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 12-AUG-2020, entry version 112. 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; 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 -!- 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}. 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; U83627; AAC60276.1; -; mRNA. DR RefSeq; NP_001007474.1; NM_001007473.1. DR SMR; O13113; -. DR STRING; 9031.ENSGALP00000000261; -. DR PaxDb; O13113; -. DR PRIDE; O13113; -. DR Ensembl; ENSGALT00000048785; ENSGALP00000052681; ENSGALG00000035626. DR GeneID; 395343; -. DR KEGG; gga:395343; -. DR CTD; 1603; -. DR eggNOG; KOG1746; Eukaryota. DR GeneTree; ENSGT00390000003324; -. DR HOGENOM; CLU_111220_2_1_1; -. DR InParanoid; O13113; -. DR KO; K12668; -. DR OMA; GVCLRLQ; -. DR OrthoDB; 1586516at2759; -. DR PhylomeDB; O13113; -. DR UniPathway; UPA00378; -. DR PRO; PR:O13113; -. DR Proteomes; UP000000539; Chromosome 27. DR Bgee; ENSGALG00000000196; 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:0008047; F:enzyme activator activity; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. 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 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 //