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   27-MAR-2024, entry version 190.
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   PDB; 8AGC; EM; 3.10 A; E=1-476.
DR   PDB; 8AGE; EM; 2.80 A; E=1-476.
DR   PDBsum; 6C26; -.
DR   PDBsum; 6EZN; -.
DR   PDBsum; 7OCI; -.
DR   PDBsum; 8AGC; -.
DR   PDBsum; 8AGE; -.
DR   AlphaFoldDB; P41543; -.
DR   EMDB; EMD-12808; -.
DR   EMDB; EMD-15419; -.
DR   EMDB; EMD-4161; -.
DR   EMDB; EMD-7336; -.
DR   SMR; P41543; -.
DR   BioGRID; 33755; 218.
DR   ComplexPortal; CPX-1638; Oligosaccharyl transferase complex, OST6 variant.
DR   ComplexPortal; CPX-1639; Oligosaccharyl transferase complex, OST3 variant.
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   GlyCosmos; P41543; 5 sites, No reported glycans.
DR   GlyGen; P41543; 5 sites.
DR   iPTMnet; P41543; -.
DR   MaxQB; P41543; -.
DR   PaxDb; 4932-YJL002C; -.
DR   PeptideAtlas; P41543; -.
DR   EnsemblFungi; YJL002C_mRNA; YJL002C; YJL002C.
DR   GeneID; 853455; -.
DR   KEGG; sce:YJL002C; -.
DR   AGR; SGD:S000003539; -.
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; VVYIETV; -.
DR   OrthoDB; 5265755at2759; -.
DR   BioCyc; MetaCyc:YJL002C-MONOMER; -.
DR   BioCyc; YEAST:YJL002C-MONOMER; -.
DR   BRENDA; 2.4.99.18; 984.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 853455; 0 hits in 10 CRISPR screens.
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; NAS:ComplexPortal.
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:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT 1; 1.
DR   PANTHER; PTHR21049; RIBOPHORIN I; 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          31..41
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          43..46
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          48..57
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          65..70
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           72..77
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          78..87
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          128..138
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          142..148
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          155..163
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          170..172
FT                   /evidence="ECO:0007829|PDB:6EZN"
FT   STRAND          174..181
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          183..187
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          192..194
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          197..199
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:6EZN"
FT   STRAND          218..225
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          231..243
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   TURN            244..247
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          248..259
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           270..278
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          286..289
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          291..294
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          300..306
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          307..310
FT                   /evidence="ECO:0007829|PDB:6EZN"
FT   STRAND          314..317
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          320..323
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          334..344
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           345..347
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          349..351
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          358..365
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          369..371
FT                   /evidence="ECO:0007829|PDB:7OCI"
FT   STRAND          373..375
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          377..383
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          388..393
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          399..406
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          416..423
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          425..427
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   TURN            428..430
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          434..440
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           443..467
FT                   /evidence="ECO:0007829|PDB:8AGE"
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
//