OST2_YEAST
ID OST2_YEAST Reviewed; 130 AA.
AC P46964; D6W2G3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2;
DE Short=Oligosaccharyl transferase subunit OST2;
DE AltName: Full=Oligosaccharyl transferase 16 kDa subunit;
DE AltName: Full=Oligosaccharyl transferase subunit epsilon;
GN Name=OST2; OrderedLocusNames=YOR103C; ORFNames=YOR3211C;
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 2-28 AND 33-40, AND
RP MUTAGENESIS OF SER-16; GLU-25; LYS-31; ASP-48; GLN-61; CYS-62; ARG-69;
RP GLY-80; GLY-86; ALA-112; GLU-113; LEU-119; PHE-123 AND HIS-127.
RX PubMed=7593165; DOI=10.1083/jcb.131.2.371;
RA Silberstein S., Collins P.G., Kelleher D.J., Gilmore R.;
RT "The essential OST2 gene encodes the 16-kD subunit of the yeast
RT oligosaccharyltransferase, a highly conserved protein expressed in diverse
RT eukaryotic organisms.";
RL J. Cell Biol. 131:371-383(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
RP INTERACTION WITH SEC61 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 [13]
RP TOPOLOGY, AND INTERACTION WITH OST1; OST3; OST4; 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 [14]
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 [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-130.
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 [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 1-130.
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 P46964; P52870: SBH1; NbExp=2; IntAct=EBI-12673, EBI-16410;
CC P46964; P32915: SEC61; NbExp=2; IntAct=EBI-12673, EBI-16400;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000269|PubMed:29301962}.
CC -!- SIMILARITY: Belongs to the DAD/OST2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA64024.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA99300.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U32307; AAC49086.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64024.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z75010; CAA99300.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006948; DAA10879.1; -; Genomic_DNA.
DR PIR; S61662; S61662.
DR RefSeq; NP_014746.2; NM_001183522.1.
DR PDB; 6C26; EM; 3.50 A; 2=1-130.
DR PDB; 6EZN; EM; 3.30 A; B=1-130.
DR PDB; 7OCI; EM; 3.46 A; B=1-130.
DR PDBsum; 6C26; -.
DR PDBsum; 6EZN; -.
DR PDBsum; 7OCI; -.
DR AlphaFoldDB; P46964; -.
DR SMR; P46964; -.
DR BioGRID; 34500; 377.
DR ComplexPortal; CPX-1638; Oligosaccharyl transferase complex variant 1.
DR ComplexPortal; CPX-1639; Oligosaccharyl transferase complex variant 2.
DR DIP; DIP-2455N; -.
DR IntAct; P46964; 10.
DR MINT; P46964; -.
DR STRING; 4932.YOR103C; -.
DR TCDB; 9.B.142.3.14; the integral membrane glycosyltransferase family 39 (gt39) family.
DR MaxQB; P46964; -.
DR PaxDb; P46964; -.
DR PRIDE; P46964; -.
DR EnsemblFungi; YOR103C_mRNA; YOR103C; YOR103C.
DR GeneID; 854270; -.
DR KEGG; sce:YOR103C; -.
DR SGD; S000005629; OST2.
DR VEuPathDB; FungiDB:YOR103C; -.
DR eggNOG; KOG1746; Eukaryota.
DR GeneTree; ENSGT00390000003324; -.
DR HOGENOM; CLU_111220_1_1_1; -.
DR InParanoid; P46964; -.
DR OMA; FIFAHII; -.
DR BioCyc; MetaCyc:YOR103C-MON; -.
DR BioCyc; YEAST:YOR103C-MON; -.
DR BRENDA; 2.4.99.18; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:P46964; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P46964; 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:ComplexPortal.
DR InterPro; IPR003038; DAD/Ost2.
DR PANTHER; PTHR10705; PTHR10705; 1.
DR Pfam; PF02109; DAD; 1.
DR PIRSF; PIRSF005588; DAD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7593165"
FT CHAIN 2..130
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit OST2"
FT /id="PRO_0000124032"
FT TOPO_DOM 2..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29301962"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TOPO_DOM 67..71
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29301962"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TOPO_DOM 93..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29301962"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT MUTAGEN 16
FT /note="S->P: In OST2-3; ts; reduced activity."
FT MUTAGEN 25
FT /note="E->G: In OST2-3; ts; reduced activity."
FT MUTAGEN 31
FT /note="K->M: In OST2-1; ts; reduced activity."
FT MUTAGEN 48
FT /note="D->V: In OST2-2; ts; reduced activity."
FT MUTAGEN 61
FT /note="Q->R: In OST2-3; ts; reduced activity."
FT MUTAGEN 62
FT /note="C->S: In OST2-1; ts; reduced activity."
FT MUTAGEN 69
FT /note="R->C: In OST2-6; ts; reduced activity."
FT MUTAGEN 80
FT /note="G->E: In OST2-1; ts; reduced activity."
FT MUTAGEN 86
FT /note="G->R: In OST2-4; ts; reduced activity."
FT MUTAGEN 112
FT /note="A->S: In OST2-6; ts; reduced activity."
FT MUTAGEN 113
FT /note="E->K: In OST2-6; ts; reduced activity."
FT MUTAGEN 113
FT /note="E->V: In OST2-5; ts; reduced activity."
FT MUTAGEN 119
FT /note="L->S: In OST2-2; ts; reduced activity."
FT MUTAGEN 123
FT /note="F->L: In OST2-2; ts; reduced activity."
FT MUTAGEN 127
FT /note="H->Y: In OST2-1; ts; reduced activity."
FT HELIX 24..40
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 42..67
FT /evidence="ECO:0007829|PDB:6EZN"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 75..99
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 109..128
FT /evidence="ECO:0007829|PDB:6EZN"
SQ SEQUENCE 130 AA; 14698 MW; B317E20D32B3573D CRC64;
MAKAPKANTP KVTSTSSAVL TDFQETFKTS KRAYFAQIEK YPKLKLIDTF CFFLVLLGVI
QCTFIILIRD NFPFNAFLAG FIICVGQFVL LMSLRLQLCN SFPGISKNRA FAEFIVASLI
LHFVCLHFIN
