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DAD1_CHICK
ID   DAD1_CHICK              Reviewed;         123 AA.
AC   O13113;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 119.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9271627; DOI=10.1007/s002510050291;
RA   Wang K., Gan L., Kuo C.L., Hood L.;
RT   "A highly conserved apoptotic suppressor gene is located near the chicken
RT   T-cell receptor alpha chain constant region.";
RL   Immunogenetics 46:376-382(1997).
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.
CC       {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; U83627; AAC60276.1; -; mRNA.
DR   RefSeq; NP_001007474.1; NM_001007473.1.
DR   AlphaFoldDB; O13113; -.
DR   SMR; O13113; -.
DR   STRING; 9031.ENSGALP00000000261; -.
DR   PaxDb; O13113; -.
DR   Ensembl; ENSGALT00000048785; ENSGALP00000052681; ENSGALG00000035626.
DR   GeneID; 395343; -.
DR   KEGG; gga:395343; -.
DR   CTD; 1603; -.
DR   VEuPathDB; HostDB:geneid_395343; -.
DR   eggNOG; KOG1746; Eukaryota.
DR   GeneTree; ENSGT00390000003324; -.
DR   HOGENOM; CLU_111220_2_1_1; -.
DR   InParanoid; O13113; -.
DR   OMA; FIFAHII; -.
DR   OrthoDB; 1586516at2759; -.
DR   PhylomeDB; O13113; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:O13113; -.
DR   Proteomes; UP000000539; Chromosome 27.
DR   Bgee; ENSGALG00000035626; Expressed in granulocyte and 14 other tissues.
DR   ExpressionAtlas; O13113; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
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; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..123
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit DAD1"
FT                   /id="PRO_0000124015"
FT   TOPO_DOM        1..40
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   123 AA;  12926 MW;  D468651E6A5D01C5 CRC64;
     MSGTAGSGVG AAGSVGSVVR RFLAEYGSGT SSRLKVLDAY LLYVMLTGAL QFGYCLGVGT
     FPFNSFLSGF ISAVGSFILG VCLRIQINPQ NKGEFQGISP ERAFADFLFA NTILHLVVIN
     FVG
 
 
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