Q9STX3 (GID2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
F-box protein GID2

Alternative name(s):
Protein SLEEPY 1

Gene names

Name:	GID2
Synonyms:	SLY1
Ordered Locus Names:	At4g24210
ORF Names:	T22A6.40

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to activate the pathway. Ref.5 Ref.6 Ref.7 Ref.9
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Part of some SCF(GID2) complex, which consist of SKP1B, CUL1 cullin, GID2/SLY1 and some RING box protein. Interacts directly with SKP1A and SKP1B. Interacts directly with DELLA proteins GAI, RGA, RGL1, RGL3 and probably RGL2. May have a higher affinity for phosphorylated DELLA proteins. Ref.6 Ref.7 Ref.8
Subcellular location	Nucleus Ref.6 Ref.7.
Tissue specificity	Expressed in all tissues tested, including rosette leaves, green siliques, flowers, stems, cauline leaves and seedlings. Ref.5
Sequence similarities	Contains 1 F-box domain.

Ontologies

Keywords
Biological process	Gibberellin signaling pathway Ubl conjugation pathway
Cellular component	Nucleus
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	gibberellic acid mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW seed dormancy process Inferred from mutant phenotype. Source: TAIR seed germination Inferred from mutant phenotype. Source: TAIR
Cellular component	SCF ubiquitin ligase complex Inferred from physical interaction Ref.7. Source: TAIR nucleus Inferred from direct assay Ref.6. Source: TAIR
Molecular function	protein binding Inferred from physical interaction Ref.6Ref.7. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GAI	Q9LQT8	4	EBI-619033,EBI-963606
GID1A	Q9MAA7	3	EBI-619033,EBI-963597
GID1B	Q9LYC1	3	EBI-619033,EBI-963686
RGA	Q9SLH3	4	EBI-619033,EBI-963624
SKP1B	Q9FHW7	3	EBI-619033,EBI-604076

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 151	151	F-box protein GID2		PRO_0000119962
Regions
	Domain	29 – 75	47	F-box
Experimental info
	Mutagenesis	138	1	E → K in gar2-1/sly1-d; gain of function allele that promotes plant growth by increasing the affinity with DELLA protein substrates. Ref.6 Ref.7
	Sequence conflict	3	1	R → L in AAM65209. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9STX3 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 4404DE81E9DFDA9D	FASTA	151	17,455
	10 20 30 40 50 60 MKRSTTDSDL AGDAHNETNK KMKSTEEEEI GFSNLDENLV YEVLKHVDAK TLAMSSCVSK 70 80 90 100 110 120 IWHKTAQDER LWELICTRHW TNIGCGQNQL RSVVLALGGF RRLHSLYLWP LSKPNPRARF 130 140 150 GKDELKLTLS LLSIRYYEKM SFTKRPLPES K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The Arabidopsis SLEEPY1 gene encodes a putative F-box subunit of an SCF E3 ubiquitin ligase." McGinnis K.M., Thomas S.G., Soule J.D., Strader L.C., Zale J.M., Sun T.-P., Steber C.M. Plant Cell 15:1120-1130(2003) [PubMed: 12724538] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[6]	"The Arabidopsis F-box protein SLEEPY1 targets gibberellin signaling repressors for gibberellin-induced degradation." Dill A., Thomas S.G., Hu J., Steber C.M., Sun T.-P. Plant Cell 16:1392-1405(2004) [PubMed: 15155881] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, COMPONENT OF A SCF COMPLEX, INTERACTION WITH GAI AND RGA, MUTAGENESIS OF GLU-138.
[7]	"The Arabidopsis mutant sleepy1gar2-1 protein promotes plant growth by increasing the affinity of the SCFSLY1 E3 ubiquitin ligase for DELLA protein substrates." Fu X., Richards D.E., Fleck B., Xie D., Burton N., Harberd N.P. Plant Cell 16:1406-1418(2004) [PubMed: 15161962] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, COMPONENT OF A SCF COMPLEX WITH SKP1B AND CUL1, INTERACTION WITH SKP1A; SKP1B; GAI AND RGA, MUTAGENESIS OF GLU-138.
[8]	"Della proteins and gibberellin-regulated seed germination and floral development in Arabidopsis." Tyler L., Thomas S.G., Hu J., Dill A., Alonso J.M., Ecker J.R., Sun T.-P. Plant Physiol. 135:1008-1019(2004) [PubMed: 15173565] [Abstract] Cited for: INTERACTION WITH GAI; RGA; RGL1 AND RGL3.
[9]	"Recessive-interfering mutations in the gibberellin signaling gene SLEEPY1 are rescued by overexpression of its homologue, SNEEZY." Strader L.C., Ritchie S., Soule J.D., McGinnis K.M., Steber C.M. Proc. Natl. Acad. Sci. U.S.A. 101:12771-12776(2004) [PubMed: 15308775] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Web resources

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL078637 Genomic DNA. Translation: CAB45056.1. AL161561 Genomic DNA. Translation: CAB79331.1. CP002687 Genomic DNA. Translation: AEE84867.1. BT004192 mRNA. Translation: AAO42210.1. BT005395 mRNA. Translation: AAO63815.1. AY087672 mRNA. Translation: AAM65209.1.
IPI	IPI00537916.
PIR	T09884.
RefSeq	NP_194152.1. NM_118554.2.
UniGene	At.43332.
3D structure databases
ProteinModelPortal	Q9STX3.
SMR	Q9STX3. Positions 31-77.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9STX3. 12 interactions.
STRING	Q9STX3.
Proteomic databases
PRIDE	Q9STX3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G24210.1; AT4G24210.1; AT4G24210.
GeneID	828522.
GenomeReviews	Gene locus AT4G24210 in contig CT486007_GR.
KEGG	ath:AT4G24210.
NMPDR	fig|3702.1.peg.20308.
Organism-specific databases
TAIR	At4g24210.
Phylogenomic databases
GeneTree	EPGT00050000012518.
HOGENOM	HBG749593.
InParanoid	Q9STX3.
OMA	LWELICT.
PhylomeDB	Q9STX3.
ProtClustDB	CLSN2685400.
Gene expression databases
Genevestigator	Q9STX3.
GermOnline	AT4G24210. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001810. F-box_dom_cyclin-like. IPR022364. F-box_dom_Skp2-like. [Graphical view]
KO	K14495.
Pfam	PF00646. F-box. 1 hit. [Graphical view]
SMART	SM00256. FBOX. 1 hit. [Graphical view]
SUPFAM	SSF81383. F-box_dom_Skp2-like. 1 hit.
PROSITE	PS50181. FBOX. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GID2_ARATH

Accession

Primary (citable) accession number: Q9STX3
Secondary accession number(s): Q8LAQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program