GDIA_CANLF
ID GDIA_CANLF Reviewed; 447 AA.
AC O97555;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 110.
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;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=9802909; DOI=10.1091/mbc.9.11.3241;
RA Chen W., Feng Y., Chen D., Wandinger-Ness A.;
RT "Rab11 is required for trans-Golgi network-to-plasma membrane transport and
RT a preferential target for GDP dissociation inhibitor.";
RL Mol. Biol. Cell 9:3241-3257(1998).
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:9802909}.
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; AF027360; AAD04246.1; -; mRNA.
DR RefSeq; NP_001003185.1; NM_001003185.1.
DR AlphaFoldDB; O97555; -.
DR SMR; O97555; -.
DR STRING; 9615.ENSCAFP00000028963; -.
DR GeneID; 403819; -.
DR CTD; 2664; -.
DR InParanoid; O97555; -.
DR OrthoDB; 763627at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 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 2: Evidence at transcript level;
KW Cytoplasm; Golgi apparatus; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..447
FT /note="Rab GDP dissociation inhibitor alpha"
FT /id="PRO_0000056670"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50396"
SQ SEQUENCE 447 AA; 50521 MW; 10280DAD33E4BCD0 CRC64;
MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE ELYKRFQLLE
GPPEAMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVVEGSFI YKGGKIYKVP
STETEALASN LMGMFEKRRF RKFLVFVANF DENDPKTFEG VDPQSTSMRD VYRKFDLGQD
VIDFTGHALA LYRTDDYLDQ PCLETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
LSAIYGGTYM LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYIPDR VRKAGQVIRI
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI AIASTTVETA
EPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGSESQVFC SCSYDATTHF ETTCNDIKDI
YKRMAGSAFD FENMKRKQND VFGEADQ