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