ID   DAD1_BETPN              Reviewed;         115 AA.
AC   Q9M3T9;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1;
DE            Short=Oligosaccharyl transferase subunit DAD1;
DE   AltName: Full=Defender against cell death 1;
DE            Short=DAD-1;
GN   Name=DAD1; Synonyms=DAD;
OS   Betula pendula (European white birch) (Betula verrucosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Betula.
OX   NCBI_TaxID=3505;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Korhonen M.S., Palva T.E., Kangasjarvi J.;
RL   Submitted (JAN-2000) 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. 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}.
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; AJ279687; CAB66329.1; -; mRNA.
DR   AlphaFoldDB; Q9M3T9; -.
DR   SMR; Q9M3T9; -.
DR   UniPathway; UPA00378; -.
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..115
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit DAD1"
FT                   /id="PRO_0000124021"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..55
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   115 AA;  12575 MW;  ADC5B0597D258B93 CRC64;
     MARSTSKDAQ ALIQSLRSAY AATPSNLKII DLYVVFAVFT ALIQVVYMAI VGSFPFNAFL
     SGLLSCIGTA VLAVCLRIQV NKENKEFKDL APERAFADFV LCNLVLHLVI MNFLG