SPY_ARATH
ID SPY_ARATH Reviewed; 914 AA.
AC Q96301; Q56YX8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY {ECO:0000305};
DE EC=2.4.1.255 {ECO:0000269|Ref.5};
DE AltName: Full=GDP-fucose protein O-fucosyltransferase SPINDLY {ECO:0000305};
DE EC=2.4.1.221 {ECO:0000269|PubMed:28244988};
GN Name=SPY {ECO:0000303|PubMed:8799194};
GN OrderedLocusNames=At3g11540 {ECO:0000312|Araport:AT3G11540};
GN ORFNames=F24K9.29 {ECO:0000312|EMBL:AAG51433.1};
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 MUTAGENESIS OF GLY-593 AND
RP CYS-845.
RC STRAIN=cv. Columbia;
RX PubMed=8799194; DOI=10.1073/pnas.93.17.9292;
RA Jacobsen S.E., Binkowski K.A., Olszewski N.E.;
RT "SPINDLY, a tetratricopeptide repeat protein involved in gibberellin signal
RT transduction in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9292-9296(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RA Thornton T.M., Kreppel L., Hart G.W., Olszewski N.E.;
RT "Genetic and biochemical analysis of Arabidopsis SPY.";
RL (In) Altman A., Ziv M., Izhar S. (eds.);
RL Plant biotechnology and in vitro biology in the 21st century, pp.445-448,
RL Kluwer Academic Publishers, New York (1999).
RN [6]
RP FUNCTION.
RX PubMed=11457967; DOI=10.1104/pp.126.3.1174;
RA Swain S.M., Tseng T.-S., Olszewski N.E.;
RT "Altered expression of SPINDLY affects gibberellin response and plant
RT development.";
RL Plant Physiol. 126:1174-1185(2001).
RN [7]
RP HOMODIMERIZATION, AND DOMAIN.
RX PubMed=11457975; DOI=10.1104/pp.126.3.1250;
RA Tseng T.-S., Swain S.M., Olszewski N.E.;
RT "Ectopic expression of the tetratricopeptide repeat domain of SPINDLY
RT causes defects in gibberellin response.";
RL Plant Physiol. 126:1250-1258(2001).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12068105; DOI=10.1104/pp.020002;
RA Swain S.M., Tseng T.-S., Thornton T.M., Gopalraj M., Olszewski N.E.;
RT "SPINDLY is a nuclear-localized repressor of gibberellin signal
RT transduction expressed throughout the plant.";
RL Plant Physiol. 129:605-615(2002).
RN [9]
RP FUNCTION.
RX PubMed=12136030; DOI=10.1093/genetics/161.3.1279;
RA Hartweck L.M., Scott C.L., Olszewski N.E.;
RT "Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana
RT L. Heynh. have overlapping functions necessary for gamete and seed
RT development.";
RL Genetics 161:1279-1291(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH GI.
RX PubMed=15155885; DOI=10.1105/tpc.019224;
RA Tseng T.-S., Salome P.A., McClung C.R., Olszewski N.E.;
RT "SPINDLY and GIGANTEA interact and act in Arabidopsis thaliana pathways
RT involved in light responses, flowering, and rhythms in cotyledon
RT movements.";
RL Plant Cell 16:1550-1563(2004).
RN [11]
RP FUNCTION.
RX PubMed=15608330; DOI=10.1105/tpc.104.028472;
RA Greenboim-Wainberg Y., Maymon I., Borochov R., Alvarez J., Olszewski N.,
RA Ori N., Eshed Y., Weiss D.;
RT "Cross talk between gibberellin and cytokinin: the Arabidopsis GA response
RT inhibitor SPINDLY plays a positive role in cytokinin signaling.";
RL Plant Cell 17:92-102(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [14]
RP INTERACTION WITH TCP14 AND TCP15.
RX PubMed=22267487; DOI=10.1105/tpc.111.093518;
RA Steiner E., Efroni I., Gopalraj M., Saathoff K., Tseng T.S., Kieffer M.,
RA Eshed Y., Olszewski N., Weiss D.;
RT "The Arabidopsis O-linked N-acetylglucosamine transferase SPINDLY interacts
RT with class I TCPs to facilitate cytokinin responses in leaves and
RT flowers.";
RL Plant Cell 24:96-108(2012).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLU-567 AND LYS-665.
RX PubMed=28244988; DOI=10.1038/nchembio.2320;
RA Zentella R., Sui N., Barnhill B., Hsieh W.P., Hu J., Shabanowitz J.,
RA Boyce M., Olszewski N.E., Zhou P., Hunt D.F., Sun T.P.;
RT "The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth
RT repressor DELLA.";
RL Nat. Chem. Biol. 13:479-485(2017).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32928908; DOI=10.1242/dev.192039;
RA Mutanwad K.V., Zangl I., Lucyshyn D.;
RT "The Arabidopsis O-fucosyltransferase SPINDLY regulates root hair
RT patterning independently of gibberellin signaling.";
RL Development 147:0-0(2020).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APRR5, AND MUTAGENESIS OF
RP GLY-593.
RX PubMed=31899321; DOI=10.1016/j.molp.2019.12.013;
RA Wang Y., He Y., Su C., Zentella R., Sun T.P., Wang L.;
RT "Nuclear Localized O-Fucosyltransferase SPY Facilitates PRR5 Proteolysis to
RT Fine-Tune the Pace of Arabidopsis Circadian Clock.";
RL Mol. Plant 13:446-458(2020).
RN [18]
RP FUNCTION, AND INTERACTION WITH CPN20.
RX PubMed=34712252; DOI=10.3389/fpls.2021.724144;
RA Liang L., Wang Q., Song Z., Wu Y., Liang Q., Wang Q., Yang J., Bi Y.,
RA Zhou W., Fan L.M.;
RT "O-fucosylation of CPN20 by SPINDLY derepresses abscisic acid signaling
RT during seed germination and seedling development.";
RL Front. Plant Sci. 12:724144-724144(2021).
CC -!- FUNCTION: Probable O-linked N-acetylglucosamine transferase (OGT)
CC involved in various processes such as gibberellin (GA) signaling
CC pathway and circadian clock. OGTs catalyze the addition of nucleotide-
CC activated sugars directly onto the polypeptide through O-glycosidic
CC linkage with the hydroxyl of serine or threonine. Probably acts by
CC adding O-linked sugars to yet unknown proteins. Acts as a repressor of
CC GA signaling pathway to inhibit hypocotyl elongation. Functions with
CC GIGANTEA (GI) in pathways controlling flowering, circadian cotyledon
CC movements and hypocotyl elongation. Acts as a light-regulated promoter
CC of elongation via its interaction with GI. Acts as an activator of
CC cytokinin signaling. Required with SEC for gamete and seed development
CC (PubMed:12136030). Its OGT activity has been proved in vitro but not in
CC vivo (Ref.5, PubMed:11457967, PubMed:12136030, PubMed:15155885,
CC PubMed:15608330, PubMed:8799194). Possesses O-fucosyltransferase
CC activity on specific serine and threonine residues (PubMed:28244988).
CC Mediates O-fucosylation of the DELLA protein RGA, a repressor of the GA
CC signaling pathway (PubMed:28244988). O-fucosylation enhances RGA
CC activity by promoting RGA binding to key transcription factors in
CC brassinosteroid and light-signaling pathways (PubMed:28244988).
CC Regulates root hair patterning upstream of the transcription factor
CC WER, independently of DELLA proteins and GA signaling
CC (PubMed:32928908). Involved in abscisic acid (ABA) signaling partly
CC through functional ABAR (PubMed:34712252). Mediates O-fucosylation of
CC CPN20 that may depress ABA responses during seed germination and
CC seedling development (PubMed:34712252). Involved in the modulation of
CC the pace of the circadian clock by mediating O-fucosylation of APRR5,
CC one of the core circadian clock components (PubMed:31899321). O-
CC fucosylation promotes APRR5 proteolysis (PubMed:31899321).
CC {ECO:0000269|PubMed:11457967, ECO:0000269|PubMed:12136030,
CC ECO:0000269|PubMed:15155885, ECO:0000269|PubMed:15608330,
CC ECO:0000269|PubMed:28244988, ECO:0000269|PubMed:31899321,
CC ECO:0000269|PubMed:32928908, ECO:0000269|PubMed:34712252,
CC ECO:0000269|PubMed:8799194, ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-
CC acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.255;
CC Evidence={ECO:0000269|Ref.5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48905;
CC Evidence={ECO:0000269|Ref.5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-
CC (N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:48908, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:90840; EC=2.4.1.255;
CC Evidence={ECO:0000269|Ref.5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48909;
CC Evidence={ECO:0000269|Ref.5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-
CC L-seryl-[protein] + GDP + H(+); Xref=Rhea:RHEA:63644, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:17914, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:189632; EC=2.4.1.221;
CC Evidence={ECO:0000269|PubMed:28244988};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000269|PubMed:28244988};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + L-threonyl-[protein] = 3-O-(alpha-L-
CC fucosyl)-L-threonyl-[protein] + GDP + H(+); Xref=Rhea:RHEA:70491,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:17915, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:189631; EC=2.4.1.221;
CC Evidence={ECO:0000269|PubMed:28244988};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000269|PubMed:28244988};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50.5 uM for GDP-beta-L-fucose {ECO:0000269|PubMed:28244988};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:28244988};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: Homomultimer; via its TPR repeats. Interacts with GI
CC (PubMed:15155885). Interacts with TCP14 and TCP15 (PubMed:22267487,
CC PubMed:15155885). Interacts (via N-terminus) with APRR5
CC (PubMed:31899321). Interacts with CPN20 (PubMed:34712252).
CC {ECO:0000269|PubMed:15155885, ECO:0000269|PubMed:22267487,
CC ECO:0000269|PubMed:31899321, ECO:0000269|PubMed:34712252}.
CC -!- INTERACTION:
CC Q96301; Q9SQI2: GI; NbExp=4; IntAct=EBI-446372, EBI-446380;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12068105,
CC ECO:0000269|PubMed:31899321}. Nucleus {ECO:0000269|PubMed:12068105,
CC ECO:0000269|PubMed:31899321}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q96301-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed. Present throughout the plant (at
CC protein level). {ECO:0000269|PubMed:12068105}.
CC -!- DEVELOPMENTAL STAGE: Detected in all organs of the plant and at all
CC stages of the life cycle. Detected 1 day after germination in the
CC radicle just before its emergence from the seed. At 2.5 and 3 days
CC after germination, expression in the young seedling is highest in the
CC cotyledons and the root tip. At 3, 4 and 5 days, expression is also
CC detectable in the hypocotyl. At 10 days of age, expression in the first
CC pair of true leaves is reduced relative to the rest of the seedling. 2
CC days later, this difference disappears and the expression level is
CC again fairly similar throughout the aboveground portion of the plant,
CC with a higher intensity in the vegetative apex. This developmental
CC regulation is not detected in leaves developing at later nodes. Older
CC plants also display uniform expression throughout the vegetative
CC organs, but this expression is less intense. In older seedlings,
CC expression is observed throughout the root, particularly at the tip of
CC the primary root and in lateral roots. Expression is also observed in
CC trichomes and senescing leaves, and in inflorescence internodes,
CC flowers. Expression is observed in the seeds and carpels of fully
CC elongated siliques. Lower expression is also observed in expanding
CC siliques and in the developing seeds in these siliques. Expression is
CC also detected in the embryo of maturing seeds (after the disappearance
CC of the endosperm) (at protein level). {ECO:0000269|PubMed:12068105}.
CC -!- DOMAIN: The TPR repeats mediate protein-protein interactions and are
CC essential for its function. Expression of such repeats in plants
CC accelerate flowering. {ECO:0000269|PubMed:11457975}.
CC -!- DISRUPTION PHENOTYPE: Altered root epidermis morphology and root hair
CC patterning. {ECO:0000269|PubMed:32928908}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94413.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD95289.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U62135; AAC49446.1; -; mRNA.
DR EMBL; AC008153; AAG51433.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75060.1; -; Genomic_DNA.
DR EMBL; AK220931; BAD94413.1; ALT_FRAME; mRNA.
DR EMBL; AK221192; BAD95289.1; ALT_FRAME; mRNA.
DR EMBL; AK221314; BAD94086.1; -; mRNA.
DR RefSeq; NP_187761.1; NM_111987.4. [Q96301-1]
DR AlphaFoldDB; Q96301; -.
DR SMR; Q96301; -.
DR BioGRID; 5661; 8.
DR IntAct; Q96301; 1.
DR STRING; 3702.AT3G11540.1; -.
DR CAZy; GT41; Glycosyltransferase Family 41.
DR iPTMnet; Q96301; -.
DR PaxDb; Q96301; -.
DR PRIDE; Q96301; -.
DR ProteomicsDB; 226785; -. [Q96301-1]
DR EnsemblPlants; AT3G11540.1; AT3G11540.1; AT3G11540. [Q96301-1]
DR GeneID; 820327; -.
DR Gramene; AT3G11540.1; AT3G11540.1; AT3G11540. [Q96301-1]
DR KEGG; ath:AT3G11540; -.
DR Araport; AT3G11540; -.
DR TAIR; locus:2080722; AT3G11540.
DR eggNOG; KOG4626; Eukaryota.
DR HOGENOM; CLU_001721_4_0_1; -.
DR InParanoid; Q96301; -.
DR OMA; YQAHREW; -.
DR PhylomeDB; Q96301; -.
DR BRENDA; 2.4.1.221; 399.
DR BRENDA; 2.4.1.255; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q96301; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96301; baseline and differential.
DR Genevisible; Q96301; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; TAS:TAIR.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; TAS:TAIR.
DR GO; GO:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; IGI:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR029489; OGT/SEC/SPY_C.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13844; Glyco_transf_41; 2.
DR Pfam; PF00515; TPR_1; 4.
DR SMART; SM00671; SEL1; 4.
DR SMART; SM00028; TPR; 11.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 11.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cytoplasm; Developmental protein;
KW Differentiation; Flowering; Gibberellin signaling pathway;
KW Glycosyltransferase; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Transferase.
FT CHAIN 1..914
FT /note="Probable UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase SPINDLY"
FT /id="PRO_0000191776"
FT REPEAT 43..76
FT /note="TPR 1"
FT REPEAT 77..110
FT /note="TPR 2"
FT REPEAT 112..144
FT /note="TPR 3"
FT REPEAT 152..185
FT /note="TPR 4"
FT REPEAT 186..219
FT /note="TPR 5"
FT REPEAT 220..253
FT /note="TPR 6"
FT REPEAT 261..294
FT /note="TPR 7"
FT REPEAT 295..328
FT /note="TPR 8"
FT REPEAT 329..362
FT /note="TPR 9"
FT REPEAT 364..396
FT /note="TPR 10"
FT REPEAT 397..430
FT /note="TPR 11"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..914
FT /note="Catalytic region"
FT REGION 866..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MUTAGEN 567
FT /note="E->K: In spy-15; Abolishes O-fucosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28244988"
FT MUTAGEN 593
FT /note="G->S: In spy-3; induces a constitutive induction of
FT GA signal. Abolishes O-fucosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31899321,
FT ECO:0000269|PubMed:8799194"
FT MUTAGEN 665
FT /note="K->M: In spy-19; Abolishes O-fucosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28244988"
FT MUTAGEN 845
FT /note="C->Y: In spy-5; induces a constitutive induction of
FT GA signal."
FT /evidence="ECO:0000269|PubMed:8799194"
SQ SEQUENCE 914 AA; 101430 MW; A881D84BB5C33493 CRC64;
MVGLEDDTER ERSPVVENGF SNGSRSSSSS AGVLSPSRKV TQGNDTLSYA NILRARNKFA
DALALYEAML EKDSKNVEAH IGKGICLQTQ NKGNLAFDCF SEAIRLDPHN ACALTHCGIL
HKEEGRLVEA AESYQKALMA DASYKPAAEC LAIVLTDLGT SLKLAGNTQE GIQKYYEALK
IDPHYAPAYY NLGVVYSEMM QYDNALSCYE KAALERPMYA EAYCNMGVIY KNRGDLEMAI
TCYERCLAVS PNFEIAKNNM AIALTDLGTK VKLEGDVTQG VAYYKKALYY NWHYADAMYN
LGVAYGEMLK FDMAIVFYEL AFHFNPHCAE ACNNLGVLYK DRDNLDKAVE CYQMALSIKP
NFAQSLNNLG VVYTVQGKMD AAASMIEKAI LANPTYAEAF NNLGVLYRDA GNITMAIDAY
EECLKIDPDS RNAGQNRLLA MNYINEGLDD KLFEAHRDWG WRFTRLHPQY TSWDNLKDPE
RPITIGYISP DFFTHSVSYF IEAPLTHHDY TKYKVVVYSA VVKADAKTYR FRDKVLKKGG
VWKDIYGIDE KKIASMVRED KIDILVELTG HTANNKLGTM ACRPAPVQVT WIGYPNTTGL
PTVDYRITDS LADPPDTKQK QVEELVRLPD CFLCYTPSPE AGPVCPTPAL SNGFVTFGSF
NNLAKITPKV LQVWARILCA VPNSRLVVKC KPFCCDSIRQ RFLTTLEQLG LESKRVDLLP
LILFNHDHMQ AYSLMDISLD TFPYAGTTTT CESLYMGVPC VTMAGSVHAH NVGVSLLTKV
GLGHLVAKNE DEYVQLSVDL ASDVTALSKL RMSLRDLMAG SPVCNGPSFA VGLESAYRNM
WKKYCKGEVP SLRRMEMLQK EVHDDPLISK DLGPSRVSVT GEATPSLKAN GSAPVPSSLP
TQSPQLSKRM DSTS
