STT3B_ARATH
ID STT3B_ARATH Reviewed; 735 AA.
AC Q9FX21; Q0WN68;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B;
DE Short=Oligosaccharyl transferase subunit STT3B;
DE Short=STT3-B;
DE EC=2.4.99.18;
DE AltName: Full=Protein STAUROSPORIN AND TEMPERATURE SENSITIVE 3-LIKE B;
GN Name=STT3B; OrderedLocusNames=At1g34130; ORFNames=F12G12.5;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 515-735.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE, 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 [6]
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 {ECO:0000250|UniProtKB:P39007}.
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 preferentially in the root but also in
CC the shoot. {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: No visible phenotype.
CC {ECO:0000269|PubMed:12972670}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX816490; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC015446; AAG12524.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31675.1; -; Genomic_DNA.
DR EMBL; BX816490; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK229582; BAF01432.1; -; mRNA.
DR PIR; D86465; D86465.
DR RefSeq; NP_174675.2; NM_103136.4.
DR AlphaFoldDB; Q9FX21; -.
DR SMR; Q9FX21; -.
DR STRING; 3702.AT1G34130.1; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR SwissPalm; Q9FX21; -.
DR PaxDb; Q9FX21; -.
DR PRIDE; Q9FX21; -.
DR ProteomicsDB; 228275; -.
DR EnsemblPlants; AT1G34130.1; AT1G34130.1; AT1G34130.
DR GeneID; 840312; -.
DR Gramene; AT1G34130.1; AT1G34130.1; AT1G34130.
DR KEGG; ath:AT1G34130; -.
DR Araport; AT1G34130; -.
DR TAIR; locus:2009051; AT1G34130.
DR eggNOG; KOG2292; Eukaryota.
DR HOGENOM; CLU_009279_1_0_1; -.
DR InParanoid; Q9FX21; -.
DR OMA; VAYSSWY; -.
DR OrthoDB; 187775at2759; -.
DR PhylomeDB; Q9FX21; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9FX21; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FX21; baseline and differential.
DR Genevisible; Q9FX21; 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:0005634; C:nucleus; 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 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..735
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit STT3B"
FT /id="PRO_0000420537"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..142
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 162..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 164..181
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 182..192
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 213..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..229
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 230..234
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 235..251
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 252..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 257..282
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 283..290
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 291..310
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 311..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..380
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 404..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 410..426
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 427..430
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 431..452
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 453..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..735
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 562..564
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 70..72
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 190..192
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 372..375
FT /note="SVSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 562..566
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 629..636
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT BINDING 72
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 190
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 192
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 429
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 567
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 72
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 183
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 375
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 632
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT CONFLICT 595
FT /note="A -> P (in Ref. 3; BX816490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 735 AA; 82980 MW; DBBB06AD4D97CAB4 CRC64;
MGGKSEPAKS ESMATKPDLL NTSFFSFKSL KLKTKQQELL LRISILGLVY ILAFIARLFS
VLRYESMIHE FDPYFNYRTT LFLTEKGFYE FWNWFDSESW YPLGRIIGGT LYPGLMVTAA
LIYWTLRFLR FFVHIREVCV LTAPFFASNT TLVAYFFGKE LWDTGAGLVA AVLIAICPGY
ISRSVAGSYD NEAVAIFALL LTFYLFVKAV NTGSLAWALA SAFGYFYMVS AWGGYVFIIN
LVPLYVLVLL ITGRYSMRLY IAYNCMYILG MLLAMQIRFV GFQHVQSGEH MGAMGVFLLM
QVFYFLDWVK YQLNDTKLFQ TFLRITVTSA ILVGGVAVGV GTASGYISPW TGRFYSLLDP
TYAKDHIPII ASVSEHQPTA WSSFMFDYHI LLFLFPAGLY FCFKRLTDAT IFIVMYGLTS
LYFAGVMVRL ILVATPAVCL ISAIAVSATI KNLTSLLRTK QKVSQTGSTK GAGSSKASSK
VTLDQSQPFQ KNGAIALLVG VFYLLSRYAI HCTWVTAEAY SSPSIVLAAR GAHGNRIIFD
DYREAYYWLR QNTATDAKIM SWWDYGYQIT AMGNRTVIVD NNTWNNTHIA TVGRAMSSYE
DDAYDIMRSL DVNYVLVVFG GVTGYSSDDI NKFLWMVRIG GGVFPVIKEP DYLVNGEFRV
DKGASPKMLN CLMYKLCYYR FGELTTEYGK PPGYDRARGV EIGNKDIKLE HLEEAYTTSN
WIVRIYRVKP PTNRL
