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SPY_HORVU
ID   SPY_HORVU               Reviewed;         944 AA.
AC   O82422;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY;
DE            EC=2.4.1.255 {ECO:0000250|UniProtKB:Q96301};
DE   AltName: Full=HvSPY;
GN   Name=SPY;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Himalaya;
RX   PubMed=9634587; DOI=10.2307/3870685;
RA   Robertson M., Swain S.M., Chandler P.M., Olszewski N.E.;
RT   "Identification of a negative regulator of gibberellin action, HvSPY, in
RT   barley.";
RL   Plant Cell 10:995-1007(1998).
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:9634587}.
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 all parts of plants, including
CC       immature leaf blade, leaf sheath, mature leaf blade, roots, germinating
CC       embryos and aleurone layers. {ECO:0000269|PubMed:9634587}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC       transferase subfamily. {ECO:0000305}.
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DR   EMBL; AF035820; AAC36055.1; -; mRNA.
DR   AlphaFoldDB; O82422; -.
DR   SMR; O82422; -.
DR   CAZy; GT41; Glycosyltransferase Family 41.
DR   EnsemblPlants; HORVU.MOREX.r2.6HG0462400.1; HORVU.MOREX.r2.6HG0462400.1; HORVU.MOREX.r2.6HG0462400.
DR   EnsemblPlants; HORVU.MOREX.r2.6HG0462400.1.mrna1; HORVU.MOREX.r2.6HG0462400.1.mrna1; HORVU.MOREX.r2.6HG0462400.1.
DR   Gramene; HORVU.MOREX.r2.6HG0462400.1; HORVU.MOREX.r2.6HG0462400.1; HORVU.MOREX.r2.6HG0462400.
DR   Gramene; HORVU.MOREX.r2.6HG0462400.1.mrna1; HORVU.MOREX.r2.6HG0462400.1.mrna1; HORVU.MOREX.r2.6HG0462400.1.
DR   UniPathway; UPA00378; -.
DR   ExpressionAtlas; O82422; baseline and differential.
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:0009910; P:negative regulation of flower development; IEA:EnsemblPlants.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IEA:EnsemblPlants.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants.
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; 3.
DR   Pfam; PF13181; TPR_8; 2.
DR   SMART; SM00671; SEL1; 3.
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..944
FT                   /note="Probable UDP-N-acetylglucosamine--peptide N-
FT                   acetylglucosaminyltransferase SPINDLY"
FT                   /id="PRO_0000191778"
FT   REPEAT          34..67
FT                   /note="TPR 1"
FT   REPEAT          68..101
FT                   /note="TPR 2"
FT   REPEAT          102..135
FT                   /note="TPR 3"
FT   REPEAT          143..176
FT                   /note="TPR 4"
FT   REPEAT          177..210
FT                   /note="TPR 5"
FT   REPEAT          211..244
FT                   /note="TPR 6"
FT   REPEAT          252..285
FT                   /note="TPR 7"
FT   REPEAT          286..319
FT                   /note="TPR 8"
FT   REPEAT          320..353
FT                   /note="TPR 9"
FT   REPEAT          355..387
FT                   /note="TPR 10"
FT   REPEAT          388..421
FT                   /note="TPR 11"
FT   REGION          422..944
FT                   /note="Catalytic region"
FT   REGION          873..944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..944
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   944 AA;  103828 MW;  CBEAD8B0D1CE2F88 CRC64;
     MESLQGKESN GAVPVCNGGG GAAAPPAKQQ LPEGTDALRY ANILRSRNKF ADALQLYTTV
     LDKDGANVEA LIGKGICLQA QSLPRQALDC FTEAVKVDPK NACALTHCGM IYKDEGHLVE
     AAEAYQKARS ADPSYKAASE FLAIVLTDLG TSLKLAGNTE DGIQKYCEAL EVDSHYAPAY
     YNLGVVYSEM MQFDVALTCY EKAALERPLY AEAYCNMGVI YKNRGELDAA IACYDRCLTI
     SPNFEIAKNN MAIALTDLGT KVKIEGDINQ GVAYYKKALF YNWHYADAMY NLGVAYGEML
     NFEMAIVFYE LALHFNPRCA EACNNLGVIY KDRDNLDKAV ECYQMALSIK PNFSQSLNNL
     GVVYTVQGKM DAAASMIEKA ILANPTYAEA YNNLGVLYRD AGSITLSVQA YERCLQIDPD
     SRNAGQNRLL AMNYIDEGSD DKLYDAHREW GKRFMKLYAQ YTSWDNPKVA DRPLVIGYVS
     PDFFTHSVSY FVEAPLTHHD YTKCKVVVYS GVVKADAKTL RFKDKVLKKG GVWRDIYGID
     EKKVATLVRE DKVDILVELT GHTANNKLGT MACRPAPIQV TWIGYPNTTG LPAIDYRITD
     SLADSPNTNQ KHVEELVRLP ESFLCYTPSP EAGPVCPTPA ISNGFITFGS FNNLAKITPK
     VMQVWARILC AVPNSRLVVK CKPFCCDSIR QKFLSTLEEL GLESLRVDLL PLIHLNHDHM
     QAYSLMDISL DTFPYAGTTT TCESLYMGVP CVTMAGSVHA HNVGVSLLTK VGLGRLVAKT
     EDEYVSLALD LASDVSALEE LRKSLRELMI KSPVCDGESF TRGLESAYRS MWHRYCDGDS
     PALRRLEVLA DQTGEDLNKT AVKLADLKAQ RVNATAEEDN QSPVTKFDAT SKGGEQPQPQ
     IMVNGVTSPE GNQAVKAQPQ IMVNGVSSPH SPSGRCEANG HSSR
 
 
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