DAD1_MESAU
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 25-MAY-2022, entry version 82.
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}.
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DR EMBL; D15058; BAA03651.1; -; mRNA.
DR PIR; C54437; C54437.
DR RefSeq; NP_001268553.1; NM_001281624.1.
DR RefSeq; XP_012980316.1; XM_013124862.1.
DR AlphaFoldDB; P61806; -.
DR SMR; P61806; -.
DR STRING; 10036.XP_005085621.1; -.
DR GeneID; 101827723; -.
DR CTD; 1603; -.
DR eggNOG; KOG1746; Eukaryota.
DR OrthoDB; 1586516at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; 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; PTHR10705; 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
