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Protein

Rab GDP dissociation inhibitor alpha

Gene

GDI1

Organism
Bos taurus (Bovine)
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

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
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-BTA-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
SMG p25A GDI
Gene namesi
Name:GDI1
Synonyms:RABGDIA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome X

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • Golgi apparatus Source: UniProtKB-SubCell
  • midbody Source: Ensembl
  • myelin sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891K → A: Strongly reduces dissociation of RAB3A from the membrane. 1 Publication
Mutagenesisi431 – 4311F → E: Strongly reduces dissociation of RAB3A from the membrane. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Rab GDP dissociation inhibitor alphaPRO_0000056669Add
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
Modified residuei427 – 4271PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP21856.
PeptideAtlasiP21856.
PRIDEiP21856.

Expressioni

Gene expression databases

BgeeiENSBTAG00000012125.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-82N.
IntActiP21856. 1 interaction.
STRINGi9913.ENSBTAP00000016093.

Structurei

Secondary structure

1
447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Helixi14 – 2512Combined sources
Beta strandi30 – 334Combined sources
Beta strandi35 – 395Combined sources
Helixi41 – 433Combined sources
Helixi49 – 557Combined sources
Helixi64 – 663Combined sources
Helixi69 – 713Combined sources
Beta strandi74 – 774Combined sources
Beta strandi80 – 823Combined sources
Helixi86 – 949Combined sources
Helixi96 – 994Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi107 – 1126Combined sources
Beta strandi115 – 1184Combined sources
Helixi123 – 1286Combined sources
Beta strandi130 – 1323Combined sources
Helixi134 – 14916Combined sources
Helixi155 – 1584Combined sources
Turni163 – 1653Combined sources
Helixi168 – 1747Combined sources
Helixi179 – 18810Combined sources
Beta strandi193 – 1953Combined sources
Helixi196 – 1994Combined sources
Beta strandi200 – 2023Combined sources
Helixi203 – 21412Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi223 – 2275Combined sources
Helixi233 – 24513Combined sources
Beta strandi248 – 2525Combined sources
Beta strandi257 – 2615Combined sources
Beta strandi264 – 2707Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi278 – 2825Combined sources
Helixi284 – 2863Combined sources
Helixi288 – 2903Combined sources
Beta strandi291 – 30616Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi315 – 3217Combined sources
Helixi323 – 3253Combined sources
Beta strandi332 – 3387Combined sources
Helixi339 – 3413Combined sources
Beta strandi349 – 3568Combined sources
Helixi362 – 3654Combined sources
Helixi367 – 3704Combined sources
Turni371 – 3733Combined sources
Beta strandi377 – 39014Combined sources
Turni394 – 3963Combined sources
Beta strandi398 – 4003Combined sources
Beta strandi408 – 4103Combined sources
Helixi411 – 42515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D5TX-ray1.04A1-431[»]
1GNDX-ray1.81A1-447[»]
1LV0X-ray2.00A1-447[»]
ProteinModelPortaliP21856.
SMRiP21856. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21856.

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab GDI family.Curated

Phylogenomic databases

eggNOGiKOG1439. Eukaryota.
COG5044. LUCA.
GeneTreeiENSGT00530000063044.
HOGENOMiHOG000163825.
HOVERGENiHBG000839.
InParanoidiP21856.
KOiK17255.
OMAiYCDPTYV.
OrthoDBiEOG091G06PV.
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.

P21856-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE
60 70 80 90 100
ELYKRFQLLE GPPETMGRGR 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 ICDPSYVPDR VRKAGQVIRI
310 320 330 340 350
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI
360 370 380 390 400
AIASTTVETT DPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGSESQVFC
410 420 430 440
SCSYDATTHF ETTCNDIKDI YKRMAGSAFD FENMKRKQND VFGEADQ
Length:447
Mass (Da):50,566
Last modified:May 1, 1991 - v1
Checksum:i69C68B03BDC1BA3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90103 mRNA. Translation: BAA14134.1.
BC123440 mRNA. Translation: AAI23441.1.
PIRiA35652.
RefSeqiNP_776489.1. NM_174064.3.
UniGeneiBt.2235.

Genome annotation databases

EnsembliENSBTAT00000016093; ENSBTAP00000016093; ENSBTAG00000012125.
GeneIDi281188.
KEGGibta:281188.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90103 mRNA. Translation: BAA14134.1.
BC123440 mRNA. Translation: AAI23441.1.
PIRiA35652.
RefSeqiNP_776489.1. NM_174064.3.
UniGeneiBt.2235.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D5TX-ray1.04A1-431[»]
1GNDX-ray1.81A1-447[»]
1LV0X-ray2.00A1-447[»]
ProteinModelPortaliP21856.
SMRiP21856. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-82N.
IntActiP21856. 1 interaction.
STRINGi9913.ENSBTAP00000016093.

Proteomic databases

PaxDbiP21856.
PeptideAtlasiP21856.
PRIDEiP21856.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000016093; ENSBTAP00000016093; ENSBTAG00000012125.
GeneIDi281188.
KEGGibta:281188.

Organism-specific databases

CTDi2664.

Phylogenomic databases

eggNOGiKOG1439. Eukaryota.
COG5044. LUCA.
GeneTreeiENSGT00530000063044.
HOGENOMiHOG000163825.
HOVERGENiHBG000839.
InParanoidiP21856.
KOiK17255.
OMAiYCDPTYV.
OrthoDBiEOG091G06PV.
TreeFamiTF300449.

Enzyme and pathway databases

ReactomeiR-BTA-194840. Rho GTPase cycle.

Miscellaneous databases

EvolutionaryTraceiP21856.

Gene expression databases

BgeeiENSBTAG00000012125.

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...

Entry informationi

Entry nameiGDIA_BOVIN
AccessioniPrimary (citable) accession number: P21856
Secondary accession number(s): A4FUY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: September 7, 2016
This is version 125 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

3D-structure, Complete proteome, 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.