DAD1_CAEEL
ID DAD1_CAEEL Reviewed; 113 AA.
AC P52872;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit dad-1;
DE Short=Oligosaccharyl transferase subunit dad-1;
DE AltName: Full=Defender against cell death 1;
DE Short=Protein dad-1;
GN Name=dad-1 {ECO:0000312|WormBase:F57B10.10};
GN ORFNames=F57B10.10 {ECO:0000312|WormBase:F57B10.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=7556086; DOI=10.1002/j.1460-2075.1995.tb00122.x;
RA Sugimoto A., Hozak R.R., Nakashima T., Nishimoto T., Rothman J.H.;
RT "dad-1, an endogenous programmed cell death suppressor in Caenorhabditis
RT elegans and vertebrates.";
RL EMBO J. 14:4434-4441(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23691084; DOI=10.1371/journal.pone.0063687;
RA Stevens J., Spang A.;
RT "N-glycosylation is required for secretion and mitosis in C. elegans.";
RL PLoS ONE 8:E63687-E63687(2013).
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 (By similarity). Possesses cell death-inhibiting
CC activity. Suppresses some programmed cell death in C.elegans
CC (PubMed:7556086). {ECO:0000250|UniProtKB:E2R4X3,
CC ECO:0000269|PubMed:7556086}.
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 {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down is mostly embryonic
CC lethal. Embryogenesis proceeds more slowly and embryos are osmo-
CC sensitive. {ECO:0000269|PubMed:23691084}.
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; X89080; CAA61451.1; -; mRNA.
DR EMBL; FO081416; CCD71478.1; -; Genomic_DNA.
DR PIR; S59116; S59116.
DR RefSeq; NP_491889.1; NM_059488.6.
DR AlphaFoldDB; P52872; -.
DR SMR; P52872; -.
DR BioGRID; 37821; 2.
DR ComplexPortal; CPX-968; Oligosaccharyl transferase complex.
DR DIP; DIP-24414N; -.
DR IntAct; P52872; 1.
DR STRING; 6239.F57B10.10; -.
DR EPD; P52872; -.
DR PaxDb; P52872; -.
DR PeptideAtlas; P52872; -.
DR EnsemblMetazoa; F57B10.10.1; F57B10.10.1; WBGene00000896.
DR GeneID; 172370; -.
DR KEGG; cel:CELE_F57B10.10; -.
DR UCSC; F57B10.10.2; c. elegans.
DR CTD; 172370; -.
DR WormBase; F57B10.10; CE11316; WBGene00000896; dad-1.
DR eggNOG; KOG1746; Eukaryota.
DR GeneTree; ENSGT00390000003324; -.
DR HOGENOM; CLU_111220_2_1_1; -.
DR InParanoid; P52872; -.
DR OMA; FIFAHII; -.
DR OrthoDB; 1586516at2759; -.
DR PhylomeDB; P52872; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P52872; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000896; Expressed in embryo and 4 other tissues.
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:0043066; P:negative regulation of apoptotic process; IDA:WormBase.
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 3: Inferred from homology;
KW Apoptosis; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..113
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit dad-1"
FT /id="PRO_0000124017"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..55
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 113 AA; 12747 MW; 933057F18CBB6DE6 CRC64;
MAAQVVPVLS KLFDDYQKTT SSKLKIIDAY MTYILFTGIF QFIYCLLVGT FPFNSFLSGF
ISTVTSFVLA SCLRMQVNQE NRSEFTAVST ERAFADFIFA NLILHLVVVN FLG
