SPY_EUSER
ID SPY_EUSER Reviewed; 918 AA.
AC Q8LP10;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 80.
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 exaltatum subsp. russellianum (Bluebells) (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] + 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 -!- 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 CAZy; GT41; Glycosyltransferase Family 41.
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; 2.
DR Pfam; PF13176; TPR_7; 1.
DR SMART; SM00671; SEL1; 3.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 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"
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
