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Protein

Rab GDP dissociation inhibitor alpha

Gene

Gdi1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes.2 Publications

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • oxidoreductase activity Source: InterPro
  • Rab GDP-dissociation inhibitor activity Source: RGD
  • Rab GTPase binding Source: UniProtKB

GO - Biological processi

  • negative regulation of axonogenesis Source: UniProtKB
  • negative regulation of protein targeting to membrane Source: UniProtKB
  • protein transport Source: InterPro
  • Rab protein signal transduction Source: UniProtKB
  • regulation of catalytic activity Source: GOC
  • response to calcium ion Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-RNO-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rab GDP dissociation inhibitor alpha
Short name:
Rab GDI alpha
Alternative name(s):
Guanosine diphosphate dissociation inhibitor 1
Short name:
GDI-1
Gene namesi
Name:Gdi1
Synonyms:Rabgdia
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi2676. Gdi1.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: UniProtKB-SubCell
  • midbody Source: Ensembl
  • myelin sheath Source: UniProtKB
  • neuron projection Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Rab GDP dissociation inhibitor alphaPRO_0000056676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei427 – 4271PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP50398.
PRIDEiP50398.

2D gel databases

World-2DPAGE0004:P50398.

PTM databases

iPTMnetiP50398.
PhosphoSiteiP50398.

Expressioni

Tissue specificityi

High expression in brain, lower in other tissues.1 Publication

Gene expression databases

GenevisibleiP50398. RN.

Interactioni

Subunit structurei

Interacts with RHOH, RAB1A, RAB3A, RAB5A and RAB10.By similarity

GO - Molecular functioni

  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi247236. 1 interaction.
IntActiP50398. 1 interaction.
STRINGi10116.ENSRNOP00000053135.

Structurei

3D structure databases

ProteinModelPortaliP50398.
SMRiP50398. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab GDI family.Curated

Phylogenomic databases

eggNOGiKOG1439. Eukaryota.
COG5044. LUCA.
GeneTreeiENSGT00530000063044.
HOGENOMiHOG000163825.
HOVERGENiHBG000839.
InParanoidiP50398.
KOiK17255.
OMAiYCDPTYV.
OrthoDBiEOG7PP56D.
PhylomeDBiP50398.
TreeFamiTF300449.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR018203. GDP_dissociation_inhibitor.
IPR016040. NAD(P)-bd_dom.
IPR000806. RabGDI.
[Graphical view]
PfamiPF00996. GDI. 1 hit.
[Graphical view]
PRINTSiPR00892. RABGDI.
PR00891. RABGDIREP.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

P50398-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE
60 70 80 90 100
ELYKRFQLLE GPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL
110 120 130 140 150
DFKVVEGSFV YKGGKIYKVP STETEALASN LMGMFEKRRF RKFLVFVANF
160 170 180 190 200
DENDPKTFEG VDPQTTSMRD VYRKFDLGQD VIDFTGHALA LYRTDDYLDQ
210 220 230 240 250
PCLETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR LSAIYGGTYM
260 270 280 290 300
LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYIPDR VRKAGQVIRI
310 320 330 340 350
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI
360 370 380 390 400
AIASTTVETA EPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGSESQVFC
410 420 430 440
SCSYDATTHF ETTCNDIKDI YKRMAGSAFD FENMKRKQND VFGEADQ
Length:447
Mass (Da):50,537
Last modified:October 1, 1996 - v1
Checksum:i58384671991DF793
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991D → Y in CAA52413 (PubMed:8188702).Curated
Sequence conflicti230 – 2301G → S in AAB16909 (PubMed:7513052).Curated
Sequence conflicti330 – 3301S → P in AAB16909 (PubMed:7513052).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74402 mRNA. Translation: CAA52413.1.
U07952 mRNA. Translation: AAB16909.1.
BC099763 mRNA. Translation: AAH99763.1.
AF130987 mRNA. Translation: AAD25536.1.
PIRiA54091.
B56024.
RefSeqiNP_058784.2. NM_017088.2.
UniGeneiRn.4000.

Genome annotation databases

EnsembliENSRNOT00000089814; ENSRNOP00000070171; ENSRNOG00000056870.
GeneIDi25183.
KEGGirno:25183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74402 mRNA. Translation: CAA52413.1.
U07952 mRNA. Translation: AAB16909.1.
BC099763 mRNA. Translation: AAH99763.1.
AF130987 mRNA. Translation: AAD25536.1.
PIRiA54091.
B56024.
RefSeqiNP_058784.2. NM_017088.2.
UniGeneiRn.4000.

3D structure databases

ProteinModelPortaliP50398.
SMRiP50398. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247236. 1 interaction.
IntActiP50398. 1 interaction.
STRINGi10116.ENSRNOP00000053135.

PTM databases

iPTMnetiP50398.
PhosphoSiteiP50398.

2D gel databases

World-2DPAGE0004:P50398.

Proteomic databases

PaxDbiP50398.
PRIDEiP50398.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000089814; ENSRNOP00000070171; ENSRNOG00000056870.
GeneIDi25183.
KEGGirno:25183.

Organism-specific databases

CTDi2664.
RGDi2676. Gdi1.

Phylogenomic databases

eggNOGiKOG1439. Eukaryota.
COG5044. LUCA.
GeneTreeiENSGT00530000063044.
HOGENOMiHOG000163825.
HOVERGENiHBG000839.
InParanoidiP50398.
KOiK17255.
OMAiYCDPTYV.
OrthoDBiEOG7PP56D.
PhylomeDBiP50398.
TreeFamiTF300449.

Enzyme and pathway databases

ReactomeiR-RNO-194840. Rho GTPase cycle.

Miscellaneous databases

NextBioi605677.
PROiP50398.

Gene expression databases

GenevisibleiP50398. RN.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR018203. GDP_dissociation_inhibitor.
IPR016040. NAD(P)-bd_dom.
IPR000806. RabGDI.
[Graphical view]
PfamiPF00996. GDI. 1 hit.
[Graphical view]
PRINTSiPR00892. RABGDI.
PR00891. RABGDIREP.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of two rab GDI species from rat brain: brain-specific and ubiquitous types."
    Nishimura N., Nakamura H., Takai Y., Sano K.
    J. Biol. Chem. 269:14191-14198(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Cloning, characterization, and expression of a novel GDP dissociation inhibitor isoform from skeletal muscle."
    Shisheva A., Suedhof T.C., Czech M.P.
    Mol. Cell. Biol. 14:3459-3468(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Brain.
  3. "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].
    Tissue: Prostate.
  4. "Impairment of bile salt-dependent lipase secretion in human pancreatic tumoral SOJ-6 cells."
    Caillol N., Pasqualini E., Lloubes R., Lombardo D.
    J. Cell. Biochem. 79:628-647(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-439.
    Tissue: Pancreas.
  5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 80-98; 104-112; 143-156; 194-208; 211-218; 222-240 AND 279-290, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Hippocampus.

Entry informationi

Entry nameiGDIA_RAT
AccessioniPrimary (citable) accession number: P50398
Secondary accession number(s): Q499U0, Q9R274
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 17, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.