ID   OST4_CANAX              Reviewed;          60 AA.
AC   Q9P838;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 4 kDa subunit;
DE            Short=OTase 4 kDa subunit;
DE            Short=Oligosaccharyl transferase 4 kDa subunit;
GN   Name=OST4;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   De Backer M.D., Logghe M., Viaene J., Loonen I., Vandoninck S.,
RA   de Hoogt R., Nelissen B., Dewaele S., Simons F., Verhasselt P.,
RA   Contreras R., Luyten W.H.M.L.;
RT   "A novel method for systematic identification of genes required for growth
RT   of Candida albicans.";
RL   Submitted (DEC-1999) 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:Q99380}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:Q99380}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type III membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the OST4 family. {ECO:0000305}.
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DR   EMBL; AJ390501; CAB77641.1; -; mRNA.
DR   AlphaFoldDB; Q9P838; -.
DR   SMR; Q9P838; -.
DR   CGD; CAL0000177487; orf19.1360.1.
DR   VEuPathDB; FungiDB:CAWG_06063; -.
DR   PhylomeDB; Q9P838; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR018943; Oligosaccaryltransferase.
DR   InterPro; IPR036330; Ost4p_sf.
DR   Pfam; PF10215; Ost4; 1.
DR   SUPFAM; SSF103464; SSF103464; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..60
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase 4 kDa subunit"
FT                   /id="PRO_0000058096"
FT   TOPO_DOM        1..6
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..60
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          37..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   60 AA;  6672 MW;  A4F07689FFBBFCA4 CRC64;
     MITDEQLNTI ALTFGFASII LIIIYHAIST NVHKLEDETP SSSFTRTNTT ETTVASKKKK