GDIA_BOVIN
ID GDIA_BOVIN Reviewed; 447 AA.
AC P21856; A4FUY4;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Rab GDP dissociation inhibitor alpha;
DE Short=Rab GDI alpha;
DE AltName: Full=Guanosine diphosphate dissociation inhibitor 1;
DE Short=GDI-1;
DE AltName: Full=SMG p25A GDI;
GN Name=GDI1; Synonyms=RABGDIA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2115118; DOI=10.1128/mcb.10.8.4116-4122.1990;
RA Matsui Y., Kikuchi A., Araki S., Hata Y., Kondo J., Teranishi Y., Takai Y.;
RT "Molecular cloning and characterization of a novel type of regulatory
RT protein (GDI) for smg p25A, a ras p21-like GTP-binding protein.";
RL Mol. Cell. Biol. 10:4116-4122(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SIMILARITY TO CHOROIDEREMIA PROTEIN.
RX PubMed=1904992; DOI=10.1038/351614b0;
RA Fodor E., Lee R.T., O'Donnell J.J.;
RT "Analysis of choroideraemia gene.";
RL Nature 351:614-614(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS), AND INTERACTION WITH RAB3A.
RX PubMed=8609986; DOI=10.1038/381042a0;
RA Schalk I., Zeng K., Wu S.-K., Stura E.A., Matteson J., Huang M., Tandon A.,
RA Wilson I.A., Balch W.E.;
RT "Structure and mutational analysis of Rab GDP-dissociation inhibitor.";
RL Nature 381:42-48(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) OF 1-431, AND FUNCTION.
RX PubMed=11208110; DOI=10.1034/j.1600-0854.2000.010309.x;
RA Luan P., Heine A., Zeng K., Moyer B., Greasely S.E., Kuhn P., Balch W.E.,
RA Wilson I.A.;
RT "A new functional domain of guanine nucleotide dissociation inhibitor
RT (alpha-GDI) involved in Rab recycling.";
RL Traffic 1:270-281(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, AND MUTAGENESIS OF LYS-89
RP AND PHE-431.
RX PubMed=12623022; DOI=10.1016/s0969-2126(03)00034-0;
RA An Y., Shao Y., Alory C., Matteson J., Sakisaka T., Chen W., Gibbs R.A.,
RA Wilson I.A., Balch W.E.;
RT "Geranylgeranyl switching regulates GDI-Rab GTPase recycling.";
RL Structure 11:347-357(2003).
CC -!- FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins
CC by inhibiting the dissociation of GDP from them, and the subsequent
CC binding of GTP to them. Promotes the dissociation of GDP-bound Rab
CC proteins from the membrane and inhibits their activation. Promotes the
CC dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes.
CC {ECO:0000269|PubMed:11208110, ECO:0000269|PubMed:12623022}.
CC -!- SUBUNIT: Interacts with RHOH (By similarity). Interacts with the non-
CC phosphorylated forms of RAB1A, RAB3A, RAB5A, RAB5B, RAB5C, RAB8A,
CC RAB8B, RAB10, RAB12, RAB35, and RAB43 (By similarity). Interacts with
CC RAB3A (PubMed:8609986). {ECO:0000250|UniProtKB:P31150,
CC ECO:0000269|PubMed:8609986}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus, trans-
CC Golgi network {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR EMBL; D90103; BAA14134.1; -; mRNA.
DR EMBL; BC123440; AAI23441.1; -; mRNA.
DR PIR; A35652; A35652.
DR RefSeq; NP_776489.1; NM_174064.3.
DR PDB; 1D5T; X-ray; 1.04 A; A=1-431.
DR PDB; 1GND; X-ray; 1.81 A; A=1-447.
DR PDB; 1LV0; X-ray; 2.00 A; A=1-447.
DR PDBsum; 1D5T; -.
DR PDBsum; 1GND; -.
DR PDBsum; 1LV0; -.
DR AlphaFoldDB; P21856; -.
DR SMR; P21856; -.
DR DIP; DIP-82N; -.
DR IntAct; P21856; 1.
DR MINT; P21856; -.
DR STRING; 9913.ENSBTAP00000016093; -.
DR PaxDb; P21856; -.
DR PeptideAtlas; P21856; -.
DR PRIDE; P21856; -.
DR Ensembl; ENSBTAT00000016093; ENSBTAP00000016093; ENSBTAG00000012125.
DR GeneID; 281188; -.
DR KEGG; bta:281188; -.
DR CTD; 2664; -.
DR VEuPathDB; HostDB:ENSBTAG00000012125; -.
DR VGNC; VGNC:29307; GDI1.
DR eggNOG; KOG1439; Eukaryota.
DR GeneTree; ENSGT00950000182994; -.
DR HOGENOM; CLU_021695_0_0_1; -.
DR InParanoid; P21856; -.
DR OMA; DHYGGES; -.
DR OrthoDB; 763627at2759; -.
DR TreeFam; TF300449; -.
DR Reactome; R-BTA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR EvolutionaryTrace; P21856; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000012125; Expressed in Ammon's horn and 101 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IDA:UniProtKB.
DR GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0032482; P:Rab protein signal transduction; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR000806; RabGDI.
DR PANTHER; PTHR11787; PTHR11787; 1.
DR Pfam; PF00996; GDI; 1.
DR PRINTS; PR00892; RABGDI.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Golgi apparatus; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..447
FT /note="Rab GDP dissociation inhibitor alpha"
FT /id="PRO_0000056669"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50396"
FT MUTAGEN 89
FT /note="K->A: Strongly reduces dissociation of RAB3A from
FT the membrane."
FT /evidence="ECO:0000269|PubMed:12623022"
FT MUTAGEN 431
FT /note="F->E: Strongly reduces dissociation of RAB3A from
FT the membrane."
FT /evidence="ECO:0000269|PubMed:12623022"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1LV0"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1D5T"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1GND"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 291..306
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1GND"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:1D5T"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 377..390
FT /evidence="ECO:0007829|PDB:1D5T"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1D5T"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:1D5T"
FT HELIX 411..425
FT /evidence="ECO:0007829|PDB:1D5T"
SQ SEQUENCE 447 AA; 50566 MW; 69C68B03BDC1BA3F CRC64;
MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE ELYKRFQLLE
GPPETMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVVEGSFV YKGGKIYKVP
STETEALASN LMGMFEKRRF RKFLVFVANF DENDPKTFEG VDPQNTSMRD VYRKFDLGQD
VIDFTGHALA LYRTDDYLDQ PCLETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
LSAIYGGTYM LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYVPDR VRKAGQVIRI
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI AIASTTVETT
DPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGSESQVFC SCSYDATTHF ETTCNDIKDI
YKRMAGSAFD FENMKRKQND VFGEADQ
