ID   OSTC_CHICK              Reviewed;         149 AA.
AC   Q5ZJR3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Oligosaccharyltransferase complex subunit OSTC {ECO:0000250|UniProtKB:Q9NRP0};
GN   Name=OSTC {ECO:0000250|UniProtKB:Q9NRP0}; ORFNames=RCJMB04_16e19;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Specific component of the STT3A-containing form of the
CC       oligosaccharyl transferase (OST) complex that catalyzes the initial
CC       transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from
CC       the lipid carrier dolichol-pyrophosphate to an asparagine residue
CC       within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains,
CC       the first step in protein N-glycosylation. 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. {ECO:0000250|UniProtKB:Q9NRP0}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9NRP0}.
CC   -!- SUBUNIT: Specific component of the STT3A-containing form of the
CC       oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:P86218}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the OSTC family. {ECO:0000305}.
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DR   EMBL; AJ720371; CAG32030.1; -; mRNA.
DR   RefSeq; NP_001006442.1; NM_001006442.1.
DR   AlphaFoldDB; Q5ZJR3; -.
DR   SMR; Q5ZJR3; -.
DR   STRING; 9031.ENSGALP00000017119; -.
DR   PRIDE; Q5ZJR3; -.
DR   Ensembl; ENSGALT00000017138; ENSGALP00000017119; ENSGALG00000010526.
DR   Ensembl; ENSGALT00000086076; ENSGALP00000063282; ENSGALG00000010526.
DR   GeneID; 422525; -.
DR   KEGG; gga:422525; -.
DR   CTD; 58505; -.
DR   VEuPathDB; HostDB:geneid_422525; -.
DR   eggNOG; KOG3356; Eukaryota.
DR   GeneTree; ENSGT00390000001376; -.
DR   HOGENOM; CLU_109136_1_0_1; -.
DR   InParanoid; Q5ZJR3; -.
DR   OMA; WIFMRMK; -.
DR   OrthoDB; 1575260at2759; -.
DR   PhylomeDB; Q5ZJR3; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q5ZJR3; -.
DR   Proteomes; UP000000539; Chromosome 4.
DR   Bgee; ENSGALG00000010526; Expressed in spermatocyte and 14 other tissues.
DR   ExpressionAtlas; Q5ZJR3; baseline and differential.
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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   InterPro; IPR042416; OSTC.
DR   PANTHER; PTHR13160; PTHR13160; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..149
FT                   /note="Oligosaccharyltransferase complex subunit OSTC"
FT                   /id="PRO_0000320604"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..83
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..117
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..149
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   149 AA;  16743 MW;  1FC0AB6055415E17 CRC64;
     METLFRLPFA VLECPNIKLK RPGWVHMPSA MTVYALVVVS YFLITGGIIY DVIVEPPSVG
     SMTDEHGHQR PVAFLAYRVN GQYIMEGLAS SFLFTMGGLG FIILDRSNAP NIPKLNRFLL
     LFIGFVSVLL SFFMARVFMR MKLPGYLMG