ID   DAD2_HORVU              Reviewed;         114 AA.
AC   Q9SME8;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2;
DE            Short=Oligosaccharyl transferase subunit DAD2;
DE   AltName: Full=Defender against cell death 2;
DE            Short=DAD-2;
GN   Name=DAD2;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10781951; DOI=10.1016/s0925-4773(00)00254-9;
RA   Lindholm P., Kuittinen T., Sorri O., Guo D., Merits A., Tormakangas K.,
RA   Runeberg-Roos P.;
RT   "Glycosylation of phytepsin and expression of dad1, dad2 and ost1 during
RT   onset of cell death in germinating barley scutella.";
RL   Mech. Dev. 93:169-173(2000).
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:P46964}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:P46964}.
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; AJ133277; CAB56224.1; -; mRNA.
DR   AlphaFoldDB; Q9SME8; -.
DR   SMR; Q9SME8; -.
DR   EnsemblPlants; HORVU.MOREX.r2.7HG0530900.1; HORVU.MOREX.r2.7HG0530900.1; HORVU.MOREX.r2.7HG0530900.
DR   EnsemblPlants; HORVU.MOREX.r2.7HG0530900.1.mrna1; HORVU.MOREX.r2.7HG0530900.1.mrna1; HORVU.MOREX.r2.7HG0530900.1.
DR   Gramene; HORVU.MOREX.r2.7HG0530900.1; HORVU.MOREX.r2.7HG0530900.1; HORVU.MOREX.r2.7HG0530900.
DR   Gramene; HORVU.MOREX.r2.7HG0530900.1.mrna1; HORVU.MOREX.r2.7HG0530900.1.mrna1; HORVU.MOREX.r2.7HG0530900.1.
DR   OMA; MGKSATT; -.
DR   UniPathway; UPA00378; -.
DR   ExpressionAtlas; Q9SME8; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..114
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit DAD2"
FT                   /id="PRO_0000124024"
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..54
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        76..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   114 AA;  12304 MW;  46BA9FD2ECEF5182 CRC64;
     MPKAAGDAKL LIQSLNKAYA ATPTNLKIID LYVVFAVATA LVQVVYMGIV GSFPFNSFLS
     GVLSSIGTAV LGVCLRIQVN KDNKEFKDLP PERAFADFVL CNLVLHLVIM NFLG