ID   OST4_DROPS              Reviewed;          40 AA.
AC   B5E1E8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4 {ECO:0000250|UniProtKB:Q99380};
GN   ORFNames=GA24324;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1] {ECO:0000312|EMBL:EDY69109.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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:P0C6T2}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:P0C6T2}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type III membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the OST4 family. {ECO:0000255}.
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DR   EMBL; CM000071; EDY69109.1; -; Genomic_DNA.
DR   RefSeq; XP_002138551.1; XM_002138515.2.
DR   AlphaFoldDB; B5E1E8; -.
DR   SMR; B5E1E8; -.
DR   STRING; 7237.FBpp0276459; -.
DR   EnsemblMetazoa; FBtr0278021; FBpp0276459; FBgn0245721.
DR   GeneID; 6898510; -.
DR   KEGG; dpo:Dpse_GA24324; -.
DR   eggNOG; ENOG502TACJ; Eukaryota.
DR   HOGENOM; CLU_186352_2_0_1; -.
DR   InParanoid; B5E1E8; -.
DR   Proteomes; UP000001819; Chromosome 3.
DR   Bgee; FBgn0245721; Expressed in male reproductive system and 2 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR   InterPro; IPR018943; Oligosaccaryltransferase.
DR   InterPro; IPR036330; Ost4p_sf.
DR   Pfam; PF10215; Ost4; 1.
DR   SUPFAM; SSF103464; SSF103464; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..40
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit 4"
FT                   /id="PRO_0000386613"
FT   TOPO_DOM        1..4
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..40
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   40 AA;  4384 MW;  81F3BC3BF3EEAF94 CRC64;
     MITDVQLAIF SNVLGVFLFL LVVAYHYINA NTGKSSPKAK