STT3A_ARATH
ID STT3A_ARATH Reviewed; 779 AA.
AC Q93ZY3; Q94A42;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A;
DE Short=Oligosaccharyl transferase subunit STT3A;
DE Short=STT3-A;
DE EC=2.4.99.18;
DE AltName: Full=Integral membrane protein 1;
DE AltName: Full=Protein STAUROSPORIN AND TEMPERATURE SENSITIVE 3-LIKE A;
GN Name=STT3A; OrderedLocusNames=At5g19690; ORFNames=T29J13_110;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
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 [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=12972670; DOI=10.1105/tpc.013862;
RA Koiwa H., Li F., McCully M.G., Mendoza I., Koizumi N., Manabe Y.,
RA Nakagawa Y., Zhu J., Rus A., Pardo J.M., Bressan R.A., Hasegawa P.M.;
RT "The STT3a subunit isoform of the Arabidopsis oligosaccharyltransferase
RT controls adaptive responses to salt/osmotic stress.";
RL Plant Cell 15:2273-2284(2003).
RN [5]
RP FUNCTION.
RX PubMed=19763086; DOI=10.1038/emboj.2009.262;
RA Nekrasov V., Li J., Batoux M., Roux M., Chu Z.H., Lacombe S., Rougon A.,
RA Bittel P., Kiss-Papp M., Chinchilla D., van Esse H.P., Jorda L.,
RA Schwessinger B., Nicaise V., Thomma B.P., Molina A., Jones J.D., Zipfel C.;
RT "Control of the pattern-recognition receptor EFR by an ER protein complex
RT in plant immunity.";
RL EMBO J. 28:3428-3438(2009).
RN [6]
RP FUNCTION.
RX PubMed=19763087; DOI=10.1038/emboj.2009.263;
RA Saijo Y., Tintor N., Lu X., Rauf P., Pajerowska-Mukhtar K., Haeweker H.,
RA Dong X., Robatzek S., Schulze-Lefert P.;
RT "Receptor quality control in the endoplasmic reticulum for plant innate
RT immunity.";
RL EMBO J. 28:3439-3449(2009).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=22923678; DOI=10.1104/pp.112.204263;
RA Nikolovski N., Rubtsov D., Segura M.P., Miles G.P., Stevens T.J.,
RA Dunkley T.P., Munro S., Lilley K.S., Dupree P.;
RT "Putative glycosyltransferases and other plant Golgi apparatus proteins are
RT revealed by LOPIT proteomics.";
RL Plant Physiol. 160:1037-1051(2012).
CC -!- FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST)
CC complex that catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC the complex associates with the Sec61 complex at the channel-forming
CC translocon complex that mediates protein translocation across the
CC endoplasmic reticulum (ER). All subunits are required for a maximal
CC enzyme activity. This subunit contains the active site and the acceptor
CC peptide and donor lipid-linked oligosaccharide (LLO) binding pockets
CC (By similarity). Controls adaptive responses to salt/osmotic stress.
CC Acts as a key glycosylation determinant for EFR function during plant
CC innate immunity (PubMed:12972670, PubMed:19763086, PubMed:19763087).
CC {ECO:0000250|UniProtKB:P39007, ECO:0000269|PubMed:12972670,
CC ECO:0000269|PubMed:19763086, ECO:0000269|PubMed:19763087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein]
CC = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-
CC acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-
CC asparaginy-[protein]; Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:9529,
CC Rhea:RHEA-COMP:12635, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:12805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:57497,
CC ChEBI:CHEBI:57570, ChEBI:CHEBI:132529; EC=2.4.99.18;
CC Evidence={ECO:0000250|UniProtKB:P39007};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22923678}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22923678}.
CC -!- TISSUE SPECIFICITY: Expressed in the root and in the shoot.
CC {ECO:0000269|PubMed:12972670}.
CC -!- DOMAIN: Despite low primary sequence conservation between eukaryotic
CC catalytic subunits and bacterial and archaeal single subunit OSTs
CC (ssOST), structural comparison revealed several common motifs at
CC spatially equivalent positions, like the DXD motif 1 on the external
CC loop 1 and the DXD motif 2 on the external loop 2 involved in binding
CC of the metal ion cofactor and the carboxamide group of the acceptor
CC asparagine, the conserved Glu residue of the TIXE/SVSE motif on the
CC external loop 5 involved in catalysis, as well as the WWDYG and the
CC DK/MI motifs in the globular domain that define the binding pocket for
CC the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg
CC residue was found to interact with a negatively charged side chain at
CC the -2 position of the sequon. This Arg is conserved in bacterial
CC enzymes and correlates with an extended sequon requirement (Asp-X-Asn-
CC X-Ser/Thr) for bacterial N-glycosylation.
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- DISRUPTION PHENOTYPE: Salt/osmotic sensitivity associated with root tip
CC growth arrest and swelling and the induction of lateral roots.
CC {ECO:0000269|PubMed:12972670}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; AF296838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92738.1; -; Genomic_DNA.
DR EMBL; AY050397; AAK91413.1; -; mRNA.
DR EMBL; AY056191; AAL07040.1; -; mRNA.
DR EMBL; AY059649; AAL31142.1; -; mRNA.
DR RefSeq; NP_568380.1; NM_121974.5.
DR AlphaFoldDB; Q93ZY3; -.
DR SMR; Q93ZY3; -.
DR BioGRID; 17365; 10.
DR STRING; 3702.AT5G19690.1; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR SwissPalm; Q93ZY3; -.
DR PaxDb; Q93ZY3; -.
DR PRIDE; Q93ZY3; -.
DR ProteomicsDB; 228274; -.
DR EnsemblPlants; AT5G19690.1; AT5G19690.1; AT5G19690.
DR GeneID; 832089; -.
DR Gramene; AT5G19690.1; AT5G19690.1; AT5G19690.
DR KEGG; ath:AT5G19690; -.
DR Araport; AT5G19690; -.
DR TAIR; locus:2183149; AT5G19690.
DR eggNOG; KOG2292; Eukaryota.
DR HOGENOM; CLU_009279_1_0_1; -.
DR InParanoid; Q93ZY3; -.
DR OMA; RNACGGV; -.
DR OrthoDB; 187775at2759; -.
DR PhylomeDB; Q93ZY3; -.
DR BRENDA; 2.4.99.18; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q93ZY3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93ZY3; baseline and differential.
DR Genevisible; Q93ZY3; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Magnesium;
KW Manganese; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..779
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit STT3A"
FT /id="PRO_0000420536"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..124
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 144..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 146..163
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 164..174
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..194
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 195..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..211
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 212..216
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..233
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 234..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 239..264
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 265..272
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 293..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..364
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 365..387
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 388..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 394..410
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 411..414
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 415..436
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 437..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..779
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 448..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..587
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT REGION 754..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 52..54
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 172..174
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 356..359
FT /note="SVSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 585..589
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 652..659
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT COMPBIAS 448..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 413
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 590
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 54
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 165
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 359
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 655
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT CONFLICT 735
FT /note="T -> K (in Ref. 3; AAK91413/AAL31142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 779 AA; 86113 MW; 74F702FF6772478B CRC64;
MAALESPLPG TPTAMRNAFG NVLSVLILVL IGVLAFSIRL FSVIKYESVI HEFDPYFNYR
VTQFLSKNGI YEFWNWFDDR TWYPLGRVIG GTVYPGLTLT AGTIWWGLNS LNIPLSVETV
CVFTAPVFSA FASWATYLLT KEVKGSGAGL AAAALLAMVP SYISRSVAGS YDNEAVAIFA
LIFTFYLYIK TLNTGSLFYA TLNALAYFYM VCSWGGYTFI INLIPMHVLL CIVTGRYSPR
LYIAYAPLVV LGTLLAALVP VVGFNAVLTS EHFASFLVFI IIHVVALVYY IKGILSPKMF
KVAVTLVVSI GMVVCFIVVA ILVALVASSP TGGWSGRSLS LLDPTYASKY IPIIASVSEH
QPPTWPSYFM DINVLAFLVP AGIIACFSPL SDASSFVVLY IVMSVYFSGV MVRLMLVLAP
AACIMSGIAL SQAFDVFTGS IKYQLGASSN STDDAEDNTS TNNAPKDDVS AGKTDKGEEI
VKERSSKKGK KKEREPADKP SVKAKIKKKA LVLPLEASIV ALLLLIMLGA FYVIHCVWAA
AEAYSAPSIV LTSQSRDGLH VFDDFRESYA WLSHNTDVDD KVASWWDYGY QTTAMANRTV
IVDNNTWNNT HIATVGTAMS SPEKAAWEIF NSLDVKYVLV VFGGLIGYPS DDINKFLWMV
RIGGGVFPHI KEADYLRDGQ YRIDSEATPT MLNSLMYKLS YYRFVETDGK GYDRVRRTEI
GKKHFKLTHF EEVFTSHHWM VRLYKLKPPR NRIRGKAKKL KSKTSSGLSS KSAKKNPWV
