ID DAD1_RAT Reviewed; 113 AA. AC P61805; O08552; O70364; P46966; P46968; Q96GB7; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 133. DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 {ECO:0000305}; DE Short=Oligosaccharyl transferase subunit DAD1; DE AltName: Full=Defender against cell death 1; DE Short=DAD-1; GN Name=Dad1 {ECO:0000312|RGD:621028}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Lewis; RA Giegerich G.; RT "Molecular cloning of the murine homologue of DAD-1, an ubiquitously RT expressed and highly conserved suppressor of apoptosis."; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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 (By similarity). N-glycosylation occurs CC cotranslationally and the complex associates with the Sec61 complex at CC the channel-forming translocon complex that mediates protein CC translocation across the endoplasmic reticulum (ER). All subunits are CC required for a maximal enzyme activity. {ECO:0000250|UniProtKB:E2R4X3, CC ECO:0000250|UniProtKB:P61803}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000250|UniProtKB:P61803}. CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex (By CC similarity). OST exists in two different complex forms which contain CC common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either CC STT3A or STT3B as catalytic subunits, and form-specific accessory CC subunits (By similarity). STT3A complex assembly occurs through the CC formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, CC subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and CC KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, CC DAD1, and OST48. The STT3A complex can form stable complexes with the CC Sec61 complex or with both the Sec61 and TRAP complexes. CC {ECO:0000250|UniProtKB:E2R4X3, ECO:0000250|UniProtKB:P61803}. 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; Y13336; CAA73780.1; -; Genomic_DNA. DR EMBL; BC061530; AAH61530.1; -; mRNA. DR RefSeq; NP_620265.1; NM_138910.4. DR AlphaFoldDB; P61805; -. DR SMR; P61805; -. DR FunCoup; P61805; 2453. DR IntAct; P61805; 2. DR MINT; P61805; -. DR STRING; 10116.ENSRNOP00000012233; -. DR PhosphoSitePlus; P61805; -. DR jPOST; P61805; -. DR PaxDb; 10116-ENSRNOP00000012233; -. DR Ensembl; ENSRNOT00000098684.2; ENSRNOP00000092852.1; ENSRNOG00000009090.7. DR Ensembl; ENSRNOT00055020459; ENSRNOP00055016463; ENSRNOG00055012038. DR Ensembl; ENSRNOT00060044393; ENSRNOP00060036789; ENSRNOG00060025638. DR Ensembl; ENSRNOT00065057504; ENSRNOP00065047345; ENSRNOG00065033446. DR GeneID; 192275; -. DR KEGG; rno:192275; -. DR UCSC; RGD:621028; rat. DR AGR; RGD:621028; -. DR CTD; 1603; -. DR RGD; 621028; Dad1. DR eggNOG; KOG1746; Eukaryota. DR GeneTree; ENSGT00390000003324; -. DR HOGENOM; CLU_111220_2_1_1; -. DR InParanoid; P61805; -. DR PhylomeDB; P61805; -. DR Reactome; R-RNO-9768727; Regulation of CDH1 posttranslational processing and trafficking to plasma membrane. DR Reactome; R-RNO-9931295; PD-L1(CD274) glycosylation and translocation to plasma membrane. DR UniPathway; UPA00378; -. DR PRO; PR:P61805; -. DR Proteomes; UP000002494; Chromosome 15. DR Bgee; ENSRNOG00000009090; Expressed in pancreas and 20 other cell types or tissues. DR ExpressionAtlas; P61805; baseline and differential. DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB. DR GO; GO:0160226; C:oligosaccharyltransferase complex A; ISO:RGD. DR GO; GO:0160227; C:oligosaccharyltransferase complex B; ISO:RGD. DR GO; GO:0008047; F:enzyme activator activity; ISO:RGD. DR GO; GO:0001824; P:blastocyst development; ISO:RGD. DR GO; GO:0009101; P:glycoprotein biosynthetic process; ISS:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD. DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:RGD. DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD. DR GO; GO:0007584; P:response to nutrient; IEP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR InterPro; IPR003038; DAD/Ost2. DR PANTHER; PTHR10705; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT DAD1; 1. DR PANTHER; PTHR10705:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT DAD1; 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_0000124014" 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" SQ SEQUENCE 113 AA; 12497 MW; 481983CADCEB2345 CRC64; MSASVVSVIS RFLEEYLSST PQRLKLLDAY LLYILLTGAL QFGYCLLVGT FPFNSFLSGF ISCVGSFILA VCLRIQINPQ NKADFQGISP ERAFADFLFA STILHLVVMN FVG //