OST4_YEAST
ID OST4_YEAST Reviewed; 36 AA.
AC Q99380; D6VRC4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4;
DE Short=Oligosaccharyl transferase subunit OST4;
DE AltName: Full=Oligosaccharyl transferase 4 kDa subunit;
DE Short=OTase 4 kDa subunit;
GN Name=OST4; OrderedLocusNames=YDL232W;
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].
RC STRAIN=NDY21;
RX PubMed=8621712; DOI=10.1074/jbc.271.6.3132;
RA Chi J.H., Roos J., Dean N.;
RT "The OST4 gene of Saccharomyces cerevisiae encodes an unusually small
RT protein required for normal levels of oligosaccharyltransferase activity.";
RL J. Biol. Chem. 271:3132-3140(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [5]
RP IDENTIFICATION IN THE OLIGOSACCHARYL TRANSFERASE COMPLEX, AND INTERACTION
RP WITH OST3 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 [6]
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 [7]
RP INTERACTION WITH OST3 AND STT3, AND MUTAGENESIS OF MET-18; MET-19; THR-20;
RP LEU-21; VAL-23; ILE-24 AND TYR-25.
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 [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 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 [10]
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 [11]
RP TOPOLOGY, AND MUTAGENESIS OF MET-18; MET-19; THR-20; LEU-21; VAL-23 AND
RP ILE-24.
RX PubMed=12810948; DOI=10.1073/pnas.1332735100;
RA Kim H., Yan Q., Von Heijne G., Caputo G.A., Lennarz W.J.;
RT "Determination of the membrane topology of Ost4p and its subunit
RT interactions in the oligosaccharyltransferase complex in Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7460-7464(2003).
RN [12]
RP COMPOSITION OF THE 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 THE 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 THE 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; STT3; 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 NMR, AND TRANSMEMBRANE DOMAIN.
RX PubMed=15001703; DOI=10.1073/pnas.0400512101;
RA Zubkov S., Lennarz W.J., Mohanty S.;
RT "Structural basis for the function of a minimembrane protein subunit of
RT yeast oligosaccharyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3821-3826(2004).
RN [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS).
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).
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:10677492, PubMed:16297388, PubMed:16096345, PubMed:15831493,
CC PubMed:15886282, PubMed:9405463, PubMed:29301962). OST assembly occurs
CC through the formation of 3 subcomplexes. Subcomplex 1 contains OST1 and
CC OST5, subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3
CC contains OST2, WBP1, and SWP1 (PubMed:29301962). Interacts with SEC61,
CC SBH1 and SSS1 (PubMed:15831493). {ECO:0000269|PubMed:10677492,
CC ECO:0000269|PubMed:15831493, ECO:0000269|PubMed:15886282,
CC ECO:0000269|PubMed:16096345, ECO:0000269|PubMed:16297388,
CC ECO:0000269|PubMed:29301962, ECO:0000269|PubMed:8175708,
CC ECO:0000269|PubMed:9405463}.
CC -!- INTERACTION:
CC Q99380; P48439: OST3; NbExp=2; IntAct=EBI-12689, EBI-12680;
CC Q99380; P52870: SBH1; NbExp=2; IntAct=EBI-12689, EBI-16410;
CC Q99380; P32915: SEC61; NbExp=2; IntAct=EBI-12689, EBI-16400;
CC Q99380; P35179: SSS1; NbExp=2; IntAct=EBI-12689, EBI-16406;
CC Q99380; P39007: STT3; NbExp=6; IntAct=EBI-12689, EBI-18447;
CC Q99380; Q02795: SWP1; NbExp=6; IntAct=EBI-12689, EBI-12666;
CC Q99380; P33767: WBP1; NbExp=6; IntAct=EBI-12689, EBI-12658;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:29301962}.
CC -!- MISCELLANEOUS: Present with 2430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the OST4 family. {ECO:0000305}.
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DR EMBL; L42519; AAB06797.1; -; Genomic_DNA.
DR EMBL; Z74280; CAA98811.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11634.1; -; Genomic_DNA.
DR PIR; S67795; S67795.
DR RefSeq; NP_010049.1; NM_001180292.1.
DR PDB; 1RKL; NMR; -; A=1-36.
DR PDB; 6C26; EM; 3.50 A; 4=1-36.
DR PDB; 6EZN; EM; 3.30 A; D=1-36.
DR PDB; 6XCR; NMR; -; A=1-36.
DR PDB; 6XCU; NMR; -; A=1-36.
DR PDB; 7OCI; EM; 3.46 A; D=1-36.
DR PDBsum; 1RKL; -.
DR PDBsum; 6C26; -.
DR PDBsum; 6EZN; -.
DR PDBsum; 6XCR; -.
DR PDBsum; 6XCU; -.
DR PDBsum; 7OCI; -.
DR AlphaFoldDB; Q99380; -.
DR BMRB; Q99380; -.
DR SMR; Q99380; -.
DR BioGRID; 31879; 691.
DR ComplexPortal; CPX-1638; Oligosaccharyl transferase complex variant 1.
DR ComplexPortal; CPX-1639; Oligosaccharyl transferase complex variant 2.
DR DIP; DIP-2457N; -.
DR IntAct; Q99380; 13.
DR MINT; Q99380; -.
DR STRING; 4932.YDL232W; -.
DR TCDB; 9.B.142.3.14; the integral membrane glycosyltransferase family 39 (gt39) family.
DR PaxDb; Q99380; -.
DR EnsemblFungi; YDL232W_mRNA; YDL232W; YDL232W.
DR GeneID; 851366; -.
DR KEGG; sce:YDL232W; -.
DR SGD; S000002391; OST4.
DR VEuPathDB; FungiDB:YDL232W; -.
DR eggNOG; ENOG502SF94; Eukaryota.
DR HOGENOM; CLU_160806_3_0_1; -.
DR InParanoid; Q99380; -.
DR BioCyc; MetaCyc:YDL232W-MON; -.
DR BioCyc; YEAST:YDL232W-MON; -.
DR BRENDA; 2.4.99.18; 984.
DR UniPathway; UPA00378; -.
DR EvolutionaryTrace; Q99380; -.
DR PRO; PR:Q99380; -.
DR Proteomes; UP000002311; Chromosome IV.
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:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR InterPro; IPR018943; Oligosaccaryltransferase.
DR InterPro; IPR036330; Ost4p_sf.
DR Pfam; PF10215; Ost4; 1.
DR SUPFAM; SSF103464; SSF103464; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..36
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit OST4"
FT /id="PRO_0000058093"
FT TOPO_DOM 1..9
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:12810948"
FT TRANSMEM 10..28
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:12810948"
FT TOPO_DOM 29..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:12810948"
FT MUTAGEN 18
FT /note="M->K: Severe growth defect; abolishes interaction
FT with OST3 and STT3."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 18
FT /note="M->L: No effect on interaction between OST3 and
FT STT3."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 19
FT /note="M->K: Severe growth defect; abolishes interaction
FT with OST3."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 19
FT /note="M->L: Disrupts interaction between OST3 and STT3."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 20
FT /note="T->D: Severe growth defect."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 20
FT /note="T->K: Severe growth defect; abolishes interaction
FT with OST3; disrupts interaction between OST3 and STT3."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 21
FT /note="L->K: Abolishes interaction with OST3 and STT3;
FT disrupts interaction between OST3 and STT3."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 23
FT /note="V->D: Severe growth defect."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 23
FT /note="V->K: Severe growth defect; abolishes interaction
FT with OST3; disrupts interaction between OST3 and STT3."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 24
FT /note="I->D: Severe growth defect."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 24
FT /note="I->K: Disrupts interaction between OST3 and STT3."
FT /evidence="ECO:0000269|PubMed:10677492,
FT ECO:0000269|PubMed:12810948"
FT MUTAGEN 25
FT /note="Y->D: Severe growth defect."
FT /evidence="ECO:0000269|PubMed:10677492"
FT HELIX 4..31
FT /evidence="ECO:0007829|PDB:6EZN"
SQ SEQUENCE 36 AA; 3985 MW; BA14A9C3B197F12A CRC64;
MISDEQLNSL AITFGIVMMT LIVIYHAVDS TMSPKN
