GID2_ARATH
ID GID2_ARATH Reviewed; 151 AA.
AC Q9STX3; Q8LAQ7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=F-box protein GID2;
DE AltName: Full=Protein SLEEPY 1;
GN Name=GID2; Synonyms=SLY1; OrderedLocusNames=At4g24210; ORFNames=T22A6.40;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12724538; DOI=10.1105/tpc.010827;
RA McGinnis K.M., Thomas S.G., Soule J.D., Strader L.C., Zale J.M., Sun T.-P.,
RA Steber C.M.;
RT "The Arabidopsis SLEEPY1 gene encodes a putative F-box subunit of an SCF E3
RT ubiquitin ligase.";
RL Plant Cell 15:1120-1130(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, COMPONENT OF A SCF COMPLEX, INTERACTION
RP WITH GAI AND RGA, AND MUTAGENESIS OF GLU-138.
RX PubMed=15155881; DOI=10.1105/tpc.020958;
RA Dill A., Thomas S.G., Hu J., Steber C.M., Sun T.-P.;
RT "The Arabidopsis F-box protein SLEEPY1 targets gibberellin signaling
RT repressors for gibberellin-induced degradation.";
RL Plant Cell 16:1392-1405(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, COMPONENT OF A SCF COMPLEX WITH SKP1B AND
RP CUL1, INTERACTION WITH SKP1A; SKP1B; GAI AND RGA, AND MUTAGENESIS OF
RP GLU-138.
RX PubMed=15161962; DOI=10.1105/tpc.021386;
RA Fu X., Richards D.E., Fleck B., Xie D., Burton N., Harberd N.P.;
RT "The Arabidopsis mutant sleepy1gar2-1 protein promotes plant growth by
RT increasing the affinity of the SCFSLY1 E3 ubiquitin ligase for DELLA
RT protein substrates.";
RL Plant Cell 16:1406-1418(2004).
RN [8]
RP INTERACTION WITH GAI; RGA; RGL1 AND RGL3.
RX PubMed=15173565; DOI=10.1104/pp.104.039578;
RA Tyler L., Thomas S.G., Hu J., Dill A., Alonso J.M., Ecker J.R., Sun T.-P.;
RT "Della proteins and gibberellin-regulated seed germination and floral
RT development in Arabidopsis.";
RL Plant Physiol. 135:1008-1019(2004).
RN [9]
RP FUNCTION.
RX PubMed=15308775; DOI=10.1073/pnas.0404287101;
RA Strader L.C., Ritchie S., Soule J.D., McGinnis K.M., Steber C.M.;
RT "Recessive-interfering mutations in the gibberellin signaling gene SLEEPY1
RT are rescued by overexpression of its homologue, SNEEZY.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12771-12776(2004).
CC -!- FUNCTION: Essential component of the SCF-type E3 ligase complex,
CC SCF(GID2), a complex that positively regulates the gibberellin
CC signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex
CC mediates the ubiquitination and subsequent degradation of DELLA
CC proteins (GAI, RGA and RGL2), some repressors of the gibberellin
CC pathway, leading to activate the pathway. {ECO:0000269|PubMed:12724538,
CC ECO:0000269|PubMed:15155881, ECO:0000269|PubMed:15161962,
CC ECO:0000269|PubMed:15308775}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of some SCF(GID2) complex, which consist of SKP1B, CUL1
CC cullin, GID2/SLY1 and some RING box protein. Interacts directly with
CC SKP1A and SKP1B. Interacts directly with DELLA proteins GAI, RGA, RGL1,
CC RGL3 and probably RGL2. May have a higher affinity for phosphorylated
CC DELLA proteins. {ECO:0000269|PubMed:15155881,
CC ECO:0000269|PubMed:15161962, ECO:0000269|PubMed:15173565}.
CC -!- INTERACTION:
CC Q9STX3; Q9LQT8: GAI; NbExp=7; IntAct=EBI-619033, EBI-963606;
CC Q9STX3; Q9MAA7: GID1A; NbExp=3; IntAct=EBI-619033, EBI-963597;
CC Q9STX3; Q9LYC1: GID1B; NbExp=3; IntAct=EBI-619033, EBI-963686;
CC Q9STX3; Q9SLH3: RGA; NbExp=4; IntAct=EBI-619033, EBI-963624;
CC Q9STX3; Q9FHW7: SKP1B; NbExp=3; IntAct=EBI-619033, EBI-604076;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15155881,
CC ECO:0000269|PubMed:15161962}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including rosette
CC leaves, green siliques, flowers, stems, cauline leaves and seedlings.
CC {ECO:0000269|PubMed:12724538}.
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DR EMBL; AL078637; CAB45056.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79331.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84867.1; -; Genomic_DNA.
DR EMBL; BT004192; AAO42210.1; -; mRNA.
DR EMBL; BT005395; AAO63815.1; -; mRNA.
DR EMBL; AY087672; AAM65209.1; -; mRNA.
DR PIR; T09884; T09884.
DR RefSeq; NP_194152.1; NM_118554.3.
DR AlphaFoldDB; Q9STX3; -.
DR BioGRID; 13811; 13.
DR IntAct; Q9STX3; 14.
DR STRING; 3702.AT4G24210.1; -.
DR PaxDb; Q9STX3; -.
DR PRIDE; Q9STX3; -.
DR ProteomicsDB; 222349; -.
DR DNASU; 828522; -.
DR EnsemblPlants; AT4G24210.1; AT4G24210.1; AT4G24210.
DR GeneID; 828522; -.
DR Gramene; AT4G24210.1; AT4G24210.1; AT4G24210.
DR KEGG; ath:AT4G24210; -.
DR Araport; AT4G24210; -.
DR TAIR; locus:2135917; AT4G24210.
DR eggNOG; ENOG502RYCP; Eukaryota.
DR HOGENOM; CLU_111348_0_0_1; -.
DR InParanoid; Q9STX3; -.
DR OMA; NIGCGQN; -.
DR OrthoDB; 1387635at2759; -.
DR PhylomeDB; Q9STX3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9STX3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STX3; baseline and differential.
DR Genevisible; Q9STX3; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IPI:TAIR.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0010162; P:seed dormancy process; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR045118; FBXO9/FBXO48.
DR PANTHER; PTHR12874; PTHR12874; 2.
DR Pfam; PF00646; F-box; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 1: Evidence at protein level;
KW Gibberellin signaling pathway; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..151
FT /note="F-box protein GID2"
FT /id="PRO_0000119962"
FT DOMAIN 29..75
FT /note="F-box"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 138
FT /note="E->K: In gar2-1/sly1-d; gain of function allele that
FT promotes plant growth by increasing the affinity with DELLA
FT protein substrates."
FT /evidence="ECO:0000269|PubMed:15155881,
FT ECO:0000269|PubMed:15161962"
FT CONFLICT 3
FT /note="R -> L (in Ref. 4; AAM65209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 151 AA; 17455 MW; 4404DE81E9DFDA9D CRC64;
MKRSTTDSDL AGDAHNETNK KMKSTEEEEI GFSNLDENLV YEVLKHVDAK TLAMSSCVSK
IWHKTAQDER LWELICTRHW TNIGCGQNQL RSVVLALGGF RRLHSLYLWP LSKPNPRARF
GKDELKLTLS LLSIRYYEKM SFTKRPLPES K
