SPY_SOLLC
ID SPY_SOLLC Reviewed; 931 AA.
AC Q8RVB2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY;
DE Short=LeSPY;
DE EC=2.4.1.255 {ECO:0000250|UniProtKB:Q96301};
GN Name=SPY;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Shoot;
RX PubMed=12147734; DOI=10.1093/jxb/erf033;
RA Greb T., Schmitz G., Theres K.;
RT "Isolation and characterization of the Spindly homologue from tomato.";
RL J. Exp. Bot. 53:1829-1830(2002).
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). {ECO:0000250}.
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 -!- MISCELLANEOUS: Does not correspond to the procera gene.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ312093; CAC85168.1; -; Genomic_DNA.
DR EMBL; AJ312094; CAC85169.1; -; mRNA.
DR RefSeq; NP_001233937.1; NM_001247008.2.
DR RefSeq; XP_010325708.1; XM_010327406.2.
DR AlphaFoldDB; Q8RVB2; -.
DR SMR; Q8RVB2; -.
DR STRING; 4081.Solyc09g010180.2.1; -.
DR CAZy; GT41; Glycosyltransferase Family 41.
DR PaxDb; Q8RVB2; -.
DR PRIDE; Q8RVB2; -.
DR EnsemblPlants; Solyc09g010180.3.1; Solyc09g010180.3.1; Solyc09g010180.3.
DR GeneID; 543775; -.
DR Gramene; Solyc09g010180.3.1; Solyc09g010180.3.1; Solyc09g010180.3.
DR KEGG; sly:543775; -.
DR eggNOG; KOG4626; Eukaryota.
DR HOGENOM; CLU_001721_4_0_1; -.
DR InParanoid; Q8RVB2; -.
DR OMA; YQAHREW; -.
DR OrthoDB; 142546at2759; -.
DR PhylomeDB; Q8RVB2; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000004994; Chromosome 9.
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; 4.
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;
KW Reference proteome; Repeat; TPR repeat; Transferase.
FT CHAIN 1..931
FT /note="Probable UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase SPINDLY"
FT /id="PRO_0000191779"
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..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..931
FT /note="Catalytic region"
FT REGION 864..931
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"
FT COMPBIAS 864..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 103492 MW; 1933A81C48132C62 CRC64;
MAWTEKDVEN GKESESLGNN GFLKGGQSSS GSKGSPGRIS HVKKIFEDKD AITYANILRS
RNKFVDALAI YESVLEKDSK SIESLIGKGI CLQMQNTGRL AFESFSEAIK VDPQNACALT
HCGILYKDEG RLVEAAESYE KALKADPSYT PAAECLAIVL TDIGTSLKLA GNTQEGIQKY
YEAIKIDSHY APAYYNLGVV YSEMMQYDMA LNCYEKAALE RPMYAEAYCN MGVIFKNRGD
LESAIACYER CLAVSPNFEI AKNNMAIALT DLGTKVKLEG DINQGVAYYK KALCYNWHYA
DAMYNLGVAY GEMLKFDMAI VFYELAFHFN PHCAEACNNL GVIYKDRDNL DKAVECYQLA
LSIKPNFSQS LNNLGVVYTV QGKMDAAASM IEKAIIANPT YAEAYNNLGV LYRDAGNISL
AIEAYEQCLK IDPDSRNAGQ NRLLAMNYIN EGTDDKLYEA HRDWGRRFMK LYPQYTSWDN
SKVPERPLVI GYVSPDYFTH SVSYFIEAPL AHHDYTNYKV VVYSSVVKAD AKTNRFRDKV
MKKGGLWRDI YGIDEKKVSS MIREDKVDIM VELTGHTANN KLGTMACRPA PVQVTWIGYP
NTTGLPTIDY RITDAMADPP NAKQKHVEEL VRLPNSFLCY TPSPEAGPVC PAPALSNGFV
TFGSFNNLAK ITPKVLKVWA RILSAVPHSR LIVKCKPFCC DSVRQRFLSI LEQLGLEPQR
VDLLPLILLN HDHMQAYSLM DISLDTFPYA GTTTTCESLY MGVPCVTMGG SVHAHNVGVS
LLKTVGLENL VARNEDEYVE SAIQLASDVT SLSNLRMSLR ELMSKSPLCD GAKFTRNIES
IYRSMWRRYC DGDVPSLRRM ELLQQQQTQT ESVVPEESSV NPSERTITSA PTDGSIKENG
FTAVPALALK SSTSEENGVQ SNHNGNHGNL S
