STT3_YEAST
ID STT3_YEAST Reviewed; 718 AA.
AC P39007; D6VUB5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3;
DE Short=Oligosaccharyl transferase subunit STT3;
DE EC=2.4.99.18;
DE AltName: Full=Staurosporine and temperature sensitivity protein 3;
GN Name=STT3; OrderedLocusNames=YGL022W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7590309; DOI=10.1016/0378-1119(95)00431-5;
RA Yoshida S., Ohya Y., Nakano A., Anraku Y.;
RT "STT3, a novel essential gene related to the PKC1/STT1 protein kinase
RT pathway, is involved in protein glycosylation in yeast.";
RL Gene 164:167-172(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION.
RX PubMed=7588624; DOI=10.1002/j.1460-2075.1995.tb00178.x;
RA Zufferey R., Knauer R., Burda P., Stagljar I., Te Heesen S., Lehle L.,
RA Aebi M.;
RT "STT3, a highly conserved protein required for yeast oligosaccharyl
RT transferase activity in vivo.";
RL EMBO J. 14:4949-4960(1995).
RN [5]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=9405463; DOI=10.1074/jbc.272.51.32513;
RA Karaoglu D., Kelleher D.J., Gilmore R.;
RT "The highly conserved Stt3 protein is a subunit of the yeast
RT oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p.";
RL J. Biol. Chem. 272:32513-32520(1997).
RN [6]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=9435788; DOI=10.1007/s004380050611;
RA Spirig U., Glavas M., Bodmer D., Reiss G., Burda P., Lippuner V.,
RA te Heesen S., Aebi M.;
RT "The STT3 protein is a component of the yeast oligosaccharyltransferase
RT complex.";
RL Mol. Gen. Genet. 256:628-637(1997).
RN [7]
RP INTERACTION WITH OST3 AND OST4.
RX PubMed=10677492; DOI=10.1073/pnas.040556797;
RA Kim H., Park H., Montalvo L., Lennarz W.J.;
RT "Studies on the role of the hydrophobic domain of Ost4p in interactions
RT with other subunits of yeast oligosaccharyl transferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1516-1520(2000).
RN [8]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11580295; DOI=10.1021/bi0111911;
RA Karaoglu D., Kelleher D.J., Gilmore R.;
RT "Allosteric regulation provides a molecular mechanism for preferential
RT utilization of the fully assembled dolichol-linked oligosaccharide by the
RT yeast oligosaccharyltransferase.";
RL Biochemistry 40:12193-12206(2001).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF TRP-516; TRP-517; ASP-518; TYR-519; GLY-520
RP AND ILE-593.
RX PubMed=12359722; DOI=10.1074/jbc.m208136200;
RA Yan Q., Lennarz W.J.;
RT "Studies on the function of oligosaccharyl transferase subunits. Stt3p is
RT directly involved in the glycosylation process.";
RL J. Biol. Chem. 277:47692-47700(2002).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP COMPOSITION OF OLIGOSACCHARYLTRANSFERASE COMPLEXES.
RX PubMed=16297388; DOI=10.1016/j.febslet.2005.10.063;
RA Schwarz M., Knauer R., Lehle L.;
RT "Yeast oligosaccharyltransferase consists of two functionally distinct sub-
RT complexes, specified by either the Ost3p or Ost6p subunit.";
RL FEBS Lett. 579:6564-6568(2005).
RN [13]
RP COMPOSITION OF OLIGOSACCHARYLTRANSFERASE COMPLEXES.
RX PubMed=16096346; DOI=10.1093/glycob/cwj025;
RA Spirig U., Bodmer D., Wacker M., Burda P., Aebi M.;
RT "The 3.4-kDa Ost4 protein is required for the assembly of two distinct
RT oligosaccharyltransferase complexes in yeast.";
RL Glycobiology 15:1396-1406(2005).
RN [14]
RP COMPOSITION OF OLIGOSACCHARYLTRANSFERASE COMPLEXES.
RX PubMed=16096345; DOI=10.1093/glycob/cwj026;
RA Yan A., Lennarz W.J.;
RT "Two oligosaccharyl transferase complexes exist in yeast and associate with
RT two different translocons.";
RL Glycobiology 15:1407-1415(2005).
RN [15]
RP TOPOLOGY, AND MUTAGENESIS OF ARG-159; SER-160; SER-164; TRP-208; GLY-210;
RP VAL-393 AND ARG-404.
RX PubMed=15781470; DOI=10.1074/jbc.m412213200;
RA Kim H., von Heijne G., Nilsson I.;
RT "Membrane topology of the STT3 subunit of the oligosaccharyl transferase
RT complex.";
RL J. Biol. Chem. 280:20261-20267(2005).
RN [16]
RP INTERACTION WITH SEC61.
RX PubMed=15831493; DOI=10.1074/jbc.m502858200;
RA Chavan M., Yan A., Lennarz W.J.;
RT "Subunits of the translocon interact with components of the oligosaccharyl
RT transferase complex.";
RL J. Biol. Chem. 280:22917-22924(2005).
RN [17]
RP TOPOLOGY, AND INTERACTION WITH OST3; OST4; OST6; WBP1 AND SWP1.
RX PubMed=15886282; DOI=10.1073/pnas.0502669102;
RA Yan A., Wu E., Lennarz W.J.;
RT "Studies of yeast oligosaccharyl transferase subunits using the split-
RT ubiquitin system: topological features and in vivo interactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7121-7126(2005).
RN [18]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [19]
RP STRUCTURE BY NMR OF 465-718, AND TOPOLOGY.
RX PubMed=22865878; DOI=10.1074/jbc.m112.342253;
RA Huang C., Bhaskaran R., Mohanty S.;
RT "Eukaryotic N-glycosylation occurs via the membrane-anchored C-terminal
RT domain of the Stt3p subunit of oligosaccharyltransferase.";
RL J. Biol. Chem. 287:32450-32458(2012).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS).
RX PubMed=29466327; DOI=10.1038/nature25755;
RA Bai L., Wang T., Zhao G., Kovach A., Li H.;
RT "The atomic structure of a eukaryotic oligosaccharyltransferase complex.";
RL Nature 555:328-333(2018).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), GLYCOSYLATION AT
RP ASN-539, AND MUTAGENESIS OF ASP-47; ASP-166; GLU-168; GLU-350; ARG-404 AND
RP LYS-586.
RX PubMed=29301962; DOI=10.1126/science.aar5140;
RA Wild R., Kowal J., Eyring J., Ngwa E.M., Aebi M., Locher K.P.;
RT "Structure of the yeast oligosaccharyltransferase complex gives insight
RT into eukaryotic N-glycosylation.";
RL Science 359:545-550(2018).
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 (PubMed:12359722). This subunit contains the active
CC site and the acceptor peptide and donor lipid-linked oligosaccharide
CC (LLO) binding pockets (PubMed:29301962). {ECO:0000269|PubMed:12359722,
CC ECO:0000269|PubMed:29301962}.
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:0000269|PubMed:11580295};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21.3 uM for an Asn-Tyr-Thr tripeptide
CC {ECO:0000269|PubMed:11580295};
CC KM=0.094 uM for Glc(3)Man(9)GlcNAc(2)-PP-Dol
CC {ECO:0000269|PubMed:11580295};
CC Note=Glycosylates at a rate of 3.5 peptides per minute per OST.
CC {ECO:0000269|PubMed:29301962};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:12359722}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex,
CC which appears to exist in two assemblies comprising OST1, OST2, OST4,
CC OST5, STT3, SWP1, WPB1, and either OST3 or OST6 (PubMed:10677492,
CC PubMed:16297388, PubMed:16096345, PubMed:15831493, PubMed:15886282,
CC PubMed:9405463, PubMed:9435788, PubMed:29301962). OST assembly occurs
CC through the formation of 3 subcomplexes. Subcomplex 1 contains OST1 and
CC OST5, subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3
CC contains OST2, WBP1, and SWP1 (PubMed:29301962). Interacts with SEC61
CC (PubMed:15831493). {ECO:0000269|PubMed:10677492,
CC ECO:0000269|PubMed:15831493, ECO:0000269|PubMed:15886282,
CC ECO:0000269|PubMed:16096345, ECO:0000269|PubMed:16297388,
CC ECO:0000269|PubMed:29301962, ECO:0000269|PubMed:9405463,
CC ECO:0000269|PubMed:9435788}.
CC -!- INTERACTION:
CC P39007; Q99380: OST4; NbExp=6; IntAct=EBI-18447, EBI-12689;
CC P39007; P32915: SEC61; NbExp=2; IntAct=EBI-18447, EBI-16400;
CC P39007; P33767: WBP1; NbExp=2; IntAct=EBI-18447, EBI-12658;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:29301962}.
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:0000305|PubMed:29301962}.
CC -!- MISCELLANEOUS: Present with 3000 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the STT3 family. {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; D28952; BAA06079.1; -; Genomic_DNA.
DR EMBL; Z72544; CAA96722.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08076.1; -; Genomic_DNA.
DR PIR; S64024; S64024.
DR RefSeq; NP_011493.1; NM_001180887.1.
DR PDB; 2LGZ; NMR; -; A=465-718.
DR PDB; 6C26; EM; 3.50 A; A=1-718.
DR PDB; 6EZN; EM; 3.30 A; F=1-718.
DR PDB; 7OCI; EM; 3.46 A; F=1-718.
DR PDBsum; 2LGZ; -.
DR PDBsum; 6C26; -.
DR PDBsum; 6EZN; -.
DR PDBsum; 7OCI; -.
DR AlphaFoldDB; P39007; -.
DR BMRB; P39007; -.
DR SMR; P39007; -.
DR BioGRID; 33224; 646.
DR ComplexPortal; CPX-1638; Oligosaccharyl transferase complex variant 1.
DR ComplexPortal; CPX-1639; Oligosaccharyl transferase complex variant 2.
DR DIP; DIP-2459N; -.
DR IntAct; P39007; 8.
DR MINT; P39007; -.
DR STRING; 4932.YGL022W; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR TCDB; 9.B.142.3.14; the integral membrane glycosyltransferase family 39 (gt39) family.
DR iPTMnet; P39007; -.
DR MaxQB; P39007; -.
DR PaxDb; P39007; -.
DR PRIDE; P39007; -.
DR EnsemblFungi; YGL022W_mRNA; YGL022W; YGL022W.
DR GeneID; 852862; -.
DR KEGG; sce:YGL022W; -.
DR SGD; S000002990; STT3.
DR VEuPathDB; FungiDB:YGL022W; -.
DR eggNOG; KOG2292; Eukaryota.
DR GeneTree; ENSGT00940000155488; -.
DR HOGENOM; CLU_009279_1_0_1; -.
DR InParanoid; P39007; -.
DR OMA; VAYSSWY; -.
DR BioCyc; MetaCyc:YGL022W-MON; -.
DR BioCyc; YEAST:YGL022W-MON; -.
DR BRENDA; 2.4.99.18; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:P39007; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P39007; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:SGD.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043687; P:post-translational protein modification; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR DisProt; DP01195; -.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Magnesium; Manganese; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..718
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit STT3"
FT /id="PRO_0000072293"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 9..30
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 31..118
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 119..137
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 138..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 140..157
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 158..168
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 189..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 191..205
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 206..210
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 211..227
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 228..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 233..258
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 259..266
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 267..286
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 287..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 301..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..355
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 356..378
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 379..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 385..401
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 402..405
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 406..427
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 428..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29466327"
FT TRANSMEM 442..464
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29466327"
FT TOPO_DOM 465..718
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29466327"
FT REGION 516..518
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT REGION 694..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..47
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 166..168
FT /note="DXD motif 2"
FT /evidence="ECO:0000305|PubMed:29301962"
FT MOTIF 347..350
FT /note="SVSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 516..520
FT /note="WWDYG motif"
FT /evidence="ECO:0000305|PubMed:29301962"
FT MOTIF 583..590
FT /note="DK motif"
FT /evidence="ECO:0000305|PubMed:29301962"
FT BINDING 47
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 404
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 521
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 47
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 159
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 350
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 586
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:29301962"
FT MUTAGEN 47
FT /note="D->A: Lethal; impairs the catalytic activity."
FT /evidence="ECO:0000269|PubMed:29301962"
FT MUTAGEN 159
FT /note="R->A: Temperature sensitive and staurosporine
FT sensitive."
FT /evidence="ECO:0000269|PubMed:15781470"
FT MUTAGEN 160
FT /note="S->A: Temperature sensitive and staurosporine
FT sensitive."
FT /evidence="ECO:0000269|PubMed:15781470"
FT MUTAGEN 163
FT /note="G->R: Temperature sensitive and staurosporine
FT sensitive."
FT MUTAGEN 164
FT /note="S->A: Temperature sensitive and staurosporine
FT sensitive."
FT /evidence="ECO:0000269|PubMed:15781470"
FT MUTAGEN 166
FT /note="D->A: Lethal; impairs the catalytic activity."
FT /evidence="ECO:0000269|PubMed:29301962"
FT MUTAGEN 168
FT /note="E->Q: Lethal; impairs the catalytic activity."
FT /evidence="ECO:0000269|PubMed:29301962"
FT MUTAGEN 208
FT /note="W->A: Lethal; abolishes interaction with OST1 and
FT WBP1."
FT /evidence="ECO:0000269|PubMed:15781470"
FT MUTAGEN 210
FT /note="G->D: Temperature sensitive and staurosporine
FT sensitive."
FT /evidence="ECO:0000269|PubMed:15781470"
FT MUTAGEN 350
FT /note="E->A: Lethal; impairs the catalytic activity."
FT /evidence="ECO:0000269|PubMed:29301962"
FT MUTAGEN 393
FT /note="V->I: Staurosporine sensitive."
FT /evidence="ECO:0000269|PubMed:15781470"
FT MUTAGEN 404
FT /note="R->A: Lethal; abolishes interaction with OST1 and
FT WBP1."
FT /evidence="ECO:0000269|PubMed:15781470,
FT ECO:0000269|PubMed:29301962"
FT MUTAGEN 516..519
FT /note="WWDY->AAAA: Lethal; greatly reduces amount of OST1
FT in complex."
FT MUTAGEN 516
FT /note="W->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12359722"
FT MUTAGEN 517
FT /note="W->A: Lethal."
FT /evidence="ECO:0000269|PubMed:12359722"
FT MUTAGEN 518
FT /note="D->A: Lethal."
FT /evidence="ECO:0000269|PubMed:12359722"
FT MUTAGEN 519
FT /note="Y->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12359722"
FT MUTAGEN 520
FT /note="G->D: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12359722"
FT MUTAGEN 554..556
FT /note="EEK->AAA: Temperature-sensitive; reduces amount of
FT OST1 in complex."
FT MUTAGEN 586
FT /note="K->A: Temperature sensitive."
FT /evidence="ECO:0000269|PubMed:29301962"
FT MUTAGEN 592..594
FT /note="RIS->AAA: Lethal; reduces glycosylation; greatly
FT reduces amount of OST1 in complex."
FT MUTAGEN 593
FT /note="I->D: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12359722"
FT HELIX 9..30
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 31..39
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:6C26"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 172..188
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 267..286
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 356..362
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 366..369
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 370..378
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 385..401
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 406..427
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 442..473
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:2LGZ"
FT HELIX 495..505
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:2LGZ"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:6C26"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 520..526
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 540..550
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 554..563
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 575..578
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:6C26"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 588..595
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 622..625
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 628..633
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 634..637
FT /evidence="ECO:0007829|PDB:6C26"
FT STRAND 640..642
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 645..647
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 664..671
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 692..698
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 705..708
FT /evidence="ECO:0007829|PDB:2LGZ"
FT STRAND 712..716
FT /evidence="ECO:0007829|PDB:2LGZ"
SQ SEQUENCE 718 AA; 81529 MW; D00B8FF7B2B11B9F CRC64;
MGSDRSCVLS VFQTILKLVI FVAIFGAAIS SRLFAVIKFE SIIHEFDPWF NYRATKYLVN
NSFYKFLNWF DDRTWYPLGR VTGGTLYPGL MTTSAFIWHA LRNWLGLPID IRNVCVLFAP
LFSGVTAWAT YEFTKEIKDA SAGLLAAGFI AIVPGYISRS VAGSYDNEAI AITLLMVTFM
FWIKAQKTGS IMHATCAALF YFYMVSAWGG YVFITNLIPL HVFLLILMGR YSSKLYSAYT
TWYAIGTVAS MQIPFVGFLP IRSNDHMAAL GVFGLIQIVA FGDFVKGQIS TAKFKVIMMV
SLFLILVLGV VGLSALTYMG LIAPWTGRFY SLWDTNYAKI HIPIIASVSE HQPVSWPAFF
FDTHFLIWLF PAGVFLLFLD LKDEHVFVIA YSVLCSYFAG VMVRLMLTLT PVICVSAAVA
LSKIFDIYLD FKTSDRKYAI KPAALLAKLI VSGSFIFYLY LFVFHSTWVT RTAYSSPSVV
LPSQTPDGKL ALIDDFREAY YWLRMNSDED SKVAAWWDYG YQIGGMADRT TLVDNNTWNN
THIAIVGKAM ASPEEKSYEI LKEHDVDYVL VIFGGLIGFG GDDINKFLWM IRISEGIWPE
EIKERDFYTA EGEYRVDARA SETMRNSLLY KMSYKDFPQL FNGGQATDRV RQQMITPLDV
PPLDYFDEVF TSENWMVRIY QLKKDDAQGR TLRDVGELTR SSTKTRRSIK RPELGLRV
