SPY_PETHY
ID SPY_PETHY Reviewed; 932 AA.
AC O82039;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY;
DE EC=2.4.1.255 {ECO:0000250|UniProtKB:Q96301};
DE AltName: Full=PhSPY;
GN Name=SPY;
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, AND TISSUE SPECIFICITY.
RC TISSUE=Anther;
RX PubMed=11722761; DOI=10.1046/j.1365-313x.2001.01144.x;
RA Izhaki A., Swain S.M., Tseng T.-S., Borochov A., Olszewski N.E., Weiss D.;
RT "The role of SPY and its TPR domain in the regulation of gibberellin action
RT throughout the life cycle of Petunia hybrida plants.";
RL Plant J. 28:181-190(2001).
CC -!- FUNCTION: Probable O-linked N-acetylglucosamine transferase (OGT)
CC involved in various processes such as gibberellin (GA) signaling
CC pathway. OGTs catalyze the addition of nucleotide-activated sugars
CC directly onto the polypeptide through O-glycosidic linkage with the
CC hydroxyl of serine or threonine. Probably acts by adding O-linked
CC sugars to yet unknown proteins. {ECO:0000269|PubMed:11722761}.
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:0000250|UniProtKB:Q96301};
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:0000250|UniProtKB:Q96301};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves and flowers. Expressed
CC during all stages of corolla maturation. {ECO:0000269|PubMed:11722761}.
CC -!- INDUCTION: Not up-regulated by GA3 or ABA application.
CC -!- DOMAIN: The TPR repeats mediate protein-protein interactions.
CC Expression of such repeats in plants generate a dominant-negative
CC mutant. {ECO:0000269|PubMed:11722761}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000305}.
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DR EMBL; Y17720; CAA76834.1; -; mRNA.
DR AlphaFoldDB; O82039; -.
DR SMR; O82039; -.
DR CAZy; GT41; Glycosyltransferase Family 41.
DR PRIDE; O82039; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.25.40.10; -; 3.
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 Pfam; PF13181; TPR_8; 1.
DR SMART; SM00671; SEL1; 5.
DR SMART; SM00028; TPR; 11.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 10.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Gibberellin signaling pathway; Glycosyltransferase; Nucleus; Repeat;
KW TPR repeat; Transferase.
FT CHAIN 1..932
FT /note="Probable UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase SPINDLY"
FT /id="PRO_0000191781"
FT REPEAT 48..81
FT /note="TPR 1"
FT REPEAT 82..115
FT /note="TPR 2"
FT REPEAT 116..149
FT /note="TPR 3"
FT REPEAT 157..190
FT /note="TPR 4"
FT REPEAT 191..224
FT /note="TPR 5"
FT REPEAT 225..258
FT /note="TPR 6"
FT REPEAT 266..299
FT /note="TPR 7"
FT REPEAT 300..333
FT /note="TPR 8"
FT REPEAT 334..367
FT /note="TPR 9"
FT REPEAT 369..401
FT /note="TPR 10"
FT REPEAT 402..435
FT /note="TPR 11"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..932
FT /note="Catalytic region"
FT REGION 881..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 103940 MW; 4F0896631302D95D CRC64;
MAWTEKDVEN GKESDSLGNN GFLKGVQSSS DSKGSPVRIS PVKKSFEGKD AITYANILRS
RNKFVDALAI YESVLQKDSG SIESLIGKGI CLQMQNMGRL AFESFAEAIK LDPQNACALT
HCGILYKDEG RLVEAAESYQ KALKADPSYK PAAECLAIVL TDIGTSLKLA GNSQEGIQKY
YEAIKIDSHY APAYYNLGVV YSEMMQYDMA LNCYEKAAIE RPMYAEAYCN MGVIYKNRGD
LESAIACYER CLAVSPNFEI AKNNMAIALT DLGTKVKLEG DINQGVAYYK KALYYNWHYA
DAMYNLGVAY GEMLKFDMAI VFYELAFHFN PHCAEACNNL GVIYKDRDNL DKAVECYQMA
LTIKPNFSQS LNNLGVVYTV QGKMDAAASM IEKAIIANPT YAEAYNNLGV LYRDAGNISL
AIEAYEQCLK IDPDSRNAGQ NRLLAMNYIN EGSDDKLYEA HRDWGWRFMR LYQQYNSWDN
SKDPERQLVI GYVSPDYFTH SVSYFIEAPL AYHDYANYKV VIYSAVVKAD AKTNRFRDKV
LKKGGVWRDI YGIDEKKVSS MIREDKVDIM IELTGHTANN KLGMMACRPA PVQVTWIGYP
NTTGLPTIDY RITDSMADPP STKQKHVEEL VRLPDSFLCY TPSPEAGPVS PAPALTNGFV
TFGSFNNLAK ITPKVLQVWA RILCAVPHSR LIVKCKPFGC DSVRQRFLSI LEQLGLEPQR
VDLVPLILLN HDHMQAYSLM DISLDTFPYA GTTTTCESLY MGVPCVTMGG SVHAHNVGVS
LLKTVGLRKL VARNEDEYVE LAIQLASDVT SLSNLRMSLR ELMAKSPLCD GAQFTQNLES
TYRSMWRRYC DGDVPSLRRM ELLQQQQQTL AELVVPEESP VSPIEKTRIS ASKDGPIKEN
GFTVSPALVY NSSTIEENGV QLNQAGNPGK QS
