ID   GDIB_PONAB              Reviewed;         445 AA.
AC   Q5RCE1;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858330; CAH90566.1; -; mRNA.
DR   RefSeq; NP_001125301.1; NM_001131829.2.
DR   AlphaFoldDB; Q5RCE1; -.
DR   SMR; Q5RCE1; -.
DR   STRING; 9601.ENSPPYP00000002386; -.
DR   PRIDE; Q5RCE1; -.
DR   GeneID; 100172200; -.
DR   KEGG; pon:100172200; -.
DR   CTD; 2665; -.
DR   eggNOG; KOG1439; Eukaryota.
DR   InParanoid; Q5RCE1; -.
DR   OrthoDB; 763627at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
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   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_0000056682"
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;  50664 MW;  F548E3B0977A52FC CRC64;
     MNEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESASITPLE DLYKRYKIPG
     SPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVTEGSFV YKGGKIYKVP
     STEAEALASS LMGLFEKRRF RKFLVYVANF DEKDPRTFEG IDPKKTTMRD VYKKFDLGQD
     VIDFTGHALA LYRTDDYLDQ PCYETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
     LSAIYGGTYM LNKPIEEIIV QNGKVIGVKS EGEIARCKQL ICDPSYVKDR VEKVGQVIRV
     ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISFA HNVAAQGKYI AIVSTTVETK
     EPEKEIRPAL ELLEPIEQKF VSISDLLVPK DLGTESLIFI SRTYDATTHF ETTCDDIKNI
     YKRMTGSEFD FEEMKRKKND IYGED