ID   GDIB_CANLF              Reviewed;         445 AA.
AC   O97556;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Rab GDP dissociation inhibitor beta;
DE            Short=Rab GDI beta;
DE   AltName: Full=Guanosine diphosphate dissociation inhibitor 2;
DE            Short=GDI-2;
GN   Name=GDI2;
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].
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: GDP-dissociation inhibitor preventing the GDP to GTP exchange
CC       of most Rab proteins. By keeping these small GTPases in their inactive
CC       GDP-bound form regulates intracellular membrane trafficking. Negatively
CC       regulates protein transport to the cilium and ciliogenesis through the
CC       inhibition of RAB8A. {ECO:0000250|UniProtKB:P50395}.
CC   -!- SUBUNIT: Interacts with RHOH. Interacts with the GDP-bound forms of
CC       RAB3A, RAB3B, RAB3C, RAB5A, RAB5B, RAB5C, RAB8B, RAB10, RAB12, RAB35,
CC       and RAB43; binds RAB3D to a lesser extent. Interacts with RAB8A (GDP-
CC       bound inactive form); prevents RAB8A activation. Interacts with DZIP1;
CC       negatively regulates the interaction of GDI2 with GDP-bound RAB8A.
CC       {ECO:0000250|UniProtKB:P50395}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR   EMBL; AF027361; AAD04247.1; -; mRNA.
DR   RefSeq; NP_001003184.1; NM_001003184.1.
DR   AlphaFoldDB; O97556; -.
DR   SMR; O97556; -.
DR   STRING; 9615.ENSCAFP00000007805; -.
DR   PaxDb; O97556; -.
DR   GeneID; 403818; -.
DR   KEGG; cfa:403818; -.
DR   CTD; 2665; -.
DR   eggNOG; KOG1439; Eukaryota.
DR   InParanoid; O97556; -.
DR   OrthoDB; 763627at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IBA:GO_Central.
DR   GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR   GO; GO:1903565; P:negative regulation of protein localization to cilium; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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   Acetylation; Cytoplasm; GTPase activation; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..445
FT                   /note="Rab GDP dissociation inhibitor beta"
FT                   /id="PRO_0000056678"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P50395"
FT   MOD_RES         57
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61598"
FT   MOD_RES         112
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50395"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50399"
FT   MOD_RES         269
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50395"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50395"
SQ   SEQUENCE   445 AA;  50322 MW;  9CE6B5407A3B0400 CRC64;
     MNEEYDVIVL GTGLTECILS GIMTVNGKKV LHMDRNPYYG GESASITPLE DLYKRFKIPG
     APPASMGRGR DWNLDLIPKF LMANGQLVKM LLYTEVTRYL DFKVTEGSFV YKGGKIYKVP
     STEAEALASS LMGLFEKRRF RKFLVYVANF DEKDPRTFEG IDPKKTAIGE VYKKFDLGQD
     VIDFTGHALA LYRTDDYLDQ PCCETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
     LSAIYGGTYM LNKPIEEIIV QNGKVIGVKS EGEVARCKQL ICDPSYVKDR VEKVGQVIRV
     ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISSA HNVAAQGKYI AIVSTTAETK
     EPEKEIRPAL ELLEPIEQKF VSISDLLVPK DLGTESQIFI SRTYDATTHF ETTCDDIKNI
     YKRMTGSEFD FEEMKRKKND IYGED