ID   OST48_XENTR             Reviewed;         437 AA.
AC   B1H3C9;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2008) 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; BC161349; AAI61349.1; -; mRNA.
DR   RefSeq; NP_001120481.1; NM_001127009.1.
DR   AlphaFoldDB; B1H3C9; -.
DR   SMR; B1H3C9; -.
DR   GeneID; 100145597; -.
DR   KEGG; xtr:100145597; -.
DR   CTD; 1650; -.
DR   Xenbase; XB-GENE-5784936; ddost.
DR   InParanoid; B1H3C9; -.
DR   OrthoDB; 975158at2759; -.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
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; IBA:GO_Central.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..437
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase 48 kDa subunit"
FT                   /id="PRO_0000357450"
FT   TOPO_DOM        25..407
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   437 AA;  48265 MW;  7EFC5A3A302885B4 CRC64;
     MASLRVSVLL VAASCLLLGS GLRAGPRTLV LLENINLRET HSLFFRSLSD RGFDLSFRTA
     DDPSLSLIKY GEFLYDNLII FSPSVEDFGG NINIETISSF IDGGGSVLVA ASSDIGDPLR
     ELGSECGIEF DEDKTAVIDH HNYDISDPGQ HSLIVADSES LLKAPTIVGK APLNPILFRG
     VGMVADPDNP LVLDILTGSS TSYSFFPDKP ITQYPHAVGK NTLLIAGLQA RNNARVVFSG
     SMDFFSDAFF NSAVQKAAGG SNRYAKTGNY ELAVALSRWV FKEEGVLRVG QVSHHRVGES
     SPPSAYTVTD LVEYSIVIEQ LSNGKWVPFD GDDIQLEFVR IDPFVRTFLK KNGGKYSVQF
     KLPDVYGVFQ FKVDYNRLGY THLYSTTQVS VRPLQHTQYE RFIPSAYPYY ASAFSVMFGL
     FIFSIVFLHM KEKEKSD