GDIA_MOUSE
ID GDIA_MOUSE Reviewed; 447 AA.
AC P50396; A2AMA8; Q3TBI9; Q8VHM3; Q91Y71; Q91Z41; Q96CX5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Rab GDP dissociation inhibitor alpha;
DE Short=Rab GDI alpha;
DE AltName: Full=Guanosine diphosphate dissociation inhibitor 1;
DE Short=GDI-1;
GN Name=Gdi1; Synonyms=Rabgdia;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11027356; DOI=10.1073/pnas.97.21.11587;
RA Ishizaki H., Miyoshi J., Kamiya H., Togawa A., Tanaka M., Sasaki T.,
RA Endo K., Mizoguchi A., Ozawa S., Takai Y.;
RT "Role of rab GDP dissociation inhibitor alpha in regulating plasticity of
RT hippocampal neurotransmission.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11587-11592(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvEv;
RA D'Adamo P., Welzl H., Papadimitriou S., Raffaele di Barletta M.,
RA Tiveron C., Tatangelo L., Chapman P.F., Knevett S.G., Ramsay M.F.,
RA Valtorta F., Leoni C., Menegon A., Wolfer D.P., Lipp H.-P., Toniolo D.;
RT "Knockout mice carrying a deletion of the mental retardation gene Gdi1 show
RT impaired associative memory and inappropriate social behavior.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, and Mammary tumor;
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 [6]
RP PROTEIN SEQUENCE OF 36-54; 56-68; 104-112; 119-137; 143-169; 174-208;
RP 211-218; 222-240; 300-328; 349-379 AND 424-447, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 125-447.
RC STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RX PubMed=7513052; DOI=10.1128/mcb.14.5.3459-3468.1994;
RA Shisheva A., Suedhof T.C., Czech M.P.;
RT "Cloning, characterization, and expression of a novel GDP dissociation
RT inhibitor isoform from skeletal muscle.";
RL Mol. Cell. Biol. 14:3459-3468(1994).
RN [8]
RP INTERACTION WITH RAB10.
RX PubMed=19570034; DOI=10.1042/bj20090624;
RA Chen Y., Deng Y., Zhang J., Yang L., Xie X., Xu T.;
RT "GDI-1 preferably interacts with Rab10 in insulin-stimulated GLUT4
RT translocation.";
RL Biochem. J. 422:229-235(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins
CC by inhibiting the dissociation of GDP from them, and the subsequent
CC binding of GTP to them. Promotes the dissociation of GDP-bound Rab
CC proteins from the membrane and inhibits their activation. Promotes the
CC dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes.
CC -!- SUBUNIT: Interacts with RHOH (By similarity). Interacts with the non-
CC phosphorylated forms of RAB1A, RAB3A, RAB5A, RAB5B, RAB5C, RAB8A,
CC RAB8B, RAB12, RAB35, and RAB43 (By similarity). Interacts with RAB10
CC (PubMed:19570034). {ECO:0000250|UniProtKB:P31150,
CC ECO:0000269|PubMed:19570034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus, trans-
CC Golgi network {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: High expression in brain, lower in other tissues.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR EMBL; AF251042; AAK49815.1; -; mRNA.
DR EMBL; AF441240; AAL60197.1; -; Genomic_DNA.
DR EMBL; AK028880; BAC26169.1; -; mRNA.
DR EMBL; AK156224; BAE33632.1; -; mRNA.
DR EMBL; AK171216; BAE42320.1; -; mRNA.
DR EMBL; AL807376; CAM24345.1; -; Genomic_DNA.
DR EMBL; BC010220; AAH10220.1; -; mRNA.
DR EMBL; BC013758; AAH13758.1; -; mRNA.
DR EMBL; BC037598; AAH37598.1; -; mRNA.
DR EMBL; U07950; AAB16907.1; -; mRNA.
DR CCDS; CCDS30227.1; -.
DR PIR; C56024; C56024.
DR RefSeq; NP_034403.1; NM_010273.4.
DR AlphaFoldDB; P50396; -.
DR SMR; P50396; -.
DR BioGRID; 199890; 17.
DR IntAct; P50396; 9.
DR MINT; P50396; -.
DR STRING; 10090.ENSMUSP00000015435; -.
DR iPTMnet; P50396; -.
DR PhosphoSitePlus; P50396; -.
DR SwissPalm; P50396; -.
DR EPD; P50396; -.
DR jPOST; P50396; -.
DR MaxQB; P50396; -.
DR PaxDb; P50396; -.
DR PeptideAtlas; P50396; -.
DR PRIDE; P50396; -.
DR ProteomicsDB; 271207; -.
DR Antibodypedia; 4564; 401 antibodies from 33 providers.
DR DNASU; 14567; -.
DR Ensembl; ENSMUST00000015435; ENSMUSP00000015435; ENSMUSG00000015291.
DR GeneID; 14567; -.
DR KEGG; mmu:14567; -.
DR UCSC; uc009tom.2; mouse.
DR CTD; 2664; -.
DR MGI; MGI:99846; Gdi1.
DR VEuPathDB; HostDB:ENSMUSG00000015291; -.
DR eggNOG; KOG1439; Eukaryota.
DR GeneTree; ENSGT00950000182994; -.
DR HOGENOM; CLU_021695_0_0_1; -.
DR InParanoid; P50396; -.
DR OMA; DHYGGES; -.
DR OrthoDB; 763627at2759; -.
DR PhylomeDB; P50396; -.
DR TreeFam; TF300449; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 14567; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Gdi1; mouse.
DR PRO; PR:P50396; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P50396; protein.
DR Bgee; ENSMUSG00000015291; Expressed in embryonic brain and 259 other tissues.
DR ExpressionAtlas; P50396; baseline and differential.
DR Genevisible; P50396; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0032482; P:Rab protein signal transduction; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; ISO: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 Cytoplasm; Direct protein sequencing; Golgi apparatus; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..447
FT /note="Rab GDP dissociation inhibitor alpha"
FT /id="PRO_0000056673"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 58
FT /note="I -> M (in Ref. 1; AAK49815 and 3; BAE33632/
FT BAE42320)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="A -> R (in Ref. 7; AAB16907)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="N -> T (in Ref. 1; AAK49815)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="D -> E (in Ref. 7; AAB16907)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="P -> S (in Ref. 2; AAL60197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50522 MW; F7B9BC942B35DF58 CRC64;
MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE ELYKRFQILE
GPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVVEGSFV YKGGKIYKVP
STETEALASN LMGMFEKRRF RKFLVFVANF DENDPKTFEG VDPQNTSMRD VYRKFDLGQD
VIDFTGHALA LYRTDDYLDQ PCLETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
LSAIYGGTYM LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYIPDR VQKAGQVIRI
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI AIASTTVETA
EPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGSESQVFC SCSYDATTHF ETTCNDIKDI
YKRMAGSAFD FENMKRKQND VFGEADQ
