ID A0A2Y9MPE1_DELLE Unreviewed; 149 AA.
AC A0A2Y9MPE1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Oligosaccharyltransferase complex subunit {ECO:0000256|RuleBase:RU366060};
GN Name=OSTC {ECO:0000313|RefSeq:XP_022422816.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022422816.1};
RN [1] {ECO:0000313|RefSeq:XP_022422816.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022422816.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Specific component of the STT3A-containing form of the
CC oligosaccharyl transferase (OST) complex that catalyzes the initial
CC transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from
CC the lipid carrier dolichol-pyrophosphate to an asparagine residue
CC within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains,
CC the first step in protein N-glycosylation. 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. May be involved in N-
CC glycosylation of APP (amyloid-beta precursor protein). Can modulate
CC gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1.
CC {ECO:0000256|RuleBase:RU366060}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000256|RuleBase:RU366060}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU366060}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU366060}.
CC -!- SIMILARITY: Belongs to the OSTC family. {ECO:0000256|ARBA:ARBA00009376,
CC ECO:0000256|RuleBase:RU366060}.
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DR RefSeq; XP_022422816.1; XM_022567108.1.
DR AlphaFoldDB; A0A2Y9MPE1; -.
DR STRING; 9749.A0A2Y9MPE1; -.
DR KEGG; dle:111171493; -.
DR InParanoid; A0A2Y9MPE1; -.
DR OrthoDB; 5388489at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR InterPro; IPR042416; OSTC.
DR PANTHER; PTHR13160; OLIGOSACCHARYLTRANSFERASE COMPLEX SUBUNIT OSTC; 1.
DR PANTHER; PTHR13160:SF9; OLIGOSACCHARYLTRANSFERASE COMPLEX SUBUNIT OSTC; 1.
DR Pfam; PF04756; OST3_OST6; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU366060};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU366060};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU366060}.
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366060"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366060"
FT TRANSMEM 118..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366060"
SQ SEQUENCE 149 AA; 16801 MW; E2E2E92BBF9408B4 CRC64;
MESLYRVPFL VLECPNLKLK KPPWVHMPSA MTVYALVVVS YFLITGGIIY DVIVEPPSVG
SMTDEHGHQR PVAFLAYRVN GQYIMEGLAS SFLFTMGGLG FIILDRSNAP NIPKLNRFLL
LFIGFVCVLL SFFMARVFMR MKLPGYLMG
//
