SEC_ARATH
ID SEC_ARATH Reviewed; 977 AA.
AC Q9M8Y0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC {ECO:0000303|PubMed:16014901};
DE EC=2.4.1.255 {ECO:0000269|PubMed:12136030};
DE AltName: Full=Protein SECRET AGENT {ECO:0000303|PubMed:16014901};
GN Name=SEC {ECO:0000303|PubMed:16014901};
GN OrderedLocusNames=At3g04240 {ECO:0000312|Araport:AT3G04240};
GN ORFNames=T6K12.14 {ECO:0000312|EMBL:AAF26789.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RX PubMed=12136030; DOI=10.1093/genetics/161.3.1279;
RA Hartweck L.M., Scott C.L., Olszewski N.E.;
RT "Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana
RT L. Heynh. have overlapping functions necessary for gamete and seed
RT development.";
RL Genetics 161:1279-1291(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION.
RX PubMed=16014901; DOI=10.1128/jvi.79.15.9381-9387.2005;
RA Chen D., Juarez S., Hartweck L., Alamillo J.M., Simon-Mateo C., Perez J.J.,
RA Fernandez-Fernandez M.R., Olszewski N.E., Garcia J.A.;
RT "Identification of secret agent as the O-GlcNAc transferase that
RT participates in Plum pox virus infection.";
RL J. Virol. 79:9381-9387(2005).
RN [6]
RP INTERACTION WITH TCP14 AND TCP15.
RX PubMed=22267487; DOI=10.1105/tpc.111.093518;
RA Steiner E., Efroni I., Gopalraj M., Saathoff K., Tseng T.S., Kieffer M.,
RA Eshed Y., Olszewski N., Weiss D.;
RT "The Arabidopsis O-linked N-acetylglucosamine transferase SPINDLY interacts
RT with class I TCPs to facilitate cytokinin responses in leaves and
RT flowers.";
RL Plant Cell 24:96-108(2012).
RN [7]
RP FUNCTION.
RX PubMed=26773002; DOI=10.1101/gad.270587.115;
RA Zentella R., Hu J., Hsieh W.P., Matsumoto P.A., Dawdy A., Barnhill B.,
RA Oldenhof H., Hartweck L.M., Maitra S., Thomas S.G., Cockrell S., Boyce M.,
RA Shabanowitz J., Hunt D.F., Olszewski N.E., Sun T.P.;
RT "O-GlcNAcylation of master growth repressor DELLA by SECRET AGENT modulates
RT multiple signaling pathways in Arabidopsis.";
RL Genes Dev. 30:164-176(2016).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATX1, AND MUTAGENESIS OF
RP PHE-540; HIS-541; HIS-604; GLN-776 AND LYS-779.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=30150325; DOI=10.15252/embj.201798115;
RA Xing L., Liu Y., Xu S., Xiao J., Wang B., Deng H., Lu Z., Xu Y., Chong K.;
RT "Arabidopsis O-GlcNAc transferase SEC activates histone methyltransferase
RT ATX1 to regulate flowering.";
RL EMBO J. 37:E98115-E98115(2018).
CC -!- FUNCTION: O-linked N-acetylglucosamine transferase (OGT) that mediates
CC O-glycosylation of capsid protein (CP) of virus in case of infection by
CC Plum pox virus (PubMed:16014901). OGTs catalyze the addition of
CC nucleotide-activated sugars directly onto the polypeptide through O-
CC glycosidic linkage with the hydroxyl of serine or threonine
CC (PubMed:16014901). Probably acts by adding O-linked sugars to yet
CC unknown proteins. Its OGT activity has been proved in vitro but not in
CC vivo (PubMed:12136030). Required with SPY for gamete and seed
CC development (PubMed:16014901). Mediates O-glycosylation of the DELLA
CC protein RGA, a repressor of the gibberellin (GA) signaling pathway
CC (PubMed:26773002). O-glycosylation by SEC inhibits RGA binding to four
CC of its interactors PIF3, PIF4, JAZ1, and BZR1 that are key regulators
CC in light, jasmonate, and brassinosteroid signaling pathways,
CC respectively (PubMed:26773002). Activates ATX1 through O-GlcNAc
CC modification to augment ATX1-mediated H3K4me3 histone epigenetic
CC modification at FLC locus, thus preventing premature flowering
CC (PubMed:30150325). {ECO:0000269|PubMed:12136030,
CC ECO:0000269|PubMed:16014901, ECO:0000269|PubMed:26773002,
CC ECO:0000269|PubMed:30150325}.
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:0000269|PubMed:12136030};
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:0000269|PubMed:12136030};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with TCP14 and TCP15 (PubMed:22267487). Interacts
CC with ATX1 (PubMed:30150325). {ECO:0000269|PubMed:22267487,
CC ECO:0000269|PubMed:30150325}.
CC -!- INTERACTION:
CC Q9M8Y0; Q9SCU7: MYB30; NbExp=3; IntAct=EBI-4426966, EBI-4466599;
CC Q9M8Y0; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-4426966, EBI-15192297;
CC Q9M8Y0; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-4426966, EBI-4426557;
CC Q9M8Y0; Q9LVG2: TOE2; NbExp=4; IntAct=EBI-4426966, EBI-4424568;
CC -!- DISRUPTION PHENOTYPE: Early flowering phenotype due to reduced histone
CC H3 'Lys-4' trimethylation (H3K4me3) of FLC thus leading to lower FLC
CC expression. {ECO:0000269|PubMed:30150325}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000305}.
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DR EMBL; AF441079; AAL60196.1; -; mRNA.
DR EMBL; AC016829; AAF26789.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74056.1; -; Genomic_DNA.
DR EMBL; AY090938; AAM13988.1; -; mRNA.
DR EMBL; AY117340; AAM51415.1; -; mRNA.
DR RefSeq; NP_187074.1; NM_111295.4.
DR AlphaFoldDB; Q9M8Y0; -.
DR SMR; Q9M8Y0; -.
DR BioGRID; 4914; 8.
DR IntAct; Q9M8Y0; 6.
DR STRING; 3702.AT3G04240.1; -.
DR CAZy; GT41; Glycosyltransferase Family 41.
DR PaxDb; Q9M8Y0; -.
DR PRIDE; Q9M8Y0; -.
DR ProteomicsDB; 232927; -.
DR EnsemblPlants; AT3G04240.1; AT3G04240.1; AT3G04240.
DR GeneID; 819579; -.
DR Gramene; AT3G04240.1; AT3G04240.1; AT3G04240.
DR KEGG; ath:AT3G04240; -.
DR Araport; AT3G04240; -.
DR TAIR; locus:2103025; AT3G04240.
DR eggNOG; KOG4626; Eukaryota.
DR HOGENOM; CLU_001721_1_1_1; -.
DR InParanoid; Q9M8Y0; -.
DR OrthoDB; 142546at2759; -.
DR PhylomeDB; Q9M8Y0; -.
DR BRENDA; 2.4.1.255; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9M8Y0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8Y0; baseline and differential.
DR Genevisible; Q9M8Y0; AT.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:TAIR.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009910; P:negative regulation of flower development; IMP:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR037919; OGT.
DR InterPro; IPR029489; OGT/SEC/SPY_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44366; PTHR44366; 1.
DR Pfam; PF13844; Glyco_transf_41; 2.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13176; TPR_7; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 13.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 13.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Glycosyltransferase; Reference proteome; Repeat;
KW TPR repeat; Transferase.
FT CHAIN 1..977
FT /note="Probable UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase SEC"
FT /id="PRO_0000191782"
FT REPEAT 2..35
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 53..86
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 87..120
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 121..154
FT /note="TPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 155..188
FT /note="TPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 189..222
FT /note="TPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 223..256
FT /note="TPR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 257..290
FT /note="TPR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 291..324
FT /note="TPR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 325..358
FT /note="TPR 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 359..392
FT /note="TPR 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 393..426
FT /note="TPR 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 427..460
FT /note="TPR 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 461..494
FT /note="TPR 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REGION 495..977
FT /note="Catalytic region"
FT /evidence="ECO:0000305"
FT MUTAGEN 540
FT /note="F->A: Reduced activity; when associated with A-541,
FT A-604, A-776 and A-779."
FT /evidence="ECO:0000269|PubMed:30150325"
FT MUTAGEN 541
FT /note="H->A: Reduced activity; when associated with A-540,
FT A-604, A-776 and A-779."
FT /evidence="ECO:0000269|PubMed:30150325"
FT MUTAGEN 604
FT /note="H->A: Reduced activity; when associated with A-540,
FT A-541, A-776 and A-779."
FT /evidence="ECO:0000269|PubMed:30150325"
FT MUTAGEN 776
FT /note="Q->A: Reduced activity; when associated with A-540,
FT A-541, A-604 and A-779."
FT /evidence="ECO:0000269|PubMed:30150325"
FT MUTAGEN 779
FT /note="K->A: Reduced activity; when associated with A-540,
FT A-541, A-604 and A-776."
FT /evidence="ECO:0000269|PubMed:30150325"
SQ SEQUENCE 977 AA; 110114 MW; 2AC617CB4B6D5409 CRC64;
MISSKNGAAM ISRPVFLSDR VDEVFSRKLD LSVSSSSSSS LLQQFNKTHE GDDDARLALA
HQLYKGGDFK QALEHSNMVY QRNPLRTDNL LLIGAIYYQL QEYDMCIARN EEALRIQPQF
AECYGNMANA WKEKGDTDRA IRYYLIAIEL RPNFADAWSN LASAYMRKGR LSEATQCCQQ
ALSLNPLLVD AHSNLGNLMK AQGLIHEAYS CYLEAVRIQP TFAIAWSNLA GLFMESGDLN
RALQYYKEAV KLKPAFPDAY LNLGNVYKAL GRPTEAIMCY QHALQMRPNS AMAFGNIASI
YYEQGQLDLA IRHYKQALSR DPRFLEAYNN LGNALKDIGR VDEAVRCYNQ CLALQPNHPQ
AMANLGNIYM EWNMMGPASS LFKATLAVTT GLSAPFNNLA IIYKQQGNYS DAISCYNEVL
RIDPLAADAL VNRGNTYKEI GRVTEAIQDY MHAINFRPTM AEAHANLASA YKDSGHVEAA
ITSYKQALLL RPDFPEATCN LLHTLQCVCC WEDRSKMFAE VESIIRRQIN MSVLPSVQPF
HAIAYPIDPI LALEISRKYA AHCSIIASRF GLPPFTHPAG LPVKREGGFK RLRIGYVSSD
FGNHPLSHLM GSVFGMHNRE NVEVFCYALS ANDNTEWRQR IQSEAEHFLD VSAMSSDAIA
KIINQDKIQI LINLNGYTKG ARNEIFAMQP APIQVSYMGF PGTTGATYID YLVTDEFVSP
LQYAHIYSEK LVHLPHCYFV NDYKQKNQDV LDPNSKPKRS DYGLPEDKFI FACFNQLYKM
DPEIVNTWCN ILKRVPNSAL WLLRFPAAGE MRFRTYAAAQ GVQPDQIIFT DVAMKSEHIR
RSVLADVILD TPLCNGHTTG TDVLWAGVPM ITLPLEKMAT RVAGSLCLAT GLGHGMIVNS
LEEYEEKAVS LALNKPKLQA LTKELRASRL TCPLFDTMRW VKNLERSYFK MWNLHCSGQQ
PQHFKVLEND LEFPHDR
