ID   Q53G02_HUMAN            Unreviewed;       113 AA.
AC   Q53G02;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 {ECO:0000256|ARBA:ARBA00018947, ECO:0000256|RuleBase:RU361136};
DE            Short=Oligosaccharyl transferase subunit DAD1 {ECO:0000256|RuleBase:RU361136};
DE   Flags: Fragment;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD96849.1};
RN   [1] {ECO:0000313|EMBL:BAD96849.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8125298; DOI=10.1016/0378-1119(94)90802-8;
RA   Maruyama K., Sugano S.;
RT   "Oligo-capping: a simple method to replace the cap structure of eukaryotic
RT   mRNAs with oligoribonucleotides.";
RL   Gene 138:171-174(1994).
RN   [2] {ECO:0000313|EMBL:BAD96849.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9373149; DOI=10.1016/S0378-1119(97)00411-3;
RA   Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.;
RT   "Construction and characterization of a full length-enriched and a 5'-end-
RT   enriched cDNA library.";
RL   Gene 200:149-156(1997).
RN   [3] {ECO:0000313|EMBL:BAD96849.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) 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:0000256|RuleBase:RU361136}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU361136}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000256|RuleBase:RU361136}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU361136}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU361136}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the DAD/OST2 family.
CC       {ECO:0000256|ARBA:ARBA00009386, ECO:0000256|RuleBase:RU361136}.
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DR   EMBL; AK223129; BAD96849.1; -; mRNA.
DR   RefSeq; NP_001335.1; NM_001344.3.
DR   AlphaFoldDB; Q53G02; -.
DR   PeptideAtlas; Q53G02; -.
DR   DNASU; 1603; -.
DR   GeneID; 1603; -.
DR   KEGG; hsa:1603; -.
DR   CTD; 1603; -.
DR   PharmGKB; PA27136; -.
DR   OrthoDB; 206600at2759; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 1603; 815 hits in 1121 CRISPR screens.
DR   GenomeRNAi; 1603; -.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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.
DR   Genevisible; Q53G02; HS.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU361136};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361136};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361136}.
FT   TRANSMEM        30..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361136"
FT   TRANSMEM        55..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361136"
FT   TRANSMEM        93..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361136"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD96849.1"
SQ   SEQUENCE   113 AA;  12425 MW;  CA1983CADCEB20F3 CRC64;
     MSASVVSVIS RFLEEYLSST PQRLKLLDAY LLYILLTGAL QFGYCLLVGT FPFNSFLSGF
     ISCVGSFILA VCLRIQINPQ NKADFQGISP GRAFADFLFA STILHLVVMN FVG
//