ID   SPY_EUSRU               Reviewed;         918 AA.
AC   Q8LP10;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   02-SEP-2026, entry version 91.
DE   RecName: Full=Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY;
DE            Short=EgSPY;
DE            EC=2.4.1.255 {ECO:0000250|UniProtKB:Q96301};
GN   Name=SPY;
OS   Eustoma russellianum (Showy prairie gentian) (Eustoma grandiflorum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Gentianaceae; Chironieae; Chironiinae;
OC   Eustoma.
OX   NCBI_TaxID=52518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX   PubMed=12879260; DOI=10.1007/s00299-003-0672-z;
RA   Mino M., Oka M., Tasaka Y., Iwabuchi M.;
RT   "Thermoinduction of genes encoding the enzymes of gibberellin biosynthesis
RT   and a putative negative regulator of gibberellin signal transduction in
RT   Eustoma grandiflorum.";
RL   Plant Cell Rep. 22:159-165(2003).
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 (By similarity). May function as a
CC       negative regulator of GA signal transduction during vernalization,
CC       inhibiting adventitious shoot elongation during vernalization.
CC       {ECO:0000250, ECO:0000269|PubMed:12879260}.
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] + UDP + H(+);
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] + UDP + H(+);
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   -!- INDUCTION: During vernalization. {ECO:0000269|PubMed:12879260}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC       transferase subfamily. {ECO:0000305}.
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DR   EMBL; AB080739; BAC11808.1; -; mRNA.
DR   AlphaFoldDB; Q8LP10; -.
DR   SMR; Q8LP10; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0097363; F:protein O-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR   Gene3D; 3.40.50.11380; -; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR   InterPro; IPR051939; Glycosyltr_41/O-GlcNAc_trsf.
DR   InterPro; IPR029489; OGT/SEC/SPY_C.
DR   InterPro; IPR006597; Sel1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_rpt.
DR   PANTHER; PTHR44835:SF1; PROTEIN O-GLCNAC TRANSFERASE; 1.
DR   PANTHER; PTHR44835; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE SPINDLY-RELATED; 1.
DR   Pfam; PF13844; Glyco_transf_41; 2.
DR   Pfam; PF00515; TPR_1; 2.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00671; SEL1; 3.
DR   SMART; SM00028; TPR; 9.
DR   SUPFAM; SSF48452; TPR-like; 3.
DR   PROSITE; PS50005; TPR; 9.
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..918
FT                   /note="Probable UDP-N-acetylglucosamine--peptide N-
FT                   acetylglucosaminyltransferase SPINDLY"
FT                   /id="PRO_0000191777"
FT   REPEAT          34..66
FT                   /note="TPR 1"
FT   REPEAT          67..99
FT                   /note="TPR 2"
FT   REPEAT          101..132
FT                   /note="TPR 3"
FT   REPEAT          140..171
FT                   /note="TPR 4"
FT   REPEAT          172..205
FT                   /note="TPR 5"
FT   REPEAT          207..238
FT                   /note="TPR 6"
FT   REPEAT          239..271
FT                   /note="TPR 7"
FT   REPEAT          273..305
FT                   /note="TPR 8"
FT   REPEAT          306..339
FT                   /note="TPR 9"
FT   REPEAT          341..373
FT                   /note="TPR 10"
FT   REPEAT          374..407
FT                   /note="TPR 11"
FT   REGION          408..918
FT                   /note="Catalytic region"
FT   REGION          843..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..853
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   918 AA;  102154 MW;  D79209A7A6844F89 CRC64;
     MIEKAIVAKP KGLLKGVQSS SDSKGSPVKK SLEGKEAITY AKILRSRNKF VDALAIYELE
     KDSKNVEAHI GKGICLQTQN KGNLAFDCFS EAIRLDPHNA CALTHCGILY KDEGRLVEAA
     SYQKALQADP SYKPAAECLA TVLNDLGTSL KGNTQEGIQK YYEAVKIDPH YAPACYNLGV
     VYSEMMQYDV ALSCYERAAT ESPTYADAYC NTGIIYKNRG DLCLAVSPNF EIAKNNMGIA
     LTDLGTKEKL EGDIDQGVAY YKKALYYNWH YSDAMYNLGV AYGEMLKFDM AIIFDELAFH
     FNPHCAEACN NLGVIYKDRD NLDKAVECYQ KALSIKPNFS QSLNNLGVVF TVQGKMDAAA
     SMIEKAIVAN PTYAEAYNNL GVLYRDAGNI FLAIEAYEQC LKIDPDSRNA GQNRLLAMNY
     INEGADDRLY EAHRDWGGRF MRLYSQYTSW DNPKDPERPL VIGYGSPDHF LSYFIEAPLL
     YHDYENFKVV TYSAVVKADA KTNRFRERVL KKGGIWRDIY GIDEKKVASM IREDKVDILI
     ELTGHTANNK LGMMACRPAP IQVTWIGYPN TTGLPTIDYR ITDSLADPLD TKQKHVEELI
     QLPACFLCYT PSPEAGPVSP TPALSNGFIT FGSFNNLAKI TPKVLQVWAR ILCAVSNSRL
     IVKCKPFCCE SVRQTFLSTL EQLGLESTRV DLLPLILLNH DHMQAYSLMD ISLDTFPYAG
     TTTTCESLYM GVPCITMRGL VHAHNVGVSL LSTVGLGHLV AKNEDDYVRL AVQLASDVTA
     LSNLRLTLRE LMSKSPLCDG PKFIQDLELT YRSMWHRYCK GDIPSLSRME ILQKEELDVV
     QEQLHQQPNT SPQKLVKDEP ADDASGPEHG PASKDNPLVL IKINGYNTSP SSITSPSSEE
     NGVSQTRMLN CGDQCFRV
//