GDI1_ARATH
ID GDI1_ARATH Reviewed; 445 AA.
AC Q96254; B9DFX1; Q8LBY8; Q8VZB4; Q96284;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Guanosine nucleotide diphosphate dissociation inhibitor 1;
DE Short=AtGDI1;
GN Name=GDI1; OrderedLocusNames=At2g44100; ORFNames=F6E13.23;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8953772; DOI=10.2307/3870414;
RA Ueda T., Matsuda N., Anai T., Tsukaya H., Uchimiya H., Nakano A.;
RT "An Arabidopsis gene isolated by a novel method for detecting genetic
RT interaction in yeast encodes the GDP dissociation inhibitor of Ara4
RT GTPase.";
RL Plant Cell 8:2079-2091(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9091322; DOI=10.1016/s0014-5793(97)00072-0;
RA Zarsky V., Cvrckova F., Bischoff F., Palme K.;
RT "At-GDI1 from Arabidopsis thaliana encodes a rab-specific GDP dissociation
RT inhibitor that complements the sec19 mutation of Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 403:303-308(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INTERACTION WITH RABA5C.
RX PubMed=10758485; DOI=10.1046/j.1365-313x.2000.00681.x;
RA Ueda T., Matsuda N., Uchimiya H., Nakano A.;
RT "Modes of interaction between the Arabidopsis Rab protein, Ara4, and its
RT putative regulator molecules revealed by a yeast expression system.";
RL Plant J. 21:341-349(2000).
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. {ECO:0000269|PubMed:8953772,
CC ECO:0000269|PubMed:9091322}.
CC -!- SUBUNIT: Interacts with the GDP-bound form of RABA5C (via C-terminus).
CC {ECO:0000269|PubMed:10758485}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96254-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96254-2; Sequence=VSP_053854, VSP_053855;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, stems, floral
CC buds and siliques. {ECO:0000269|PubMed:8953772,
CC ECO:0000269|PubMed:9091322}.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR EMBL; D83531; BAA11944.1; -; mRNA.
DR EMBL; Y07961; CAA69258.1; -; mRNA.
DR EMBL; AC004005; AAC23429.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10374.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10375.1; -; Genomic_DNA.
DR EMBL; AF361801; AAK32814.1; -; mRNA.
DR EMBL; AY050418; AAK91434.1; -; mRNA.
DR EMBL; AY065087; AAL38263.1; -; mRNA.
DR EMBL; AY113036; AAM47344.1; -; mRNA.
DR EMBL; AK316933; BAH19638.1; -; mRNA.
DR EMBL; AK226690; BAE98797.1; -; mRNA.
DR EMBL; AK227643; BAE99631.1; -; mRNA.
DR EMBL; AY086920; AAM64484.1; -; mRNA.
DR PIR; T00690; T00690.
DR RefSeq; NP_001078054.1; NM_001084585.2. [Q96254-2]
DR RefSeq; NP_181938.1; NM_129973.3. [Q96254-1]
DR AlphaFoldDB; Q96254; -.
DR SMR; Q96254; -.
DR BioGRID; 4352; 4.
DR IntAct; Q96254; 1.
DR STRING; 3702.AT2G44100.1; -.
DR iPTMnet; Q96254; -.
DR MetOSite; Q96254; -.
DR PaxDb; Q96254; -.
DR PRIDE; Q96254; -.
DR ProteomicsDB; 221918; -. [Q96254-1]
DR EnsemblPlants; AT2G44100.1; AT2G44100.1; AT2G44100. [Q96254-1]
DR EnsemblPlants; AT2G44100.2; AT2G44100.2; AT2G44100. [Q96254-2]
DR GeneID; 819016; -.
DR Gramene; AT2G44100.1; AT2G44100.1; AT2G44100. [Q96254-1]
DR Gramene; AT2G44100.2; AT2G44100.2; AT2G44100. [Q96254-2]
DR KEGG; ath:AT2G44100; -.
DR Araport; AT2G44100; -.
DR TAIR; locus:2051839; AT2G44100.
DR eggNOG; KOG1439; Eukaryota.
DR OMA; DHYGGES; -.
DR PhylomeDB; Q96254; -.
DR PRO; PR:Q96254; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q96254; baseline and differential.
DR Genevisible; Q96254; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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: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 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Reference proteome.
FT CHAIN 1..445
FT /note="Guanosine nucleotide diphosphate dissociation
FT inhibitor 1"
FT /id="PRO_0000425807"
FT VAR_SEQ 429..431
FT /note="ELD -> VMF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_053854"
FT VAR_SEQ 432..445
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_053855"
FT CONFLICT 233
FT /note="E -> K (in Ref. 5; AAL38263)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="C -> F (in Ref. 8; AAM64484)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="L -> P (in Ref. 5; AAL38263)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="A -> P (in Ref. 2; CAA69258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 49819 MW; 228451B5A55C7545 CRC64;
MDEEYEVIVL GTGLKECILS GLLSVDGLKV LHMDRNDYYG GESTSLNLNQ LWKKFRGEEK
APAHLGSSRD YNVDMMPKFM MANGKLVRVL IHTDVTKYLS FKAVDGSYVF VQGKVQKVPA
TPMEALKSPL MGIFEKRRAG KFFSYVQEYD EKDPKTHDGM DLRRVTTKDL IAKFGLKEDT
IDFIGHAVAL HCNDNHLHQP AYDTVMRMKL YAESLARFQG GSPYIYPLYG LGELPQAFAR
LSAVYGGTYM LNKPECKVEF DEEGKVSGVT SEGETAKCKK VVCDPSYLTN KVRKIGRVAR
AIAIMSHPIP NTNDSQSVQV ILPQKQLGRK SDMYVFCCSY SHNVAPKGKF IAFVSTDAET
DNPQTELQPG IDLLGPVDEL FFDIYDRYEP VNEPTLDNCF ISTSYDATTH FDTTVVDVLN
MYKLITGKEL DLSVDLNAAS AAEEE
