OST3_CAEEL
ID OST3_CAEEL Reviewed; 340 AA.
AC P34669;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3;
DE Flags: Precursor;
GN ORFNames=ZK686.3;
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
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:P48439}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:P48439}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCD63648.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FO080431; CCD63648.1; ALT_INIT; Genomic_DNA.
DR PIR; S44911; S44911.
DR RefSeq; NP_498691.1; NM_066290.4.
DR AlphaFoldDB; P34669; -.
DR SMR; P34669; -.
DR BioGRID; 41297; 10.
DR ComplexPortal; CPX-968; Oligosaccharyl transferase complex.
DR DIP; DIP-24707N; -.
DR STRING; 6239.ZK686.3.1; -.
DR EPD; P34669; -.
DR PaxDb; P34669; -.
DR PeptideAtlas; P34669; -.
DR EnsemblMetazoa; ZK686.3.1; ZK686.3.1; WBGene00022793.
DR GeneID; 176089; -.
DR KEGG; cel:CELE_ZK686.3; -.
DR UCSC; ZK686.3; c. elegans.
DR CTD; 176089; -.
DR WormBase; ZK686.3; CE00457; WBGene00022793; -.
DR eggNOG; KOG2603; Eukaryota.
DR GeneTree; ENSGT00390000012030; -.
DR HOGENOM; CLU_052855_0_0_1; -.
DR InParanoid; P34669; -.
DR OrthoDB; 1460433at2759; -.
DR Reactome; R-CEL-5223345; Miscellaneous transport and binding events.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:P34669; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022793; Expressed in embryo and 4 other tissues.
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:0006487; P:protein N-linked glycosylation; IC:ComplexPortal.
DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12692; PTHR12692; 1.
DR Pfam; PF04756; OST3_OST6; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..340
FT /note="Probable dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 3"
FT /id="PRO_0000215299"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 33..164
FT /note="Thioredoxin"
FT DISULFID 73..76
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 38828 MW; D5C600C22AD11368 CRC64;
MRTMVLLFFM LLAVYESAQQ QTLEDKVQNL VDLTSRQSIV KFNMDKWKTL VRMQPRNYSM
IVMFTALSPG VQCPICKPAY DEFMIVANSH RYTSSEGDRR KVFFGIVDYE DAPQIFQQMN
LNTAPILYHF GPKLGAKKRP EQMDFQRQGF DADAIGRFVA DQTEVHVRVI RPPNYTAPVV
IALFVALLLG MLYMKRNSLD FLFNRTVWGF VCLAITFIFM SGQMWNHIRG PPFMITNPNT
KEPSFIHGST QFQLIAETYI VGLLYALIAI GFICVNEAAD QSNSKDRKNA GKKLNPLSLL
NIPTNTLAIA GLVCICVFFS FLLSVFRSKY RGYPYSFLFA
