ID C1GK53_PARBD Unreviewed; 174 AA.
AC C1GK53;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2 {ECO:0000256|RuleBase:RU361136};
DE Short=Oligosaccharyl transferase subunit OST2 {ECO:0000256|RuleBase:RU361136};
GN ORFNames=PADG_07639 {ECO:0000313|EMBL:EEH42819.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH42819.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH42819.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH42819.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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:0000256|RuleBase:RU361136}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU361136}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000256|RuleBase:RU361136}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU361136}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU361136}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the DAD/OST2 family.
CC {ECO:0000256|ARBA:ARBA00009386, ECO:0000256|RuleBase:RU361136}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361136}.
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DR EMBL; KN275968; EEH42819.1; -; Genomic_DNA.
DR RefSeq; XP_010763086.1; XM_010764784.1.
DR AlphaFoldDB; C1GK53; -.
DR STRING; 502780.C1GK53; -.
DR GeneID; 22586101; -.
DR KEGG; pbn:PADG_07639; -.
DR VEuPathDB; FungiDB:PADG_07639; -.
DR eggNOG; KOG1746; Eukaryota.
DR HOGENOM; CLU_111220_0_0_1; -.
DR InParanoid; C1GK53; -.
DR OMA; QSNPQNK; -.
DR OrthoDB; 206600at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003038; DAD/Ost2.
DR PANTHER; PTHR10705; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT DAD1; 1.
DR PANTHER; PTHR10705:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT DAD1; 1.
DR Pfam; PF02109; DAD; 1.
DR PIRSF; PIRSF005588; DAD; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU361136};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361136};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361136};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361136}.
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361136"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361136"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 174 AA; 18565 MW; F31FB0C5BCB3CBDF CRC64;
MSPKRRVASN SAASQAQPAP TPAKTSPRTA PMTSHASKTS LSPNSSAQEI VVGIWQRYLS
QTPKRTLQLD AFMAFLVLVG AVQFVYCLLA GNYPFNAFLG GFSAAVGQFV LTASLRMQTS
HQGGRDGKAT STSNTVSPPT DGHLLSNGTS SERAFADYVF GSLILHFFCI NFIN
//
