ID   OST48_CHICK             Reviewed;         413 AA.
AC   P48440;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit {ECO:0000250|UniProtKB:P39656};
DE            Short=DDOST 48 kDa subunit;
DE            Short=Oligosaccharyl transferase 48 kDa subunit;
DE   AltName: Full=OST 50 kDa subunit;
GN   Name=DDOST {ECO:0000250|UniProtKB:P39656}; Synonyms=OST48;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Oviduct;
RX   PubMed=8175777; DOI=10.1016/s0021-9258(17)36853-9;
RA   Kumar V., Heinemann F.S., Ozols J.;
RT   "Purification and characterization of avian oligosaccharyltransferase.
RT   Complete amino acid sequence of the 50-kDa subunit.";
RL   J. Biol. Chem. 269:13451-13457(1994).
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 (By similarity). 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 (By similarity). Required for
CC       the assembly of both SST3A- and SS3B-containing OST complexes (By
CC       similarity). {ECO:0000250|UniProtKB:P39656,
CC       ECO:0000250|UniProtKB:Q05052}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P39656}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:Q05052}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:8175777}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q29381}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q29381}.
CC   -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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DR   PIR; A54127; A54127.
DR   AlphaFoldDB; P48440; -.
DR   SMR; P48440; -.
DR   STRING; 9031.ENSGALP00000038313; -.
DR   PaxDb; P48440; -.
DR   VEuPathDB; HostDB:geneid_425542; -.
DR   eggNOG; KOG2754; Eukaryota.
DR   InParanoid; P48440; -.
DR   PhylomeDB; P48440; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IEA:InterPro.
DR   InterPro; IPR005013; DDOST_48_kDa_subunit.
DR   PANTHER; PTHR10830; PTHR10830; 1.
DR   Pfam; PF03345; DDOST_48kD; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..413
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase 48 kDa subunit"
FT                   /id="PRO_0000058094"
FT   TOPO_DOM        1..383
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..413
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   413 AA;  45912 MW;  5CDC51930F5D4BF1 CRC64;
     GPRSLVLLEN LNLRDTHSLF FRSLADRGFE LTFRTADDAG LSLIKYGEFL YDNLIIFSPS
     IEDFGGNINV ETITAFIDGG GSVLVAASSD IGDPLRELGS ECGIEFDEER TAVIDHHNYD
     ISDPGQHTLI VADAENLLKA PTIVGKKALN PILFRGVGMV ADPDNPLVLD ILTGSSTSYS
     FFPDKPITQY PHAVGKNTLL IAGLQARNNA RVVFSGSLDF FSDAFFSSAV QKAAPGSKRY
     SQTGNYELAV ALSRWVFKEE GVLRVGAVSH HRVGELAPPN AYTVTDLVEY SIVIEKLSDG
     KWIPFDGDDI QLEFVRIDPF VRTFLKRNGG KYSVQFKLPD VYGVFQFKVD YNRLGYTHLY
     SSTQVSVRPL QHTQYERFIP SAYPYYAGAF SMMVGLFMFS IVFLHMKEKE KSD