ID   DAD1_MESAU              Reviewed;         113 AA.
AC   P61806; O08552; O70364; P46966; P46968; Q96GB7;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 92.
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   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-38.
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).
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:0000250|UniProtKB:E2R4X3}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P61803}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST
CC       exists in two different complex forms which contain common core
CC       subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or
CC       STT3B as catalytic subunits, and form-specific accessory subunits.
CC       STT3A complex assembly occurs through the formation of 3 subcomplexes.
CC       Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the
CC       STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core
CC       subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The
CC       STT3A complex can form stable complexes with the Sec61 complex or with
CC       both the Sec61 and TRAP complexes. {ECO:0000250|UniProtKB:E2R4X3}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DAD/OST2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D15058; BAA03651.1; -; mRNA.
DR   PIR; C54437; C54437.
DR   RefSeq; NP_001268553.1; NM_001281624.1.
DR   RefSeq; XP_012980316.1; XM_013124862.3.
DR   AlphaFoldDB; P61806; -.
DR   SMR; P61806; -.
DR   STRING; 10036.ENSMAUP00000002275; -.
DR   Ensembl; ENSMAUT00000002451; ENSMAUP00000002275; ENSMAUG00000001827.
DR   GeneID; 101827723; -.
DR   KEGG; maua:101827723; -.
DR   CTD; 1603; -.
DR   eggNOG; KOG1746; Eukaryota.
DR   GeneTree; ENSGT00390000003324; -.
DR   OrthoDB; 445566at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000886700; Unplaced.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0160226; C:oligosaccharyltransferase complex A; IEA:Ensembl.
DR   GO; GO:0160227; C:oligosaccharyltransferase complex B; IEA:Ensembl.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:Ensembl.
DR   GO; GO:0009101; P:glycoprotein biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:Ensembl.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR   InterPro; IPR003038; DAD/Ost2.
DR   PANTHER; PTHR10705; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT DAD1; 1.
DR   PANTHER; PTHR10705:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT DAD1; 1.
DR   Pfam; PF02109; DAD; 1.
DR   PIRSF; PIRSF005588; DAD; 1.
PE   3: Inferred from homology;
KW   Acetylation; Apoptosis; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P61803"
FT   CHAIN           2..113
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit DAD1"
FT                   /id="PRO_0000124010"
FT   TOPO_DOM        2..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"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61803"
FT   VARIANT         38
FT                   /note="G -> R (in cell line tsBN7; confers temperature
FT                   sensitivity)"
FT                   /evidence="ECO:0000269|PubMed:8413235"
SQ   SEQUENCE   113 AA;  12497 MW;  481983CADCEB2345 CRC64;
     MSASVVSVIS RFLEEYLSST PQRLKLLDAY LLYILLTGAL QFGYCLLVGT FPFNSFLSGF
     ISCVGSFILA VCLRIQINPQ NKADFQGISP ERAFADFLFA STILHLVVMN FVG
//