GDIB_RAT
ID GDIB_RAT Reviewed; 445 AA.
AC P50399; Q6P797;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Rab GDP dissociation inhibitor beta;
DE Short=Rab GDI beta;
DE AltName: Full=GDI-3;
DE AltName: Full=Guanosine diphosphate dissociation inhibitor 2;
DE Short=GDI-2;
GN Name=Gdi2; Synonyms=Gdi3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8188702; DOI=10.1016/s0021-9258(17)36773-x;
RA Nishimura N., Nakamura H., Takai Y., Sano K.;
RT "Molecular cloning and characterization of two rab GDI species from rat
RT brain: brain-specific and ubiquitous types.";
RL J. Biol. Chem. 269:14191-14198(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 30-54 AND 58-74, AND CHARACTERIZATION.
RX PubMed=7779099; DOI=10.1006/bbrc.1995.1810;
RA Araki K., Nakanishi H., Hirano H., Kato M., Sasaki T., Takai Y.;
RT "Purification and characterization of Rab GDI beta from rat brain.";
RL Biochem. Biophys. Res. Commun. 211:296-305(1995).
RN [4]
RP PROTEIN SEQUENCE OF 80-98; 104-112; 119-137; 143-156; 175-193; 211-218;
RP 349-360 AND 365-402, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR EMBL; X74401; CAA52412.1; -; mRNA.
DR EMBL; BC061767; AAH61767.1; -; mRNA.
DR PIR; B54091; B54091.
DR RefSeq; NP_058972.2; NM_017276.2.
DR AlphaFoldDB; P50399; -.
DR SMR; P50399; -.
DR BioGRID; 248284; 3.
DR IntAct; P50399; 2.
DR MINT; P50399; -.
DR STRING; 10116.ENSRNOP00000024952; -.
DR iPTMnet; P50399; -.
DR PhosphoSitePlus; P50399; -.
DR SwissPalm; P50399; -.
DR jPOST; P50399; -.
DR PaxDb; P50399; -.
DR PRIDE; P50399; -.
DR Ensembl; ENSRNOT00000109674; ENSRNOP00000082980; ENSRNOG00000018091.
DR GeneID; 29662; -.
DR KEGG; rno:29662; -.
DR UCSC; RGD:61802; rat.
DR CTD; 2665; -.
DR RGD; 61802; Gdi2.
DR eggNOG; KOG1439; Eukaryota.
DR GeneTree; ENSGT00950000182994; -.
DR HOGENOM; CLU_021695_0_0_1; -.
DR InParanoid; P50399; -.
DR OMA; YIPTDLG; -.
DR OrthoDB; 763627at2759; -.
DR PhylomeDB; P50399; -.
DR TreeFam; TF300449; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P50399; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000018091; Expressed in spleen and 19 other tissues.
DR Genevisible; P50399; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; IDA:RGD.
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; TAS:RGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IEP:RGD.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; GTPase activation;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..445
FT /note="Rab GDP dissociation inhibitor beta"
FT /id="PRO_0000056683"
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:0007744|PubMed:22673903"
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"
FT CONFLICT 205..211
FT /note="TINRIKL -> RLTELNF (in Ref. 1; CAA52412)"
FT /evidence="ECO:0000305"
FT CONFLICT 231..232
FT /note="LG -> PW (in Ref. 1; CAA52412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 50537 MW; 483B7C7456B30525 CRC64;
MNEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDQNPYYG GESASITPLE DLYKRFKLPG
QPPASMGRGR DWNVDLIPKF LMANGQLVKM LLFTEVTRYM DFKVIEGSFV YKGGKIYKVP
STEAEALASS LMGLFEKRRF RKFLVYVANF DEKDPRTFEG VDPKKTSMRD VYKKFDLGQD
VIDFTGHSLA LYRTDDYLDQ PCCETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
LSAIYGGTYM LNKPIEEIIV QNGKVVGVKS EGEIARCKQL ICDPSYVKDR VEKVGQVIRV
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISFA HNVAAQGKYI AIVSTTVETK
EPEKEIRPAL ELLEPIEQKF VSISDLFVPK DLGTDSQIFI SRAYDATTHF ETTCDDIKDI
YKRMTGSEFD FEEMKRKKND IYGED
