(data stored in SCRATCH zone)

SWISSPROT: C5DCH6_LACTC

ID   C5DCH6_LACTC            Unreviewed;       485 AA.
AC   C5DCH6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 46.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 {ECO:0000256|RuleBase:RU361143};
GN   OrderedLocusNames=KLTH0B03146g {ECO:0000313|EMBL:CAR21487.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21487.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21487.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex
CC       that catalyzes the initial transfer of a defined glycan
CC       (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier
CC       dolichol-pyrophosphate to an asparagine residue within an Asn-X-
CC       Ser/Thr consensus motif in nascent polypeptide chains, the first
CC       step in protein N-glycosylation. N-glycosylation occurs
CC       cotranslationally and the complex associates with the Sec61
CC       complex at the channel-forming translocon complex that mediates
CC       protein translocation across the endoplasmic reticulum (ER). All
CC       subunits are required for a maximal enzyme activity.
CC       {ECO:0000256|RuleBase:RU361143}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|RuleBase:RU361143}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000256|RuleBase:RU361143}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU361143}; Single-pass type I membrane
CC       protein {ECO:0000256|RuleBase:RU361143}.
CC   -!- SIMILARITY: Belongs to the OST1 family.
CC       {ECO:0000256|RuleBase:RU361143}.
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DR   EMBL; CU928166; CAR21487.1; -; Genomic_DNA.
DR   RefSeq; XP_002551925.1; XM_002551879.1.
DR   STRING; 381046.XP_002551925.1; -.
DR   EnsemblFungi; CAR21487; CAR21487; KLTH0B03146g.
DR   GeneID; 8290758; -.
DR   KEGG; lth:KLTH0B03146g; -.
DR   HOGENOM; HOG000093925; -.
DR   InParanoid; C5DCH6; -.
DR   KO; K12666; -.
DR   OMA; NDATAPE; -.
DR   OrthoDB; 1294725at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR007676; Ribophorin_I.
DR   PANTHER; PTHR21049; PTHR21049; 1.
DR   Pfam; PF04597; Ribophorin_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DCH6.
DR   SWISS-2DPAGE; C5DCH6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU361143};
KW   Membrane {ECO:0000256|RuleBase:RU361143};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Transmembrane {ECO:0000256|RuleBase:RU361143};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361143}.
FT   TRANSMEM    459    476       Helical. {ECO:0000256|RuleBase:RU361143}.
SQ   SEQUENCE   485 AA;  55038 MW;  343916F4CB5B034B CRC64;
     MYYKCSSLLK TVGEMLSATR LAAIFLLFLN FVVGDLDAGI IPKLWENLEL HRTIDVSRSY
     TQELVDIRIK NIHDEPVRQY YFVLPEEVFD AISLFSSTLK GVDAYIESAI MPEQNFVANG
     RTIKVGVIGL PSPIEPGHET SILLNLVYNS RYQPYPGHVD LGEEQKLLLR TNRFPISAYN
     TQKYTLEFQG SSSFEELQSF NGEEHAGMVA NGKMVVGPFD SIMPYEDFSP IEVVFEHNTP
     LPRVSHLKRD IWVSHWASSL QFEEYYELIN DAASLKSGFS RADYMKGQHA LKKGGHLTAL
     EMILPDSSEA HYCTDLVGAV STFKVLKDHF FLKPRYPLFG NWKYNFTVGW TNQLSQFLHS
     QEDGSDTYIL SFPILNGPAD TVYDSVSLSI YLPEGAEVLD VWCPLPVQKT EVTTEKSYFD
     LNQGHTKVNI ELKNLIDRIA GSEAFVRYKV TSTTFYKKPF SIAVSVFTAL MAYFFLKHIS
     LMIDS
//

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