8BPI0, Q99KC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 131 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.