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Protein

Rab GDP dissociation inhibitor alpha

Gene

Gdi1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_297947. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:99846. Gdi1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • Golgi apparatus Source: UniProtKB-SubCell
  • midbody Source: MGI
  • myelin sheath Source: UniProtKB
  • neuron projection Source: Ensembl
  • protein complex Source: Ensembl
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_0000056673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei112 – 1121N6-acetyllysineBy similarity
Modified residuei269 – 2691N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP50396.
PaxDbiP50396.
PRIDEiP50396.

PTM databases

PhosphoSiteiP50396.

Expressioni

Tissue specificityi

High expression in brain, lower in other tissues.

Gene expression databases

BgeeiP50396.
ExpressionAtlasiP50396. baseline and differential.
GenevisibleiP50396. MM.

Interactioni

Subunit structurei

Interacts with RHOH, RAB1A, RAB3A and RAB5A (By similarity). Interacts with RAB10.By similarity1 Publication

Protein-protein interaction databases

BioGridi199890. 1 interaction.
IntActiP50396. 7 interactions.
MINTiMINT-1869124.
STRINGi10090.ENSMUSP00000015435.

Structurei

3D structure databases

ProteinModelPortaliP50396.
SMRiP50396. Positions 1-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab GDI family.Curated

Phylogenomic databases

eggNOGiCOG5044.
GeneTreeiENSGT00530000063044.
HOVERGENiHBG000839.
InParanoidiP50396.
KOiK17255.
OMAiKTWKDFD.
OrthoDBiEOG7PP56D.
PhylomeDBiP50396.
TreeFamiTF300449.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR018203. GDP_dissociation_inhibitor.
IPR016040. NAD(P)-bd_dom.
IPR000806. RabGDI.
[Graphical view]
PfamiPF00996. GDI. 1 hit.
[Graphical view]
PRINTSiPR00892. RABGDI.
PR00891. RABGDIREP.

Sequencei

Sequence statusi: Complete.

P50396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE
60 70 80 90 100
ELYKRFQILE GPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL
110 120 130 140 150
DFKVVEGSFV YKGGKIYKVP STETEALASN LMGMFEKRRF RKFLVFVANF
160 170 180 190 200
DENDPKTFEG VDPQNTSMRD VYRKFDLGQD VIDFTGHALA LYRTDDYLDQ
210 220 230 240 250
PCLETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR LSAIYGGTYM
260 270 280 290 300
LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYIPDR VQKAGQVIRI
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):50,522
Last modified:May 10, 2004 - v3
Checksum:iF7B9BC942B35DF58
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581I → M in AAK49815 (PubMed:11027356).Curated
Sequence conflicti58 – 581I → M in BAE33632 (PubMed:16141072).Curated
Sequence conflicti58 – 581I → M in BAE42320 (PubMed:16141072).Curated
Sequence conflicti128 – 1281A → R in AAB16907 (PubMed:7513052).Curated
Sequence conflicti165 – 1651N → T in AAK49815 (PubMed:11027356).Curated
Sequence conflicti196 – 1961D → E in AAB16907 (PubMed:7513052).Curated
Sequence conflicti223 – 2231P → S in AAL60197 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF251042 mRNA. Translation: AAK49815.1.
AF441240 Genomic DNA. Translation: AAL60197.1.
AK028880 mRNA. Translation: BAC26169.1.
AK156224 mRNA. Translation: BAE33632.1.
AK171216 mRNA. Translation: BAE42320.1.
AL807376 Genomic DNA. Translation: CAM24345.1.
BC010220 mRNA. Translation: AAH10220.1.
BC013758 mRNA. Translation: AAH13758.1.
BC037598 mRNA. Translation: AAH37598.1.
U07950 mRNA. Translation: AAB16907.1.
CCDSiCCDS30227.1.
PIRiC56024.
RefSeqiNP_034403.1. NM_010273.4.
UniGeneiMm.205830.

Genome annotation databases

EnsembliENSMUST00000015435; ENSMUSP00000015435; ENSMUSG00000015291.
GeneIDi14567.
KEGGimmu:14567.
UCSCiuc009tom.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF251042 mRNA. Translation: AAK49815.1.
AF441240 Genomic DNA. Translation: AAL60197.1.
AK028880 mRNA. Translation: BAC26169.1.
AK156224 mRNA. Translation: BAE33632.1.
AK171216 mRNA. Translation: BAE42320.1.
AL807376 Genomic DNA. Translation: CAM24345.1.
BC010220 mRNA. Translation: AAH10220.1.
BC013758 mRNA. Translation: AAH13758.1.
BC037598 mRNA. Translation: AAH37598.1.
U07950 mRNA. Translation: AAB16907.1.
CCDSiCCDS30227.1.
PIRiC56024.
RefSeqiNP_034403.1. NM_010273.4.
UniGeneiMm.205830.

3D structure databases

ProteinModelPortaliP50396.
SMRiP50396. Positions 1-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199890. 1 interaction.
IntActiP50396. 7 interactions.
MINTiMINT-1869124.
STRINGi10090.ENSMUSP00000015435.

PTM databases

PhosphoSiteiP50396.

Proteomic databases

MaxQBiP50396.
PaxDbiP50396.
PRIDEiP50396.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015435; ENSMUSP00000015435; ENSMUSG00000015291.
GeneIDi14567.
KEGGimmu:14567.
UCSCiuc009tom.2. mouse.

Organism-specific databases

CTDi2664.
MGIiMGI:99846. Gdi1.

Phylogenomic databases

eggNOGiCOG5044.
GeneTreeiENSGT00530000063044.
HOVERGENiHBG000839.
InParanoidiP50396.
KOiK17255.
OMAiKTWKDFD.
OrthoDBiEOG7PP56D.
PhylomeDBiP50396.
TreeFamiTF300449.

Enzyme and pathway databases

ReactomeiREACT_297947. Rho GTPase cycle.

Miscellaneous databases

NextBioi286278.
PROiP50396.
SOURCEiSearch...

Gene expression databases

BgeeiP50396.
ExpressionAtlasiP50396. baseline and differential.
GenevisibleiP50396. MM.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR018203. GDP_dissociation_inhibitor.
IPR016040. NAD(P)-bd_dom.
IPR000806. RabGDI.
[Graphical view]
PfamiPF00996. GDI. 1 hit.
[Graphical view]
PRINTSiPR00892. RABGDI.
PR00891. RABGDIREP.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Role of rab GDP dissociation inhibitor alpha in regulating plasticity of hippocampal neurotransmission."
    Ishizaki H., Miyoshi J., Kamiya H., Togawa A., Tanaka M., Sasaki T., Endo K., Mizoguchi A., Ozawa S., Takai Y.
    Proc. Natl. Acad. Sci. U.S.A. 97:11587-11592(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  2. "Knockout mice carrying a deletion of the mental retardation gene Gdi1 show impaired associative memory and inappropriate social behavior."
    D'Adamo P., Welzl H., Papadimitriou S., Raffaele di Barletta M., Tiveron C., Tatangelo L., Chapman P.F., Knevett S.G., Ramsay M.F., Valtorta F., Leoni C., Menegon A., Wolfer D.P., Lipp H.-P., Toniolo D.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvEv.
  3. "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: Skin and Spleen.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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 and FVB/N.
    Tissue: Eye and Mammary tumor.
  6. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 36-54; 56-68; 104-112; 119-137; 143-169; 174-208; 211-218; 222-240; 300-328; 349-379 AND 424-447, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  7. "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] OF 125-447.
    Strain: BALB/c.
    Tissue: Skeletal muscle.
  8. "GDI-1 preferably interacts with Rab10 in insulin-stimulated GLUT4 translocation."
    Chen Y., Deng Y., Zhang J., Yang L., Xie X., Xu T.
    Biochem. J. 422:229-235(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB10.

Entry informationi

Entry nameiGDIA_MOUSE
AccessioniPrimary (citable) accession number: P50396
Secondary accession number(s): A2AMA8
, Q3TBI9, Q8VHM3, Q91Y71, Q91Z41, Q96CX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2004
Last modified: July 22, 2015
This is version 119 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.