OST1_YEAST
ID OST1_YEAST Reviewed; 476 AA.
AC P41543; D6VWH3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1;
DE AltName: Full=N-linked oligosaccharyl transferase subunit 1;
DE AltName: Full=Oligosaccharyl transferase 64 kDa subunit;
DE AltName: Full=Oligosaccharyl transferase subunit OST1;
DE AltName: Full=Oligosaccharyl transferase subunit alpha;
DE Flags: Precursor;
GN Name=OST1; Synonyms=NLT1; OrderedLocusNames=YJL002C; ORFNames=J1404;
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 PROTEIN SEQUENCE OF 23-38 AND
RP 135-165.
RX PubMed=7860628; DOI=10.1083/jcb.128.4.525;
RA Silberstein S., Collins P.G., Kelleher D.J., Rapiejko P.J., Gilmore R.;
RT "The alpha subunit of the Saccharomyces cerevisiae
RT oligosaccharyltransferase complex is essential for vegetative growth of
RT yeast and is homologous to mammalian ribophorin I.";
RL J. Cell Biol. 128:525-536(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7720878; DOI=10.1016/0014-5793(95)00253-6;
RA Pathak R., Parker C.S., Imperiali B.;
RT "The essential yeast NLT1 gene encodes the 64 kDa glycoprotein subunit of
RT the oligosaccharyl transferase.";
RL FEBS Lett. 362:229-234(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 23-34, AND 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 [6]
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 [7]
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 [8]
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 [9]
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 [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 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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-476.
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 [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 1-476, AND
RP GLYCOSYLATION AT ASN-336 AND ASN-400.
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, 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 P41543; P35179: SSS1; NbExp=2; IntAct=EBI-12651, EBI-16406;
CC P41543; Q02795: SWP1; NbExp=3; IntAct=EBI-12651, EBI-12666;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8181570}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:29301962}.
CC -!- MISCELLANEOUS: Present with 11900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the OST1 family. {ECO:0000305}.
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DR EMBL; Z46719; CAA86674.1; -; Genomic_DNA.
DR EMBL; U22326; AAA85158.1; -; Genomic_DNA.
DR EMBL; X87611; CAA60920.1; -; Genomic_DNA.
DR EMBL; Z49277; CAA89291.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08789.1; -; Genomic_DNA.
DR PIR; A56510; A56510.
DR RefSeq; NP_012532.3; NM_001181436.3.
DR PDB; 6C26; EM; 3.50 A; 1=1-476.
DR PDB; 6EZN; EM; 3.30 A; A=1-476.
DR PDB; 7OCI; EM; 3.46 A; A=1-476.
DR PDBsum; 6C26; -.
DR PDBsum; 6EZN; -.
DR PDBsum; 7OCI; -.
DR AlphaFoldDB; P41543; -.
DR SMR; P41543; -.
DR BioGRID; 33755; 208.
DR ComplexPortal; CPX-1638; Oligosaccharyl transferase complex variant 1.
DR ComplexPortal; CPX-1639; Oligosaccharyl transferase complex variant 2.
DR DIP; DIP-2454N; -.
DR IntAct; P41543; 27.
DR MINT; P41543; -.
DR STRING; 4932.YJL002C; -.
DR BindingDB; P41543; -.
DR TCDB; 9.B.142.3.14; the integral membrane glycosyltransferase family 39 (gt39) family.
DR iPTMnet; P41543; -.
DR MaxQB; P41543; -.
DR PaxDb; P41543; -.
DR PRIDE; P41543; -.
DR EnsemblFungi; YJL002C_mRNA; YJL002C; YJL002C.
DR GeneID; 853455; -.
DR KEGG; sce:YJL002C; -.
DR SGD; S000003539; OST1.
DR VEuPathDB; FungiDB:YJL002C; -.
DR eggNOG; KOG2291; Eukaryota.
DR GeneTree; ENSGT00390000009630; -.
DR HOGENOM; CLU_031381_1_0_1; -.
DR InParanoid; P41543; -.
DR OMA; KTYMDTL; -.
DR BioCyc; MetaCyc:YJL002C-MON; -.
DR BioCyc; YEAST:YJL002C-MON; -.
DR BRENDA; 2.4.99.18; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:P41543; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P41543; 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:0006487; P:protein N-linked glycosylation; IDA:SGD.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:SGD.
DR InterPro; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049; PTHR21049; 1.
DR Pfam; PF04597; Ribophorin_I; 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..22
FT /evidence="ECO:0000269|PubMed:7860628,
FT ECO:0000269|PubMed:8181570"
FT CHAIN 23..476
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1"
FT /id="PRO_0000021960"
FT TOPO_DOM 23..449
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TOPO_DOM 471..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29301962"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29301962"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29301962"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 72..76
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 128..138
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6C26"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 231..243
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 248..259
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 334..344
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 358..365
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 399..406
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 416..423
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:6EZN"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 448..466
FT /evidence="ECO:0007829|PDB:6EZN"
SQ SEQUENCE 476 AA; 54072 MW; EFD989B50AAED348 CRC64;
MRQVWFSWIV GLFLCFFNVS SAAQYEPPAT WENVDYKRTI DVSNAYISET IEITIKNIAS
EPATEYFTAF ESGIFSKVSF FSAYFTNEAT FLNSQLLANS TTAPGDDGES EIRYGIIQFP
NAISPQEEVS LVIKSFYNTV GIPYPEHVGM SEEQHLLWET NRLPLSAYDT KKASFTLIGS
SSFEEYHPPN DESLLGKANG NSFEFGPWED IPRFSSNETL AIVYSHNAPL NQVVNLRRDI
WLSHWASTIQ FEEYYELTNK AAKLSKGFSR LELMKQIQTQ NMRQTHFVTV LDMLLPEGAT
DHYFTDLVGL VSTSHAERDH FFIRPRFPIF GGWNYNFTVG WTNKLSDFLH VSSGSDEKFV
ASIPILNGPP DTVYDNVELS VFLPEGAEIF DIDSPVPFTN VSIETQKSYF DLNKGHVKLT
FSYRNLISQV ANGQVLIKYD YPKSSFFKKP LSIACYIFTA LMGVFVLKTL NMNVTN
