ID   OST48_XENLA             Reviewed;         438 AA.
AC   Q6GNR9;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit {ECO:0000250|UniProtKB:P39656};
DE            Short=DDOST 48 kDa subunit;
DE            Short=Oligosaccharyl transferase 48 kDa subunit;
DE   Flags: Precursor;
GN   Name=ddost {ECO:0000250|UniProtKB:P39656};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). N-glycosylation occurs
CC       cotranslationally and the complex associates with the Sec61 complex at
CC       the channel-forming translocon complex that mediates protein
CC       translocation across the endoplasmic reticulum (ER). All subunits are
CC       required for a maximal enzyme activity (By similarity). Required for
CC       the assembly of both SST3A- and SS3B-containing OST complexes (By
CC       similarity). {ECO:0000250|UniProtKB:P39656,
CC       ECO:0000250|UniProtKB:Q05052}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P39656}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:Q05052}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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DR   EMBL; BC073434; AAH73434.1; -; mRNA.
DR   RefSeq; NP_001085856.1; NM_001092387.1.
DR   AlphaFoldDB; Q6GNR9; -.
DR   SMR; Q6GNR9; -.
DR   BioGRID; 102446; 1.
DR   DNASU; 444283; -.
DR   GeneID; 444283; -.
DR   KEGG; xla:444283; -.
DR   CTD; 444283; -.
DR   Xenbase; XB-GENE-5785164; ddost.S.
DR   OrthoDB; 975158at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 444283; Expressed in liver and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IEA:InterPro.
DR   InterPro; IPR005013; DDOST_48_kDa_subunit.
DR   PANTHER; PTHR10830; PTHR10830; 1.
DR   Pfam; PF03345; DDOST_48kD; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..438
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase 48 kDa subunit"
FT                   /id="PRO_0000357449"
FT   TOPO_DOM        26..408
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..438
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   438 AA;  48712 MW;  035D5A0AA2E86751 CRC64;
     MASLRLSVLL VSVSWLLLLV SGLRAGPRTL VLMENINLRE THSLFFRSLS DRGFDLSFKT
     ADDPSLSLIK YGEFLYDNLI IFSPSVEDFG GNINIETISS FIDGGGSVLV AASSDIGDPL
     RELGSECGIE FDEEKTAVID HHNYDISDPG QHTLIVADSE NLLKAPTIVG KTPLNPILFR
     GVGMVADPDN PLVLDILTGS STSYSFFPDK PITQYPHAVG KNTLLIAGLQ ARNNARVVFS
     GSLDFFSDSF FNSAVQKAAS GSNRYAKTGN YELAMALSRW VFKEEGVLRV GEVSHHRVGE
     SSPPSAYTVT DLVEYSIVIE KLSDGKWVPF DGDDIQLEFV RIDPFVRTFL KKNGGKYSVQ
     FKLPDVYGVF QFKVDYNRLG YTHLYSTTQI SVRPLQHTQY ERFIPSAYPY YASAFSVMFG
     LFIFSIVFLH MKEKEKSD