ID   DAD1_XENLA              Reviewed;         113 AA.
AC   P46967; Q66KN9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit dad1 {ECO:0000250|UniProtKB:P61803};
DE            Short=Oligosaccharyl transferase subunit dad1;
DE   AltName: Full=Defender against cell death 1;
DE            Short=DAD-1;
GN   Name=dad1 {ECO:0000250|UniProtKB:P61803};
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 [MRNA].
RX   PubMed=8413235; DOI=10.1128/mcb.13.10.6367-6374.1993;
RA   Nakashima T., Sekiguchi T., Kuraoka A., Fukushima K., Shibata Y.,
RA   Komiyama S., Nishimoto T.;
RT   "Molecular cloning of a human cDNA encoding a novel protein, DAD1, whose
RT   defect causes apoptotic cell death in hamster BHK21 cells.";
RL   Mol. Cell. Biol. 13:6367-6374(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-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. {ECO:0000250|UniProtKB:E2R4X3,
CC       ECO:0000250|UniProtKB:P61803}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P61803}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:E2R4X3}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DAD/OST2 family. {ECO:0000305}.
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DR   EMBL; D15059; BAA03652.1; -; mRNA.
DR   EMBL; BC078613; AAH78613.1; -; mRNA.
DR   PIR; B54437; B54437.
DR   RefSeq; NP_001081227.1; NM_001087758.2.
DR   RefSeq; XP_018097873.1; XM_018242384.1.
DR   AlphaFoldDB; P46967; -.
DR   SMR; P46967; -.
DR   DNASU; 397721; -.
DR   GeneID; 397721; -.
DR   KEGG; xla:397721; -.
DR   CTD; 397721; -.
DR   Xenbase; XB-GENE-922833; dad1.S.
DR   OrthoDB; 1586516at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 397721; Expressed in testis 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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR   InterPro; IPR003038; DAD/Ost2.
DR   PANTHER; PTHR10705; PTHR10705; 1.
DR   Pfam; PF02109; DAD; 1.
DR   PIRSF; PIRSF005588; DAD; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..113
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit dad1"
FT                   /id="PRO_0000124016"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   113 AA;  12596 MW;  B8B4FB18524D59B2 CRC64;
     MSVSVFSVVS RFLDEYVSST PQRLKLLDAY LLYILLTGAL QFLYCLLVGT FPFNSFLSGF
     ISSVGSFILA VCLRIQINPQ NKSDFQGISP ERAFADFLFA NTILHLVVVN FIG