ID   OST48_CAEEL             Reviewed;         445 AA.
AC   P45971;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2026, entry version 152.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit;
DE            Short=Oligosaccharyl transferase 48 kDa subunit;
DE   AltName: Full=Oligosaccharyl transferase beta subunit 1 {ECO:0000312|WormBase:T09A5.11};
DE   Flags: Precursor;
GN   Name=ostb-1 {ECO:0000312|WormBase:T09A5.11};
GN   ORFNames=T09A5.11 {ECO:0000312|WormBase:T09A5.11};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23691084; DOI=10.1371/journal.pone.0063687;
RA   Stevens J., Spang A.;
RT   "N-glycosylation is required for secretion and mitosis in C. elegans.";
RL   PLoS ONE 8:E63687-E63687(2013).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=36173858; DOI=10.1126/science.abo3191;
RA   Bou Sleiman M., Roy S., Gao A.W., Sadler M.C., von Alvensleben G.V.G.,
RA   Li H., Sen S., Harrison D.E., Nelson J.F., Strong R., Miller R.A.,
RA   Kutalik Z., Williams R.W., Auwerx J.;
RT   "Sex- and age-dependent genetics of longevity in a heterogeneous mouse
RT   population.";
RL   Science 377:eabo3191-eabo3191(2022).
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-Xaa-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 (By similarity). Required for the assembly of both
CC       SST3A- and SS3B-containing OST complexes (By similarity). Required for
CC       normal lifespan (PubMed:36173858). {ECO:0000250|UniProtKB:P39656,
CC       ECO:0000250|UniProtKB:Q05052, ECO:0000269|PubMed:36173858}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
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   -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down is mostly embryonic
CC       lethal (PubMed:23691084). Embryogenesis proceeds more slowly and
CC       embryos are osmo-sensitive (PubMed:23691084). RNAi-mediated knockdown
CC       reduces lifespan (PubMed:36173858). {ECO:0000269|PubMed:23691084,
CC       ECO:0000269|PubMed:36173858}.
CC   -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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DR   EMBL; Z36753; CAA85337.1; -; Genomic_DNA.
DR   PIR; T24723; T24723.
DR   RefSeq; NP_495655.1; NM_063254.9.
DR   AlphaFoldDB; P45971; -.
DR   SMR; P45971; -.
DR   BioGRID; 39601; 26.
DR   ComplexPortal; CPX-968; Oligosaccharyltransferase complex.
DR   FunCoup; P45971; 2620.
DR   STRING; 6239.T09A5.11.2; -.
DR   PaxDb; 6239-T09A5.11.2; -.
DR   PeptideAtlas; P45971; -.
DR   EnsemblMetazoa; T09A5.11.1; T09A5.11.1; WBGene00011638.
DR   GeneID; 174268; -.
DR   KEGG; cel:CELE_T09A5.11; -.
DR   UCSC; T09A5.11.2; c. elegans.
DR   AGR; WB:WBGene00011638; -.
DR   CTD; 174268; -.
DR   WormBase; T09A5.11; CE01081; WBGene00011638; ostb-1.
DR   eggNOG; KOG2754; Eukaryota.
DR   HOGENOM; CLU_031804_0_0_1; -.
DR   InParanoid; P45971; -.
DR   OMA; AADNHDV; -.
DR   OrthoDB; 29105at2759; -.
DR   PhylomeDB; P45971; -.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:P45971; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00011638; Expressed in embryo and 4 other cell types or tissues.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   InterPro; IPR005013; DDOST_48_kDa_subunit.
DR   InterPro; IPR055459; OST48_MD.
DR   InterPro; IPR055457; OST48_N.
DR   PANTHER; PTHR10830; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE 48 KDA SUBUNIT; 1.
DR   PANTHER; PTHR10830:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE 48 KDA SUBUNIT; 1.
DR   Pfam; PF23358; OST48_MD; 1.
DR   Pfam; PF03345; OST48_N; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..445
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase 48 kDa subunit"
FT                   /id="PRO_0000021954"
FT   TOPO_DOM        21..405
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        427..445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   445 AA;  48760 MW;  59A14E6ECF43F0F9 CRC64;
     MRWLPGLLLI ASIGFHQSLA DRVLVLGETA AVKDTHSVFL NSVKERGHEL TVRAADDSQL
     ALFKHGQLIF DHLFILAPGV QVFGGSLSPS EISKFVDAGG NVLVAAGSNI GDALREIAAE
     HGFEFEEAGT SVIDHHNYDQ TLDSGDHTTL VVGKDQLISA ELIVGNSAKL HPVLFKGIGL
     VAGKTNNLAL SIVRASGTAY SYDPKAVRAT NPSIAGSRTL LVGGLQSRNN ARIVFTGSSE
     LFSNTFFSAK TNSVNPSVQG AQSGNADFAT AITRWVMKES GVLRVKTVNH HKKGETVPPV
     EGYFITEDVV YTIEIEELKN GKWVPFQGKD VQLEFVRIDP FVRATLKNSN GRLSVAFKLP
     DVLGVFKFLV DYRRVGYTHL YDVQQVSVRP LWHTQYERFI RSAYPYYASS FSMMAGLVLF
     SIVYLYHKDT PVKGAKVLDS EKKKN
//