ID   DAD1_ARAVE              Reviewed;         113 AA.
AC   Q8I7Z2;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 {ECO:0000250|UniProtKB:Q9VLM5};
DE            Short=Oligosaccharyl transferase subunit DAD1 {ECO:0000250|UniProtKB:Q9VLM5};
DE   AltName: Full=Defender against apoptotic cell death 1 {ECO:0000312|EMBL:AAN86571.1};
DE   AltName: Full=Defender against cell death 1 {ECO:0000250|UniProtKB:Q9VLM5};
DE            Short=AvDAD1 {ECO:0000303|PubMed:12781979};
DE            Short=DAD-1 {ECO:0000250|UniProtKB:Q9VLM5};
GN   Name=DAD1 {ECO:0000303|PubMed:12781979};
OS   Araneus ventricosus (Orbweaver spider) (Epeira ventricosa).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Araneoidea; Araneidae; Araneus.
OX   NCBI_TaxID=182803;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAN86571.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=12781979;
RA   Lee K.S., Chung E.H., Han J.H., Sohn H.D., Jin B.R.;
RT   "cDNA cloning of a defender against apoptotic cell death 1 (DAD1)
RT   homologue, responsive to external temperature stimulus from the spider,
RT   Araneus ventricosus.";
RL   Comp. Biochem. Physiol. 135:117-123(2003).
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   -!- 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   -!- TISSUE SPECIFICITY: Widely expressed. Greatest expression seen in the
CC       epidermis, intermediate expression in the fat body and midgut and mild
CC       expression observed in the silk gland. {ECO:0000269|PubMed:12781979}.
CC   -!- INDUCTION: Expression is significantly induced at 4 degrees Celsius and
CC       at 37 degrees Celsius compared to the control which was maintained at
CC       25 degrees Celsius. There is a dramatic increase every 5 hours of each
CC       temperature treatment suggesting that over-expression is a cell
CC       response to inhibit programmed cell death by external temperature
CC       stimulus. {ECO:0000269|PubMed:12781979}.
CC   -!- SIMILARITY: Belongs to the DAD/OST2 family. {ECO:0000255}.
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DR   EMBL; AY166868; AAN86571.1; -; mRNA.
DR   AlphaFoldDB; Q8I7Z2; -.
DR   SMR; Q8I7Z2; -.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR   GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR   InterPro; IPR003038; DAD/Ost2.
DR   PANTHER; PTHR10705; PTHR10705; 1.
DR   Pfam; PF02109; DAD; 1.
DR   PIRSF; PIRSF005588; DAD; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Endoplasmic reticulum; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..113
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit DAD1"
FT                   /id="PRO_0000395396"
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;  12601 MW;  ECEEB962EDB09FA9 CRC64;
     MGSSAFEVLT FFLKDYKANT PQKLKIIDAY LLYILLTGIN QFLYCCLVGT FPFNSFLSGF
     ISCVASFVLG VCLRLQVNPQ NSSNFCGIPP ERAFADFIFA HVVLHLVVMN FIG