DAD1_DROME
ID DAD1_DROME Reviewed; 112 AA.
AC Q9VLM5; A0A1B2AKP8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1;
DE Short=DAD-1;
DE Short=Oligosaccharyl transferase subunit DAD1;
DE AltName: Full=Defender against apoptotic cell death 1 {ECO:0000303|PubMed:27693235, ECO:0000312|FlyBase:FBgn0263852};
DE AltName: Full=Defender against cell death 1 {ECO:0000250|UniProtKB:P61803};
GN Name=Dad1 {ECO:0000303|PubMed:27693235, ECO:0000312|FlyBase:FBgn0263852};
GN Synonyms=l(2)k12914 {ECO:0000312|FlyBase:FBgn0263852};
GN ORFNames=CG13393 {ECO:0000312|FlyBase:FBgn0263852};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, PATHWAY, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27693235; DOI=10.1016/j.ydbio.2016.09.021;
RA Zhang Y., Cui C., Lai Z.C.;
RT "The defender against apoptotic cell death 1 gene is required for tissue
RT growth and efficient N-glycosylation in Drosophila melanogaster.";
RL Dev. Biol. 420:186-195(2016).
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). Probably as part of the N-
CC glycosylation pathway, plays a role in the regulation of tissue growth
CC and apoptosis (PubMed:27693235). {ECO:0000250|UniProtKB:E2R4X3,
CC ECO:0000269|PubMed:27693235}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:27693235}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:E2R4X3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27693235}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Lethal (PubMed:27693235). RNAi-mediated knockdown
CC in the wing results in a moderate decrease in wing size, decreased N-
CC glycosylation, increased cell-death mediated by the JNK pathway and
CC increased ER stress mediated by the unfolded protein response pathway
CC (PubMed:27693235). {ECO:0000269|PubMed:27693235}.
CC -!- SIMILARITY: Belongs to the DAD/OST2 family. {ECO:0000305}.
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DR EMBL; AE014134; AAF52660.1; -; Genomic_DNA.
DR EMBL; AY113429; AAM29434.1; -; mRNA.
DR EMBL; KX531951; ANY27761.1; -; mRNA.
DR RefSeq; NP_609222.1; NM_135378.4.
DR AlphaFoldDB; Q9VLM5; -.
DR SMR; Q9VLM5; -.
DR BioGRID; 60283; 8.
DR IntAct; Q9VLM5; 8.
DR STRING; 7227.FBpp0079324; -.
DR PaxDb; Q9VLM5; -.
DR PRIDE; Q9VLM5; -.
DR DNASU; 34159; -.
DR EnsemblMetazoa; FBtr0079719; FBpp0079324; FBgn0263852.
DR GeneID; 34159; -.
DR KEGG; dme:Dmel_CG13393; -.
DR UCSC; CG13393-RA; d. melanogaster.
DR CTD; 1603; -.
DR FlyBase; FBgn0263852; Dad1.
DR VEuPathDB; VectorBase:FBgn0263852; -.
DR eggNOG; KOG1746; Eukaryota.
DR GeneTree; ENSGT00390000003324; -.
DR HOGENOM; CLU_111220_2_1_1; -.
DR InParanoid; Q9VLM5; -.
DR OMA; FIFAHII; -.
DR OrthoDB; 1586516at2759; -.
DR PhylomeDB; Q9VLM5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 34159; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Dad; fly.
DR GenomeRNAi; 34159; -.
DR PRO; PR:Q9VLM5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0263852; Expressed in eye disc (Drosophila) and 26 other tissues.
DR Genevisible; Q9VLM5; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
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; IMP:UniProtKB.
DR InterPro; IPR003038; DAD/Ost2.
DR PANTHER; PTHR10705; PTHR10705; 1.
DR Pfam; PF02109; DAD; 1.
DR PIRSF; PIRSF005588; DAD; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..112
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit DAD1"
FT /id="PRO_0000124018"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..51
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 112 AA; 12526 MW; 5070629471AA2DC3 CRC64;
MVELSSVISK FYNDYVQNTP KKLKLVDIYL GYILLTGIIQ FVYCCLVGTF PFNSFLSGFI
STVSCFVLAV CLRLQANPQN KSVFAGISPE RGFADFIFAH VILHLVVMNF IG
