ID   OST48_PONAB             Reviewed;         439 AA.
AC   Q5R501;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 56.
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   Flags: Precursor;
GN   Name=DDOST {ECO:0000250|UniProtKB:P39656};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 (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 (By
CC       similarity). OST exists in two different complex forms which contain
CC       common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either
CC       STT3A or STT3B as catalytic subunits, and form-specific accessory
CC       subunits (By similarity). STT3A complex assembly occurs through the
CC       formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258,
CC       subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and
CC       KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2,
CC       DAD1, and OST48. The STT3A complex can form stable complexes with the
CC       Sec61 complex or with both the Sec61 and TRAP complexes. Interacts with
CC       SMIM22 (By similarity). {ECO:0000250|UniProtKB:P39656,
CC       ECO:0000250|UniProtKB:Q05052}.
CC   -!- SUBCELLULAR LOCATION: 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH93165.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR861085; CAH93165.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q5R501; -.
DR   SMR; Q5R501; -.
DR   STRING; 9601.ENSPPYP00000002050; -.
DR   eggNOG; KOG2754; Eukaryota.
DR   InParanoid; Q5R501; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..439
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase 48 kDa subunit"
FT                   /id="PRO_0000357446"
FT   TOPO_DOM        27..410
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        431..439
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   439 AA;  48783 MW;  CF850058921A466B CRC64;
     MEPSTAARAW ALFWLLPPLL GAVCASGPRT LVLLDNLNVR ETHSLFFRSL KDRGFELTFK
     TADDPSLSLI KYGEFLYDNL IIFSPSVEDF GGNINVETIS AFIDGGGSVL VAASSDIGDP
     LRELGSECGI EFDEEKTAVI DHHNYDISDL GQHTLIVADT ENLLKAPTIV GKSSLNPILF
     RGVGMVADPD NPLVLDILTG SSTSYSFFPD KPITQYPHAV GKNTLLIAGL QARNNARVIF
     SGSLDFFSDS FFNSAVQKAA PGSQRYSQTG NYELAVALSR WVFKEEGVLR VGPVSHHRVG
     ETAPPNAYTV TDLVEYSIVI QQLSNGKWVP FDGDDIQLEF VRIDPFVRTF LKKKGGKYSV
     QFKLPDVYGV FQFKVDYNRL GYTHLYSSTQ VSVRPLQHTQ YERFIPSAYP YYASAFSMML
     GLFIFSIVFL HMKEKEKSD