OST6_YEAST
ID OST6_YEAST Reviewed; 332 AA.
AC Q03723; D6VZF5; E9P904;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6;
DE Short=Oligosaccharyl transferase subunit OST6;
DE AltName: Full=Oligosaccharyl transferase 37 kDa subunit;
DE Short=OTase 37 kDa subunit;
DE Flags: Precursor;
GN Name=OST6; OrderedLocusNames=YML019W;
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], AND IDENTIFICATION IN THE OLIGOSACCHARYL
RP TRANSFERASE COMPLEX.
RX PubMed=10358084; DOI=10.1074/jbc.274.24.17249;
RA Knauer R., Lehle L.;
RT "The oligosaccharyltransferase complex from Saccharomyces cerevisiae.
RT Isolation of the OST6 gene, its synthetic interaction with OST3, and
RT analysis of the native complex.";
RL J. Biol. Chem. 274:17249-17256(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP REVIEW ON OLIGOSACCHARYL TRANSFERASE.
RX PubMed=9878773; DOI=10.1016/s0304-4165(98)00128-7;
RA Knauer R., Lehle L.;
RT "The oligosaccharyltransferase complex from yeast.";
RL Biochim. Biophys. Acta 1426:259-273(1999).
RN [6]
RP FUNCTION.
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 [7]
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 [8]
RP COMPOSITION OF OLIGOSACCHARYL TRANSFERASE 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 [9]
RP COMPOSITION OF OLIGOSACCHARYL TRANSFERASE 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 [10]
RP COMPOSITION OF OLIGOSACCHARYL TRANSFERASE 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 [11]
RP TOPOLOGY, AND INTERACTION WITH OST1; OST2; OST4; STT3; 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 [12]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 24-188, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, REDOX POTENTIAL, AND MUTAGENESIS OF CYS-78
RP AND CYS-81.
RX PubMed=19549845; DOI=10.1073/pnas.0812515106;
RA Schulz B.L., Stirnimann C.U., Grimshaw J.P., Brozzo M.S., Fritsch F.,
RA Mohorko E., Capitani G., Glockshuber R., Grutter M.G., Aebi M.;
RT "Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and
RT Ost6p defines site-specific glycosylation efficiency.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:11061-11066(2009).
CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC 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:11580295). Can participate in redox reactions
CC and is able to catalyze dithiol-disulfide exchange reactions with other
CC proteins, albeit with relatively low efficiency. May form transient
CC disulfide bonds with nascent polypeptides in the endoplasmic reticulum
CC and thereby promote efficient glycosylation (PubMed:19549845).
CC {ECO:0000269|PubMed:11580295, ECO:0000269|PubMed:19549845}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -275 mV. {ECO:0000269|PubMed:19549845};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:9878773}.
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:10358084,
CC PubMed:16297388, PubMed:16096345, PubMed:15886282). 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 (By similarity).
CC {ECO:0000250|UniProtKB:P48439, ECO:0000269|PubMed:10358084,
CC ECO:0000269|PubMed:15886282, ECO:0000269|PubMed:16096345,
CC ECO:0000269|PubMed:16297388}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
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DR EMBL; Y08606; CAA69898.1; -; Genomic_DNA.
DR EMBL; Z46659; CAA86636.1; -; Genomic_DNA.
DR EMBL; AY692974; AAT92993.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09879.1; -; Genomic_DNA.
DR PIR; S49758; S49758.
DR RefSeq; NP_013693.1; NM_001182377.1.
DR PDB; 3G7Y; X-ray; 2.21 A; A=24-188.
DR PDB; 3G9B; X-ray; 1.96 A; A=24-188.
DR PDB; 3GA4; X-ray; 1.30 A; A=24-188.
DR PDB; 7OCI; EM; 3.46 A; C=1-332.
DR PDBsum; 3G7Y; -.
DR PDBsum; 3G9B; -.
DR PDBsum; 3GA4; -.
DR PDBsum; 7OCI; -.
DR AlphaFoldDB; Q03723; -.
DR SMR; Q03723; -.
DR BioGRID; 35150; 168.
DR ComplexPortal; CPX-1638; Oligosaccharyl transferase complex variant 1.
DR DIP; DIP-3851N; -.
DR IntAct; Q03723; 3.
DR STRING; 4932.YML019W; -.
DR MaxQB; Q03723; -.
DR PaxDb; Q03723; -.
DR PRIDE; Q03723; -.
DR DNASU; 854989; -.
DR EnsemblFungi; YML019W_mRNA; YML019W; YML019W.
DR GeneID; 854989; -.
DR KEGG; sce:YML019W; -.
DR SGD; S000004481; OST6.
DR VEuPathDB; FungiDB:YML019W; -.
DR eggNOG; KOG2603; Eukaryota.
DR GeneTree; ENSGT00390000012030; -.
DR HOGENOM; CLU_052855_2_1_1; -.
DR InParanoid; Q03723; -.
DR OMA; WQFGIEI; -.
DR BioCyc; MetaCyc:YML019W-MON; -.
DR BioCyc; YEAST:YML019W-MON; -.
DR BRENDA; 2.4.99.18; 984.
DR Reactome; R-SCE-5223345; Miscellaneous transport and binding events.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR UniPathway; UPA00378; -.
DR EvolutionaryTrace; Q03723; -.
DR PRO; PR:Q03723; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03723; 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:0015035; F:protein-disulfide reductase activity; IDA:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; IGI:SGD.
DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR PANTHER; PTHR12692; PTHR12692; 1.
DR Pfam; PF04756; OST3_OST6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endoplasmic reticulum; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..332
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit OST6"
FT /id="PRO_0000058098"
FT TOPO_DOM 25..188
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..267
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..332
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 35..162
FT /note="Thioredoxin"
FT DISULFID 78..81
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT MUTAGEN 78
FT /note="C->S: Alters glycosyltransferase efficiency towards
FT a subset of target proteins; when associated with S-81."
FT /evidence="ECO:0000269|PubMed:19549845"
FT MUTAGEN 81
FT /note="C->S: Alters glycosyltransferase efficiency towards
FT a subset of target proteins; when associated with S-78."
FT /evidence="ECO:0000269|PubMed:19549845"
FT CONFLICT 33
FT /note="I -> T (in Ref. 4; AAT92993)"
FT /evidence="ECO:0000305"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:3GA4"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3GA4"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3GA4"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:3GA4"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:3GA4"
FT HELIX 79..98
FT /evidence="ECO:0007829|PDB:3GA4"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:3GA4"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3GA4"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:3GA4"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:3GA4"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:3GA4"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:3GA4"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3GA4"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3GA4"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:3GA4"
SQ SEQUENCE 332 AA; 37891 MW; FC7AE156BF27F1B5 CRC64;
MKWCSTYIII WLAIIFHKFQ KSTATASHNI DDILQLKDDT GVITVTADNY PLLSRGVPGY
FNILYITMRG TNSNGMSCQL CHDFEKTYHA VADVIRSQAP QSLNLFFTVD VNEVPQLVKD
LKLQNVPHLV VYPPAESNKQ SQFEWKTSPF YQYSLVPENA ENTLQFGDFL AKILNISITV
PQAFNVQEFV YYFVACMVVF IFIKKVILPK VTNKWKLFSM ILSLGILLPS ITGYKFVEMN
AIPFIARDAK NRIMYFSGGS GWQFGIEIFS VSLMYIVMSA LSVLLIYVPK ISCVSEKMRG
LLSSFLACVL FYFFSYFISC YLIKNPGYPI VF
