ID   GDIA_PONPY              Reviewed;         447 AA.
AC   Q7YQM0; Q5NVJ5; Q5R5T3; Q5R6M9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 80.
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;
GN   Name=GDI1; Synonyms=RABGDIA;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12777533; DOI=10.1093/molbev/msg134;
RA   Kitano T., Schwarz C., Nickel B., Paeaebo S.;
RT   "Gene diversity patterns at 10 X-chromosomal loci in humans and
RT   chimpanzees.";
RL   Mol. Biol. Evol. 20:1281-1289(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250}.
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).
CC       {ECO:0000250|UniProtKB:P31150}.
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; AB102649; BAC81118.1; -; mRNA.
DR   EMBL; CR860458; CAH92581.1; -; mRNA.
DR   EMBL; CR860770; CAH92883.1; -; mRNA.
DR   EMBL; CR926033; CAI29668.1; -; mRNA.
DR   AlphaFoldDB; Q7YQM0; -.
DR   SMR; Q7YQM0; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR   GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0032482; P:Rab protein signal transduction; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Golgi apparatus; GTPase activation.
FT   CHAIN           1..447
FT                   /note="Rab GDP dissociation inhibitor alpha"
FT                   /id="PRO_0000056675"
FT   CONFLICT        90
FT                   /note="M -> T (in Ref. 2; CAH92581)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="M -> T (in Ref. 2; CAI29668)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        289
FT                   /note="D -> G (in Ref. 2; CAH92883)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  50597 MW;  1C2DB6359944CBE4 CRC64;
     MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE ELYKRFQLLE
     GPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVVEGSFV YKGGKIYKVP
     STETEALASN LMGMFEKRRF RKFLVFVANF DENDPKTFEG VDPQTTSMRD VYRKFDLGQD
     VIDFTGHALA LYRTDDYLDQ PCLETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
     LSAIYGGTYM LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYIPDR VRKAGQVIRI
     ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI AIASTTVETT
     DPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGCESQVFC SCSYDATTHF ETTCNDIKDI
     YKRMAGTAFD FENMKRKQND VFGEAEQ