OSTD_YEAST
ID OSTD_YEAST Reviewed; 286 AA.
AC Q02795; D6VZX1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1;
DE Short=Oligosaccharyl transferase subunit SWP1;
DE AltName: Full=Oligosaccharyl transferase subunit delta;
DE Flags: Precursor;
GN Name=SWP1; OrderedLocusNames=YMR149W; ORFNames=YM9375.19;
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].
RX PubMed=8428586;
RA Te Heesen S., Knauer R., Lehle L., Aebi M.;
RT "Yeast Wbp1p and Swp1p form a protein complex essential for oligosaccharyl
RT transferase activity.";
RL EMBO J. 12:279-284(1993).
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 PROTEIN SEQUENCE OF 20-35, AND IDENTIFICATION IN THE OLIGOSACCHARYL
RP TRANSFERASE COMPLEX.
RX PubMed=8175708; DOI=10.1016/s0021-9258(18)99962-x;
RA Kelleher D.J., Gilmore R.;
RT "The Saccharomyces cerevisiae oligosaccharyltransferase is a protein
RT complex composed of Wbp1p, Swp1p, and four additional polypeptides.";
RL J. Biol. Chem. 269:12908-12917(1994).
RN [6]
RP PROTEIN SEQUENCE OF 20-26.
RX PubMed=7703229; DOI=10.1021/bi00013a005;
RA Pathak R., Hendrickson T.L., Imperiali B.;
RT "Sulfhydryl modification of the yeast Wbp1p inhibits oligosaccharyl
RT transferase activity.";
RL Biochemistry 34:4179-4185(1995).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=8181570; DOI=10.1016/0014-5793(94)00356-4;
RA Knauer R., Lehle L.;
RT "The N-oligosaccharyltransferase complex from yeast.";
RL FEBS Lett. 344:83-86(1994).
RN [8]
RP IDENTIFICATION IN THE OLIGOSACCHARYL TRANSFERASE 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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
RP INTERACTION WITH SSS1 AND 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 OST1; OST2; OST4; STT3 AND WBP1.
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 STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-286.
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 [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 1-286.
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: 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. {ECO:0000269|PubMed:11580295}.
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:8175708,
CC PubMed:16297388, PubMed:16096345, PubMed:15831493, PubMed:15886282,
CC PubMed:9405463, PubMed:29301962). OST assembly occurs through the
CC formation of 3 subcomplexes. Subcomplex 1 contains OST1 and OST5,
CC subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3 contains
CC OST2, WBP1, and SWP1 (PubMed:29301962). Interacts with SEC61 and SSS1
CC (PubMed:15831493). {ECO:0000269|PubMed:15831493,
CC ECO:0000269|PubMed:15886282, ECO:0000269|PubMed:16096345,
CC ECO:0000269|PubMed:16297388, ECO:0000269|PubMed:29301962,
CC ECO:0000269|PubMed:8175708, ECO:0000269|PubMed:9405463}.
CC -!- INTERACTION:
CC Q02795; P41543: OST1; NbExp=3; IntAct=EBI-12666, EBI-12651;
CC Q02795; Q99380: OST4; NbExp=6; IntAct=EBI-12666, EBI-12689;
CC Q02795; P32915: SEC61; NbExp=3; IntAct=EBI-12666, EBI-16400;
CC Q02795; P35179: SSS1; NbExp=2; IntAct=EBI-12666, EBI-16406;
CC Q02795; P33767: WBP1; NbExp=3; IntAct=EBI-12666, EBI-12658;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8181570}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:29301962}.
CC -!- MISCELLANEOUS: Present with 8450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SWP1 family. {ECO:0000305}.
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DR EMBL; X67705; CAA47943.1; -; Genomic_DNA.
DR EMBL; Z47071; CAA87364.1; -; Genomic_DNA.
DR EMBL; AY558418; AAS56744.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10045.1; -; Genomic_DNA.
DR PIR; S28416; S28416.
DR RefSeq; NP_013869.1; NM_001182651.1.
DR PDB; 6C26; EM; 3.50 A; C=1-286.
DR PDB; 6EZN; EM; 3.30 A; H=1-286.
DR PDB; 7OCI; EM; 3.46 A; H=1-286.
DR PDBsum; 6C26; -.
DR PDBsum; 6EZN; -.
DR PDBsum; 7OCI; -.
DR AlphaFoldDB; Q02795; -.
DR SMR; Q02795; -.
DR BioGRID; 35325; 290.
DR ComplexPortal; CPX-1638; Oligosaccharyl transferase complex variant 1.
DR ComplexPortal; CPX-1639; Oligosaccharyl transferase complex variant 2.
DR DIP; DIP-2460N; -.
DR IntAct; Q02795; 36.
DR MINT; Q02795; -.
DR STRING; 4932.YMR149W; -.
DR TCDB; 9.B.142.3.14; the integral membrane glycosyltransferase family 39 (gt39) family.
DR MaxQB; Q02795; -.
DR PaxDb; Q02795; -.
DR PRIDE; Q02795; -.
DR TopDownProteomics; Q02795; -.
DR EnsemblFungi; YMR149W_mRNA; YMR149W; YMR149W.
DR GeneID; 855180; -.
DR KEGG; sce:YMR149W; -.
DR SGD; S000004757; SWP1.
DR VEuPathDB; FungiDB:YMR149W; -.
DR eggNOG; KOG2447; Eukaryota.
DR HOGENOM; CLU_079423_0_0_1; -.
DR InParanoid; Q02795; -.
DR OMA; SIVTHYV; -.
DR BioCyc; MetaCyc:YMR149W-MON; -.
DR BioCyc; YEAST:YMR149W-MON; -.
DR BRENDA; 2.4.99.18; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q02795; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q02795; protein.
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:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR InterPro; IPR008814; Swp1.
DR PANTHER; PTHR12640; PTHR12640; 1.
DR Pfam; PF05817; Ribophorin_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:7703229,
FT ECO:0000269|PubMed:8175708"
FT CHAIN 20..286
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit SWP1"
FT /id="PRO_0000021962"
FT TOPO_DOM 20..194
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29301962"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TOPO_DOM 216..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TOPO_DOM 250..252
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TOPO_DOM 274..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6C26"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:6C26"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6C26"
FT HELIX 193..215
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 231..252
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:6EZN"
SQ SEQUENCE 286 AA; 31653 MW; 53D15B8857A534E5 CRC64;
MQFFKTLAAL VSCISFVLAY VAQDVHVSFP STAGKSRVMI GKVEPRIGID ETVPTTITVE
DPNEVIQVNF AIESTNKPFQ NTLLIGLPNK NLEMAFEPEI KDNGKLSMYK YRIDLAKLDA
ALLQEASRSP EPIKATLILA SSTAKPKENL FREILQLNLN FDVDHSDSSL VDKFGIKPEI
HHIFHAEPKR VAKPIAVIFV LIIFITILSL IVTWLNSCAA AFNNIPTGVT AVYFLGFIAT
IVGFEVIFAR YYLGTSIFET LFSSLYLGAP GLLTSTKFLR SFGQTI
