GDIB_MOUSE
ID GDIB_MOUSE Reviewed; 445 AA.
AC Q61598; Q541Z9; Q8C530; Q9D8M9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7782346; DOI=10.1074/jbc.270.24.14801;
RA Janoueix-Lerosey I., Jollivet F., Camonis J., Marche P.N., Goud B.;
RT "Two-hybrid system screen with the small GTP-binding protein Rab6.
RT Identification of a novel mouse GDP dissociation inhibitor isoform and two
RT other potential partners of Rab6.";
RL J. Biol. Chem. 270:14801-14808(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Colon, Liver, Mammary gland, Medulla oblongata,
RC Pancreas, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 143-156; 175-193 AND 222-240, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-57, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP INTERACTION WITH DZIP1 AND RAB8A.
RX PubMed=25860027; DOI=10.1371/journal.pbio.1002129;
RA Zhang B., Zhang T., Wang G., Wang G., Chi W., Jiang Q., Zhang C.;
RT "GSK3beta-Dzip1-Rab8 cascade regulates ciliogenesis after mitosis.";
RL PLoS Biol. 13:e1002129-e1002129(2015).
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 (By similarity). Interacts with the non-
CC phosphorylated forms of RAB3A, RAB3B, RAB3C, RAB5A, RAB5B, RAB5C,
CC RAB8B, RAB10, RAB12, RAB35, and RAB43; binds RAB3D to a lesser extent
CC (By similarity). Interacts with RAB8A (GDP-bound inactive form);
CC prevents RAB8A activation (PubMed:25860027). Interacts with DZIP1;
CC negatively regulates the interaction of GDI2 with GDP-bound RAB8A
CC (PubMed:25860027). {ECO:0000250|UniProtKB:P50395,
CC ECO:0000269|PubMed:25860027}.
CC -!- INTERACTION:
CC Q61598; Q8BMD2: Dzip1; NbExp=2; IntAct=EBI-6665490, EBI-7089968;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61598-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61598-2; Sequence=VSP_010579;
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR EMBL; L36314; AAA78786.1; -; mRNA.
DR EMBL; AK007871; BAB25321.1; -; mRNA.
DR EMBL; AK078144; BAC37145.1; -; mRNA.
DR EMBL; AK079690; BAC37725.1; -; mRNA.
DR EMBL; AK090083; BAC41085.1; -; mRNA.
DR EMBL; AK143633; BAE25473.1; -; mRNA.
DR EMBL; AK149958; BAE29194.1; -; mRNA.
DR EMBL; AK152250; BAE31072.1; -; mRNA.
DR EMBL; AK153381; BAE31947.1; -; mRNA.
DR EMBL; AK159734; BAE35328.1; -; mRNA.
DR EMBL; AK166317; BAE38700.1; -; mRNA.
DR EMBL; AK169299; BAE41055.1; -; mRNA.
DR EMBL; BC055341; AAH55341.1; -; mRNA.
DR CCDS; CCDS36581.1; -. [Q61598-1]
DR PIR; A56024; A56024.
DR PIR; C56956; C56956.
DR RefSeq; NP_032138.3; NM_008112.4. [Q61598-1]
DR AlphaFoldDB; Q61598; -.
DR SMR; Q61598; -.
DR BioGRID; 199892; 19.
DR DIP; DIP-348N; -.
DR IntAct; Q61598; 8.
DR MINT; Q61598; -.
DR STRING; 10090.ENSMUSP00000062996; -.
DR iPTMnet; Q61598; -.
DR PhosphoSitePlus; Q61598; -.
DR SwissPalm; Q61598; -.
DR REPRODUCTION-2DPAGE; Q61598; -.
DR CPTAC; non-CPTAC-3811; -.
DR EPD; Q61598; -.
DR jPOST; Q61598; -.
DR MaxQB; Q61598; -.
DR PaxDb; Q61598; -.
DR PeptideAtlas; Q61598; -.
DR PRIDE; Q61598; -.
DR ProteomicsDB; 267788; -. [Q61598-1]
DR ProteomicsDB; 267789; -. [Q61598-2]
DR Antibodypedia; 10649; 263 antibodies from 28 providers.
DR DNASU; 14569; -.
DR Ensembl; ENSMUST00000059515; ENSMUSP00000062996; ENSMUSG00000021218. [Q61598-2]
DR Ensembl; ENSMUST00000223396; ENSMUSP00000152454; ENSMUSG00000021218. [Q61598-1]
DR GeneID; 14569; -.
DR KEGG; mmu:14569; -.
DR UCSC; uc007piu.1; mouse. [Q61598-1]
DR UCSC; uc011yvx.1; mouse. [Q61598-2]
DR CTD; 2665; -.
DR MGI; MGI:99845; Gdi2.
DR VEuPathDB; HostDB:ENSMUSG00000021218; -.
DR eggNOG; KOG1439; Eukaryota.
DR GeneTree; ENSGT00950000182994; -.
DR HOGENOM; CLU_021695_0_0_1; -.
DR InParanoid; Q61598; -.
DR OMA; YIPTDLG; -.
DR PhylomeDB; Q61598; -.
DR TreeFam; TF300449; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 14569; 10 hits in 71 CRISPR screens.
DR ChiTaRS; Gdi2; mouse.
DR PRO; PR:Q61598; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61598; protein.
DR Bgee; ENSMUSG00000021218; Expressed in saccule of membranous labyrinth and 265 other tissues.
DR ExpressionAtlas; Q61598; baseline and differential.
DR Genevisible; Q61598; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IPI:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
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; IPI:MGI.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW GTPase activation; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..445
FT /note="Rab GDP dissociation inhibitor beta"
FT /id="PRO_0000056680"
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:0007744|PubMed:23806337"
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"
FT VAR_SEQ 16..51
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010579"
FT CONFLICT 156
FT /note="R -> K (in Ref. 2; BAC37725)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="I -> N (in Ref. 2; BAB25321)"
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
