OST3_YEAST
ID OST3_YEAST Reviewed; 350 AA.
AC P48439; D6W2E7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3;
DE AltName: Full=Oligosaccharyl transferase 34 kDa subunit;
DE AltName: Full=Oligosaccharyl transferase subunit OST3;
DE AltName: Full=Oligosaccharyl transferase subunit gamma;
DE Flags: Precursor;
GN Name=OST3; OrderedLocusNames=YOR085W; ORFNames=YOR3124W;
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 23-37; 99-103;
RP 123-153 AND 345-350.
RX PubMed=7622558; DOI=10.1083/jcb.130.3.567;
RA Karaoglu D., Kelleher D.J., Gilmore R.;
RT "Functional characterization of Ost3p. Loss of the 34-kD subunit of the
RT Saccharomyces cerevisiae oligosaccharyltransferase results in biased
RT underglycosylation of acceptor substrates.";
RL J. Cell Biol. 130:567-577(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
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 [3]
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 [4]
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 [5]
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 [6]
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 [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, AND INTERACTION
RP WITH OST4 AND STT3.
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 INTERACTION WITH OST4 AND STT3.
RX PubMed=10677492; DOI=10.1073/pnas.040556797;
RA Kim H., Park H., Montalvo L., Lennarz W.J.;
RT "Studies on the role of the hydrophobic domain of Ost4p in interactions
RT with other subunits of yeast oligosaccharyl transferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1516-1520(2000).
RN [11]
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 [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 TOPOLOGY, AND INTERACTION WITH OST1; OST2; OST4 AND STT3.
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 1-350.
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 1-350.
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:10677492,
CC PubMed:16297388, PubMed:16096345, PubMed:15886282, PubMed:9405463,
CC PubMed:29301962). OST assembly occurs through the formation of 3
CC subcomplexes. Subcomplex 1 contains OST1 and OST5, subcomplex 2
CC contains STT3, OST3, and OST4, and subcomplex 3 contains OST2, WBP1,
CC and SWP1 (PubMed:29301962). {ECO:0000269|PubMed:10677492,
CC ECO:0000269|PubMed:15886282, ECO:0000269|PubMed:16096345,
CC ECO:0000269|PubMed:16297388, ECO:0000269|PubMed:29301962,
CC ECO:0000269|PubMed:9405463}.
CC -!- INTERACTION:
CC P48439; Q99380: OST4; NbExp=2; IntAct=EBI-12680, EBI-12689;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000269|PubMed:29301962}.
CC -!- MISCELLANEOUS: Present with 4030 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; U25052; AAC49042.1; -; Genomic_DNA.
DR EMBL; X79596; CAA56108.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64007.1; -; Genomic_DNA.
DR EMBL; Z74993; CAA99280.1; -; Genomic_DNA.
DR EMBL; AY558041; AAS56367.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10863.1; -; Genomic_DNA.
DR PIR; S61646; S61646.
DR RefSeq; NP_014728.1; NM_001183504.1.
DR PDB; 6C26; EM; 3.50 A; 3=1-350.
DR PDB; 6EZN; EM; 3.30 A; C=1-350.
DR PDBsum; 6C26; -.
DR PDBsum; 6EZN; -.
DR AlphaFoldDB; P48439; -.
DR SMR; P48439; -.
DR BioGRID; 34483; 429.
DR ComplexPortal; CPX-1639; Oligosaccharyl transferase complex variant 2.
DR DIP; DIP-2456N; -.
DR IntAct; P48439; 4.
DR STRING; 4932.YOR085W; -.
DR TCDB; 1.A.76.1.8; the magnesium transporter1 (magt1) family.
DR TCDB; 9.B.142.3.14; the integral membrane glycosyltransferase family 39 (gt39) family.
DR MaxQB; P48439; -.
DR PaxDb; P48439; -.
DR PRIDE; P48439; -.
DR TopDownProteomics; P48439; -.
DR EnsemblFungi; YOR085W_mRNA; YOR085W; YOR085W.
DR GeneID; 854252; -.
DR KEGG; sce:YOR085W; -.
DR SGD; S000005611; OST3.
DR VEuPathDB; FungiDB:YOR085W; -.
DR eggNOG; KOG2603; Eukaryota.
DR GeneTree; ENSGT00390000012030; -.
DR HOGENOM; CLU_052855_1_0_1; -.
DR InParanoid; P48439; -.
DR OMA; NLWAAVS; -.
DR BioCyc; MetaCyc:YOR085W-MON; -.
DR BioCyc; YEAST:YOR085W-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 PRO; PR:P48439; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P48439; 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; IMP:SGD.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:SGD.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IMP:SGD.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:SGD.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR GO; GO:0035269; P:protein O-linked mannosylation; IGI:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IGI:SGD.
DR DisProt; DP01196; -.
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; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:7622558"
FT CHAIN 23..350
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 3"
FT /id="PRO_0000020275"
FT TOPO_DOM 23..182
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TOPO_DOM 239..273
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TOPO_DOM 295..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29301962"
FT TOPO_DOM 328..350
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 29..171
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 73..76
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:6C26"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 269..289
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:6EZN"
FT HELIX 305..334
FT /evidence="ECO:0007829|PDB:6EZN"
SQ SEQUENCE 350 AA; 39483 MW; EEA573BC14E99380 CRC64;
MNWLFLVSLV FFCGVSTHPA LAMSSNRLLK LANKSPKKII PLKDSSFENI LAPPHENAYI
VALFTATAPE IGCSLCLELE SEYDTIVASW FDDHPDAKSS NSDTSIFFTK VNLEDPSKTI
PKAFQFFQLN NVPRLFIFKP NSPSILDHSV ISISTDTGSE RMKQIIQAIK QFSQVNDFSL
HLPMDWTPII TSTIITFITV LLFKKQSKLM FSIISSRIIW ATLSTFFIIC MISAYMFNQI
RNTQLAGVGP KGEVMYFLPN EFQHQFAIET QVMVLIYGTL AALVVVLVKG IQFLRSHLYP
ETKKAYFIDA ILASFCALFI YVFFAALTTV FTIKSPAYPF PLLRLSAPFK
