GDIB_PIG
ID GDIB_PIG Reviewed; 445 AA.
AC Q6Q7J2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15625692; DOI=10.1002/mrd.20204;
RA Hwang K.C., Lee H.Y., Cui X.S., Kim J.H., Kim N.H.;
RT "Identification of maternal mRNAs in porcine parthenotes at the 2-cell
RT stage: a comparison with the blastocyst stage.";
RL Mol. Reprod. Dev. 70:314-323(2005).
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; AY553929; AAS76550.1; -; mRNA.
DR RefSeq; NP_001001643.1; NM_001001643.1.
DR AlphaFoldDB; Q6Q7J2; -.
DR SMR; Q6Q7J2; -.
DR STRING; 9823.ENSSSCP00000011877; -.
DR PaxDb; Q6Q7J2; -.
DR PeptideAtlas; Q6Q7J2; -.
DR PRIDE; Q6Q7J2; -.
DR GeneID; 414427; -.
DR KEGG; ssc:414427; -.
DR CTD; 2665; -.
DR eggNOG; KOG1439; Eukaryota.
DR InParanoid; Q6Q7J2; -.
DR OrthoDB; 763627at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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_0000056681"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P50395"
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; 50268 MW; 1488CFA890E6688A CRC64;
MNEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESASITPLE DLYKRFNIPG
APPASMGRGR DWNVDLIPKF LMANGQLVKM LLFTEVTRYL DFKVTEGSFV YKGGKIYKVP
STEAEALASS LMGLFEKRRF RKFLVYVANF DENDPRTFEG VDPKKTAMRE VYKKFDLGQD
VIDFTGHALA LYRTDDYLDQ PCCETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
LSAIYGGTYM LNKPIEEIIV QNGKVIGVKS EGEIARCKQL ICDPSYVKDR VEKVGQVIRV
ICILSHPIKN TSDANSCQII IPQNQVNRKS DIYVCMISSA HNVAAQGKYI AIASTTVETK
EPEKEIRPAL ELLKPIEQKF VSISDLLVPK DLGTDSQIFI SRTYDATTHF ETTCGDIKDI
YKRMTGSEFD FEEMKRKKND IYGED