Q96301 (SPY_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY
EC=2.4.1.-

Gene names

Name:	SPY
Ordered Locus Names:	At3g11540
ORF Names:	F24K9.29

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	914 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable O-linked N-acetylglucosamine transferase (OGT) involved in various processes such as gibberellin (GA) signaling pathway and circadian clock. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by adding O-linked sugars to yet unknown proteins. Acts as a repressor of GA signaling pathway to inhibit hypocotyl elongation. Functions with GIGANTEA (GI) in pathways controlling flowering, circadian cotyledon movements and hypocotyl elongation. Acts as a light-regulated promoter of elongation via its interaction with GI. Acts as an activator of cytokinin signaling. Required with SEC for gamete and seed development. Its OGT activity has been proved in vitro but not in vivo. Ref.1 Ref.6 Ref.9 Ref.10 Ref.11
Catalytic activity	UDP-N-acetyl-D-glucosamine + peptide = UDP + N-acetyl-beta-D-glucosaminyl-peptide. Ref.5
Pathway	Protein modification; protein glycosylation.
Subunit structure	Homomultimer; via its TPR repeats. Interacts with GI. Ref.7 Ref.10
Subcellular location	Cytoplasm. Nucleus Ref.8.
Tissue specificity	Widely expressed. Present throughout the plant (at protein level). Ref.8
Developmental stage	Detected in all organs of the plant and at all stages of the life cycle. Detected 1 day after germination in the radicle just before its emergence from the seed. At 2.5 and 3 days after germination, expression in the young seedling is highest in the cotyledons and the root tip. At 3, 4 and 5 days, expression is also detectable in the hypocotyl. At 10 days of age, expression in the first pair of true leaves is reduced relative to the rest of the seedling. 2 days later, this difference disappears and the expression level is again fairly similar throughout the aboveground portion of the plant, with a higher intensity in the vegetative apex. This developmental regulation is not detected in leaves developing at later nodes. Older plants also display uniform expression throughout the vegetative organs, but this expression is less intense. In older seedlings, expression is observed throughout the root, particularly at the tip of the primary root and in lateral roots. Expression is also observed in trichomes and senescing leaves, and in inflorescence internodes, flowers. Expression is observed in the seeds and carpels of fully elongated siliques. Lower expression is also observed in expanding siliques and in the developing seeds in these siliques. Expression is also detected in the embryo of maturing seeds (after the disappearance of the endosperm) (at protein level). Ref.8
Domain	The TPR repeats mediate protein-protein interactions and are essential for its function. Expression of such repeats in plants accelerate flowering. Ref.7
Sequence similarities	Belongs to the O-GlcNAc transferase family. Contains 11 TPR repeats.
Sequence caution	The sequence BAD94413.1 differs from that shown. Reason: Frameshift at position 528. The sequence BAD95289.1 differs from that shown. Reason: Frameshift at position 528.

Ontologies

Keywords
Biological process	Biological rhythms Differentiation Flowering Gibberellin signaling pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat TPR repeat
Molecular function	Developmental protein Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cytokinin mediated signaling pathway Inferred from mutant phenotype Ref.11. Source: TAIR flower development Inferred from electronic annotation. Source: UniProtKB-KW gibberellic acid mediated signaling pathway Traceable author statement Ref.8. Source: TAIR negative regulation of gibberellic acid mediated signaling pathway Inferred from genetic interaction. Source: TAIR regulation of reactive oxygen species metabolic process Inferred from mutant phenotype. Source: TAIR rhythmic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay Ref.12. Source: TAIR nucleus Inferred from direct assay Ref.8. Source: TAIR
Molecular function	protein N-acetylglucosaminyltransferase activity Traceable author statement. Source: TAIR protein binding Inferred from physical interaction Ref.10. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GI	Q9SQI2	4	EBI-446372,EBI-446380

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q96301-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 914	914	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY		PRO_0000191776
Regions
	Repeat	43 – 76	34	TPR 1
	Repeat	77 – 110	34	TPR 2
	Repeat	112 – 144	33	TPR 3
	Repeat	152 – 185	34	TPR 4
	Repeat	186 – 219	34	TPR 5
	Repeat	220 – 253	34	TPR 6
	Repeat	261 – 294	34	TPR 7
	Repeat	295 – 328	34	TPR 8
	Repeat	329 – 362	34	TPR 9
	Repeat	364 – 396	33	TPR 10
	Repeat	397 – 430	34	TPR 11
	Region	431 – 914	484	Catalytic region
Amino acid modifications
	Modified residue	35	1	Phosphoserine Ref.12 Ref.13
Experimental info
	Mutagenesis	593	1	G → S in spy-3; induces a constitutive induction of GA signal. Ref.1
	Mutagenesis	845	1	C → Y in spy-5; induces a constitutive induction of GA signal. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: A881D84BB5C33493	FASTA	914	101,430
	10 20 30 40 50 60 MVGLEDDTER ERSPVVENGF SNGSRSSSSS AGVLSPSRKV TQGNDTLSYA NILRARNKFA 70 80 90 100 110 120 DALALYEAML EKDSKNVEAH IGKGICLQTQ NKGNLAFDCF SEAIRLDPHN ACALTHCGIL 130 140 150 160 170 180 HKEEGRLVEA AESYQKALMA DASYKPAAEC LAIVLTDLGT SLKLAGNTQE GIQKYYEALK 190 200 210 220 230 240 IDPHYAPAYY NLGVVYSEMM QYDNALSCYE KAALERPMYA EAYCNMGVIY KNRGDLEMAI 250 260 270 280 290 300 TCYERCLAVS PNFEIAKNNM AIALTDLGTK VKLEGDVTQG VAYYKKALYY NWHYADAMYN 310 320 330 340 350 360 LGVAYGEMLK FDMAIVFYEL AFHFNPHCAE ACNNLGVLYK DRDNLDKAVE CYQMALSIKP 370 380 390 400 410 420 NFAQSLNNLG VVYTVQGKMD AAASMIEKAI LANPTYAEAF NNLGVLYRDA GNITMAIDAY 430 440 450 460 470 480 EECLKIDPDS RNAGQNRLLA MNYINEGLDD KLFEAHRDWG WRFTRLHPQY TSWDNLKDPE 490 500 510 520 530 540 RPITIGYISP DFFTHSVSYF IEAPLTHHDY TKYKVVVYSA VVKADAKTYR FRDKVLKKGG 550 560 570 580 590 600 VWKDIYGIDE KKIASMVRED KIDILVELTG HTANNKLGTM ACRPAPVQVT WIGYPNTTGL 610 620 630 640 650 660 PTVDYRITDS LADPPDTKQK QVEELVRLPD CFLCYTPSPE AGPVCPTPAL SNGFVTFGSF 670 680 690 700 710 720 NNLAKITPKV LQVWARILCA VPNSRLVVKC KPFCCDSIRQ RFLTTLEQLG LESKRVDLLP 730 740 750 760 770 780 LILFNHDHMQ AYSLMDISLD TFPYAGTTTT CESLYMGVPC VTMAGSVHAH NVGVSLLTKV 790 800 810 820 830 840 GLGHLVAKNE DEYVQLSVDL ASDVTALSKL RMSLRDLMAG SPVCNGPSFA VGLESAYRNM 850 860 870 880 890 900 WKKYCKGEVP SLRRMEMLQK EVHDDPLISK DLGPSRVSVT GEATPSLKAN GSAPVPSSLP 910 TQSPQLSKRM DSTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SPINDLY, a tetratricopeptide repeat protein involved in gibberellin signal transduction in Arabidopsis." Jacobsen S.E., Binkowski K.A., Olszewski N.E. Proc. Natl. Acad. Sci. U.S.A. 93:9292-9296(1996) [PubMed: 8799194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLY-593 AND CYS-845. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Genetic and biochemical analysis of Arabidopsis SPY." Thornton T.M., Kreppel L., Hart G.W., Olszewski N.E. (In) Altman A., Ziv M., Izhar S. (eds.); Plant biotechnology and in vitro biology in the 21st century, pp.445-448, Kluwer Academic Publishers, New York (1999) Cited for: ENZYME ACTIVITY IN VITRO.
[6]	"Altered expression of SPINDLY affects gibberellin response and plant development." Swain S.M., Tseng T.-S., Olszewski N.E. Plant Physiol. 126:1174-1185(2001) [PubMed: 11457967] [Abstract] Cited for: FUNCTION.
[7]	"Ectopic expression of the tetratricopeptide repeat domain of SPINDLY causes defects in gibberellin response." Tseng T.-S., Swain S.M., Olszewski N.E. Plant Physiol. 126:1250-1258(2001) [PubMed: 11457975] [Abstract] Cited for: HOMODIMERIZATION, DOMAIN.
[8]	"SPINDLY is a nuclear-localized repressor of gibberellin signal transduction expressed throughout the plant." Swain S.M., Tseng T.-S., Thornton T.M., Gopalraj M., Olszewski N.E. Plant Physiol. 129:605-615(2002) [PubMed: 12068105] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[9]	"Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh. have overlapping functions necessary for gamete and seed development." Hartweck L.M., Scott C.L., Olszewski N.E. Genetics 161:1279-1291(2002) [PubMed: 12136030] [Abstract] Cited for: FUNCTION.
[10]	"SPINDLY and GIGANTEA interact and act in Arabidopsis thaliana pathways involved in light responses, flowering, and rhythms in cotyledon movements." Tseng T.-S., Salome P.A., McClung C.R., Olszewski N.E. Plant Cell 16:1550-1563(2004) [PubMed: 15155885] [Abstract] Cited for: FUNCTION, INTERACTION WITH GI.
[11]	"Cross talk between gibberellin and cytokinin: the Arabidopsis GA response inhibitor SPINDLY plays a positive role in cytokinin signaling." Greenboim-Wainberg Y., Maymon I., Borochov R., Alvarez J., Olszewski N., Ori N., Eshed Y., Weiss D. Plant Cell 17:92-102(2005) [PubMed: 15608330] [Abstract] Cited for: FUNCTION.
[12]	"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis." de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H. J. Proteome Res. 7:2458-2470(2008) [PubMed: 18433157] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY. Tissue: Root.
[13]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U62135 mRNA. Translation: AAC49446.1. AC008153 Genomic DNA. Translation: AAG51433.1. CP002686 Genomic DNA. Translation: AEE75060.1. AK220931 mRNA. Translation: BAD94413.1. Frameshift. AK221192 mRNA. Translation: BAD95289.1. Frameshift. AK221314 mRNA. Translation: BAD94086.1.
IPI	IPI00544177.
RefSeq	NP_187761.1. NM_111987.3.
UniGene	At.17656.
3D structure databases
ProteinModelPortal	Q96301.
SMR	Q96301. Positions 47-855.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96301. 1 interaction.
STRING	Q96301.
Protein family/group databases
CAZy	GT41. Glycosyltransferase Family 41.
Proteomic databases
PRIDE	Q96301.
ProMEX	Q96301.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G11540.1; AT3G11540.1; AT3G11540.
GeneID	820327.
GenomeReviews	Gene locus AT3G11540 in contig BA000014_GR.
KEGG	ath:AT3G11540.
NMPDR	fig|3702.1.peg.13207.
Organism-specific databases
GeneFarm	5156.
TAIR	At3g11540.
Phylogenomic databases
GeneTree	EPGT00070000030625.
HOGENOM	HBG684498.
InParanoid	Q96301.
OMA	GVPCVTM.
PhylomeDB	Q96301.
ProtClustDB	CLSN2684418.
Gene expression databases
Genevestigator	Q96301.
Family and domain databases
InterPro	IPR006597. Sel1-like. IPR001440. TPR-1. IPR013026. TPR-contain. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 5 hits.
Pfam	PF00515. TPR_1. 7 hits. [Graphical view]
SMART	SM00671. SEL1. 4 hits. SM00028. TPR. 10 hits. [Graphical view]
PROSITE	PS50005. TPR. 11 hits. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SPY_ARATH

Accession

Primary (citable) accession number: Q96301
Secondary accession number(s): Q56YX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	February 1, 1997
Last modified:	September 21, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program