ID   OST48_DANRE             Reviewed;         441 AA.
AC   Q6NYS8; Q6PHG6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 97.
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}; ORFNames=zgc:66068;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-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.
CC       {ECO:0000250|UniProtKB:Q05052}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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DR   EMBL; BC056559; AAH56559.1; -; mRNA.
DR   EMBL; BC066475; AAH66475.1; -; mRNA.
DR   RefSeq; NP_998258.1; NM_213093.1.
DR   AlphaFoldDB; Q6NYS8; -.
DR   SMR; Q6NYS8; -.
DR   STRING; 7955.ENSDARP00000105892; -.
DR   PaxDb; Q6NYS8; -.
DR   GeneID; 406408; -.
DR   KEGG; dre:406408; -.
DR   CTD; 1650; -.
DR   ZFIN; ZDB-GENE-040426-2147; ddost.
DR   eggNOG; KOG2754; Eukaryota.
DR   InParanoid; Q6NYS8; -.
DR   OrthoDB; 975158at2759; -.
DR   PhylomeDB; Q6NYS8; -.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q6NYS8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..441
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase 48 kDa subunit"
FT                   /id="PRO_0000357448"
FT   TOPO_DOM        29..410
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        432..441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        2
FT                   /note="A -> T (in Ref. 1; AAH56559)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        13
FT                   /note="A -> P (in Ref. 1; AAH56559)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="I -> V (in Ref. 1; AAH56559)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="I -> L (in Ref. 1; AAH66475)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   441 AA;  48534 MW;  1D4E5C248F6948EE CRC64;
     MATALSGGFS KNALFILSAA LMLQAVLGDG KTLVLLDNPN IRDTHSIFFR SLADRGFDLT
     FKTADDPGLS LIKYGQFLYD HLILFSPSVE DFGGNINVET ITAFIDGGGN VLVAASSDIG
     DPLRELGSEC GIEFDEEKTA VIDHHNYDIS DPGEHTLIVA DPENLLKAPT IVGKPTDKPV
     LFKGVGMVAD PDNPLVLDIL TGSSTSYSYF PDRPITQYPH AVGKNTLLIA GLQARNNARV
     VFSGSLHFFS DAFFNSAVQK AATGSKRYEQ TGNQDLAEAL SRWVFKEAGV LRVGDVTHHP
     VGESTPPAAY TVTDLVEYGI VIEMLSGGKW VPFDGDDIQL EFVRIDPFVR TYLKKNGGKY
     SVQFKLPDVY GVFQFKVDYN RLGYTHLYSS TQVSVRPLQH TQYERFIPSA FPYYASAFSM
     MAGLFVFSVV FLHMREKEKS D