TM258_DANRE
ID TM258_DANRE Reviewed; 79 AA.
AC Q6PBS6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Transmembrane protein 258 {ECO:0000250|UniProtKB:P61165};
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258;
DE Short=Oligosaccharyl transferase subunit TMEM258;
GN Name=tmem258 {ECO:0000250|UniProtKB:P61165}; ORFNames=zgc:73269;
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=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) 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. 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:0000250|UniProtKB:P61165}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P61165}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:P61165}. Cytoplasm
CC {ECO:0000250|UniProtKB:P61165}.
CC -!- SIMILARITY: Belongs to the OST5 family. {ECO:0000305}.
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DR EMBL; BC059600; AAH59600.1; -; mRNA.
DR RefSeq; NP_957063.1; NM_200769.3.
DR AlphaFoldDB; Q6PBS6; -.
DR SMR; Q6PBS6; -.
DR STRING; 7955.ENSDARP00000043171; -.
DR PaxDb; Q6PBS6; -.
DR Ensembl; ENSDART00000043172; ENSDARP00000043171; ENSDARG00000078785.
DR GeneID; 393742; -.
DR KEGG; dre:393742; -.
DR CTD; 746; -.
DR ZFIN; ZDB-GENE-040426-1739; tmem258.
DR eggNOG; KOG4452; Eukaryota.
DR GeneTree; ENSGT00390000010089; -.
DR HOGENOM; CLU_180449_0_0_1; -.
DR InParanoid; Q6PBS6; -.
DR OMA; MERYVGP; -.
DR OrthoDB; 1627291at2759; -.
DR PhylomeDB; Q6PBS6; -.
DR TreeFam; TF300295; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q6PBS6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000078785; Expressed in intestine and 27 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 Cytoplasm; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..79
FT /note="Transmembrane protein 258"
FT /id="PRO_0000235833"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 79 AA; 9098 MW; E86B7A13EF5CB080 CRC64;
MELEAMTRYT SPVNPAVFPH LTVVLLAIGM FFKAWFFVYE VTSTKYTRDV YKELLIALVA
SLFMGFGVHF LLLWVGIFV