ID   TM258_CAEEL             Reviewed;          79 AA.
AC   Q965T1;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Transmembrane protein 258 {ECO:0000305};
DE   AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258;
DE            Short=Oligosaccharyl transferase subunit TMEM258;
GN   Name=tmem-258 {ECO:0000312|WormBase:Y57E12AM.1};
GN   ORFNames=Y57E12AM.1 {ECO:0000312|WormBase:Y57E12AM.1};
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).
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:P61165}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P61165}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:P61165}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the OST5 family. {ECO:0000305}.
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DR   EMBL; BX284605; CCD74331.1; -; Genomic_DNA.
DR   RefSeq; NP_504794.1; NM_072393.3.
DR   AlphaFoldDB; Q965T1; -.
DR   SMR; Q965T1; -.
DR   STRING; 6239.Y57E12AM.1; -.
DR   PaxDb; Q965T1; -.
DR   EnsemblMetazoa; Y57E12AM.1.1; Y57E12AM.1.1; WBGene00021960.
DR   GeneID; 179094; -.
DR   KEGG; cel:CELE_Y57E12AM.1; -.
DR   UCSC; Y57E12AM.1.1; c. elegans.
DR   CTD; 179094; -.
DR   WormBase; Y57E12AM.1; CE26193; WBGene00021960; tmem-258.
DR   eggNOG; KOG4452; Eukaryota.
DR   GeneTree; ENSGT00390000010089; -.
DR   HOGENOM; CLU_180449_0_0_1; -.
DR   InParanoid; Q965T1; -.
DR   OMA; MERYVGP; -.
DR   OrthoDB; 1627291at2759; -.
DR   PhylomeDB; Q965T1; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q965T1; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00021960; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0034998; C:oligosaccharyltransferase I complex; IEA:InterPro.
DR   GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
DR   InterPro; IPR007915; TMEM258/Ost5.
DR   PANTHER; PTHR13636; PTHR13636; 1.
DR   Pfam; PF05251; Ost5; 1.
PE   3: Inferred from homology;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..79
FT                   /note="Transmembrane protein 258"
FT                   /id="PRO_0000221144"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   79 AA;  8757 MW;  59EB618581F3C16F CRC64;
     MDISKMNRYT APVNFASLPL LTTFLCGVGL LLLATFTMIQ VTSTKYNRNL LKELFIAATS
     SVFLGFGSVF LLLWVGIYV