DAD1_RAT
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 03-AUG-2022, entry version 116.
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}.
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DR EMBL; Y13336; CAA73780.1; -; Genomic_DNA.
DR EMBL; BC061530; AAH61530.1; -; mRNA.
DR RefSeq; NP_620265.1; NM_138910.3.
DR AlphaFoldDB; P61805; -.
DR SMR; P61805; -.
DR IntAct; P61805; 2.
DR MINT; P61805; -.
DR STRING; 10116.ENSRNOP00000012233; -.
DR jPOST; P61805; -.
DR PaxDb; P61805; -.
DR PRIDE; P61805; -.
DR Ensembl; ENSRNOT00000098684; ENSRNOP00000092852; ENSRNOG00000009090.
DR GeneID; 192275; -.
DR KEGG; rno:192275; -.
DR UCSC; RGD:621028; rat.
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 OMA; FIFAHII; -.
DR OrthoDB; 1586516at2759; -.
DR PhylomeDB; P61805; -.
DR TreeFam; TF312846; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P61805; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000009090; Expressed in pancreas and 20 other tissues.
DR Genevisible; P61805; RN.
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; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0001824; P:blastocyst development; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
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; 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_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
