OSTB_YEAST
ID OSTB_YEAST Reviewed; 430 AA.
AC P33767; D3DLP5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1;
DE Short=Oligosaccharyl transferase subunit WBP1;
DE AltName: Full=Oligosaccharyl transferase subunit beta;
DE Flags: Precursor;
GN Name=WBP1; OrderedLocusNames=YEL002C;
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], PROTEIN SEQUENCE OF N-TERMINUS,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=1724755;
RA Te Heesen S., Rauhut R., Aebersold R., Abelson J., Aebi M., Clark M.W.;
RT "An essential 45 kDa yeast transmembrane protein reacts with anti-nuclear
RT pore antibodies: purification of the protein, immunolocalization and
RT cloning of the gene.";
RL Eur. J. Cell Biol. 56:8-18(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 PROTEIN SEQUENCE OF 21-40.
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 [5]
RP CHARACTERIZATION.
RX PubMed=1600939;
RA Te Heesen S., Janetzky B., Lehle L., Aebi M.;
RT "The yeast WBP1 is essential for oligosaccharyl transferase activity in
RT vivo and in vitro.";
RL EMBO J. 11:2071-2075(1992).
RN [6]
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 [7]
RP IDENTIFICATION IN THE OLIGOSACCHARYL 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 [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 SEC61; SBH1 AND SSS1.
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 INTERACTION WITH OST2; OST3; OST5; 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 X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 425-430.
RX PubMed=23481256; DOI=10.1038/emboj.2013.41;
RA Ma W., Goldberg J.;
RT "Rules for the recognition of dilysine retrieval motifs by coatomer.";
RL EMBO J. 32:926-937(2013).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-430.
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 [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 1-430, AND
RP GLYCOSYLATION AT ASN-60 AND ASN-332.
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 ECO:0000269|PubMed:1600939}.
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, SBH1 and
CC SSS1 (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 P33767; P53622: COP1; NbExp=3; IntAct=EBI-12658, EBI-4860;
CC P33767; Q99380: OST4; NbExp=6; IntAct=EBI-12658, EBI-12689;
CC P33767; P52870: SBH1; NbExp=2; IntAct=EBI-12658, EBI-16410;
CC P33767; P32915: SEC61; NbExp=2; IntAct=EBI-12658, EBI-16400;
CC P33767; P35179: SSS1; NbExp=2; IntAct=EBI-12658, EBI-16406;
CC P33767; P39007: STT3; NbExp=2; IntAct=EBI-12658, EBI-18447;
CC P33767; Q02795: SWP1; NbExp=3; IntAct=EBI-12658, EBI-12666;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:1724755,
CC ECO:0000269|PubMed:8181570}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:29301962}.
CC -!- DOMAIN: The cytoplasmic C-terminal domain contains a functional
CC dilysine-retrieval motif, which is involved in the retrograde Golgi-to-
CC ER transport of the protein.
CC -!- MISCELLANEOUS: Present with 14900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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DR EMBL; X61388; CAA43660.1; -; Genomic_DNA.
DR EMBL; U18530; AAB64479.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07649.1; -; Genomic_DNA.
DR PIR; S20187; S20187.
DR RefSeq; NP_010914.3; NM_001178817.3.
DR PDB; 4J86; X-ray; 1.48 A; C/D=425-430.
DR PDB; 6C26; EM; 3.50 A; B=1-430.
DR PDB; 6EZN; EM; 3.30 A; G=1-430.
DR PDB; 7OCI; EM; 3.46 A; G=1-430.
DR PDBsum; 4J86; -.
DR PDBsum; 6C26; -.
DR PDBsum; 6EZN; -.
DR PDBsum; 7OCI; -.
DR AlphaFoldDB; P33767; -.
DR SMR; P33767; -.
DR BioGRID; 36729; 474.
DR ComplexPortal; CPX-1638; Oligosaccharyl transferase complex variant 1.
DR ComplexPortal; CPX-1639; Oligosaccharyl transferase complex variant 2.
DR DIP; DIP-676N; -.
DR ELM; P33767; -.
DR IntAct; P33767; 44.
DR MINT; P33767; -.
DR STRING; 4932.YEL002C; -.
DR TCDB; 9.B.142.3.14; the integral membrane glycosyltransferase family 39 (gt39) family.
DR iPTMnet; P33767; -.
DR MaxQB; P33767; -.
DR PaxDb; P33767; -.
DR PRIDE; P33767; -.
DR ABCD; P33767; 1 sequenced antibody.
DR EnsemblFungi; YEL002C_mRNA; YEL002C; YEL002C.
DR GeneID; 856716; -.
DR KEGG; sce:YEL002C; -.
DR SGD; S000000728; WBP1.
DR VEuPathDB; FungiDB:YEL002C; -.
DR eggNOG; KOG2754; Eukaryota.
DR GeneTree; ENSGT00390000017294; -.
DR HOGENOM; CLU_031804_1_1_1; -.
DR InParanoid; P33767; -.
DR OMA; YQFKVDY; -.
DR BioCyc; MetaCyc:YEL002C-MON; -.
DR BioCyc; YEAST:YEL002C-MON; -.
DR BRENDA; 2.4.99.18; 984.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR UniPathway; UPA00378; -.
DR PRO; PR:P33767; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P33767; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IMP:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:SGD.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:SGD.
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 InterPro; IPR005013; DDOST_48_kDa_subunit.
DR PANTHER; PTHR10830; PTHR10830; 1.
DR Pfam; PF03345; DDOST_48kD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1724755,
FT ECO:0000269|PubMed:7703229"
FT CHAIN 21..430
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit WBP1"
FT /id="PRO_0000021961"
FT TOPO_DOM 24..393
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29301962"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TOPO_DOM 415..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1724755"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29301962"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29301962"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 289..299
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 313..326
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 367..376
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 393..415
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:4J86"
SQ SEQUENCE 430 AA; 49392 MW; 495DA76BE8A9B29A CRC64;
MRTDWNFFFC ILLQAIFVVG TQTSRTLVLY DQSTEPLEEY SVYLKDLEQR NYKLEYLDIN
STSTTVDLYD KEQRLFDNII VFPTKGGKNL ARQIPVKQLI KFFENEGNIL CMSSPGAVPN
TIRLFLNELG IYPSPKGHVI RDYFSPSSEE LVVSSNHLLN KYVYNARKSE DFVFGESSAA
LLENREQIVP ILNAPRTSFT ESKGKCNSWT SGSQGFLVVG FQNLNNARLV WIGSSDFLKN
KNQDSNQEFA KELLKWTFNE KSVIKSVHAV HSHADGTSYD EEPYKIKDKV IYSVGFSEWN
GEEWLPHIAD DIQFELRQVD PYYRLTLSPS GNDSETQYYT TGEFILPDRH GVFTFLTDYR
KIGLSFTTDK DVKAIRHLAN DEYPRSWEIS NSWVYISAIC GVIVAWIFFV VSFVTTSSVG
KKLETFKKTN
