DAD1_ARATH
ID DAD1_ARATH Reviewed; 115 AA.
AC Q39080; Q53WQ9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 149.
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=AtDAD1;
DE Short=DAD-1;
GN Name=DAD1; OrderedLocusNames=At1g32210; ORFNames=F3C3.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9225471; DOI=10.1046/j.1365-313x.1997.11061325.x;
RA Gallois P., Makishima T., Hecht V., Depres B., Laudii M., Nishimoto T.,
RA Cooke R.;
RT "An Arabidopsis thaliana cDNA complementing a hamster apoptosis suppressor
RT mutant.";
RL Plant J. 11:1325-1331(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Sugiura T., Naito K., Asahi T., Suzuki H.;
RT "Differential regulation of two types of the defender against apoptotic
RT cell death 1 (dad1) genes in senescing cotyledons and petals of Arabidopsis
RT thaliana.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:P46964}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:P46964}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the DAD/OST2 family. {ECO:0000305}.
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DR EMBL; X95585; CAA64837.1; -; mRNA.
DR EMBL; Y17608; CAC80054.1; -; Genomic_DNA.
DR EMBL; AC084165; AAG23438.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31449.1; -; Genomic_DNA.
DR EMBL; BT024553; ABD38892.1; -; mRNA.
DR PIR; F86446; F86446.
DR PIR; S71269; S71269.
DR RefSeq; NP_174500.1; NM_102954.4.
DR AlphaFoldDB; Q39080; -.
DR SMR; Q39080; -.
DR BioGRID; 25347; 18.
DR IntAct; Q39080; 17.
DR STRING; 3702.AT1G32210.1; -.
DR PaxDb; Q39080; -.
DR PRIDE; Q39080; -.
DR EnsemblPlants; AT1G32210.1; AT1G32210.1; AT1G32210.
DR GeneID; 840113; -.
DR Gramene; AT1G32210.1; AT1G32210.1; AT1G32210.
DR KEGG; ath:AT1G32210; -.
DR Araport; AT1G32210; -.
DR TAIR; locus:2031765; AT1G32210.
DR eggNOG; KOG1746; Eukaryota.
DR HOGENOM; CLU_111220_2_1_1; -.
DR OMA; FIFAHII; -.
DR OrthoDB; 1586516at2759; -.
DR PhylomeDB; Q39080; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q39080; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39080; baseline and differential.
DR Genevisible; Q39080; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Apoptosis; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..115
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit DAD1"
FT /id="PRO_0000124019"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..55
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 102
FT /note="C -> Y (in Ref. 1; CAA64837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 115 AA; 12695 MW; B944C9EA03AF0705 CRC64;
MVKSTSKDAQ DLFRSLRSAY SATPTNLKII DLYVVFAVFT ALIQVVYMAL VGSFPFNSFL
SGVLSCIGTA VLAVCLRIQV NKENKEFKDL APERAFADFV LCNLVLHLVI INFLG
