ID F9XC12_ZYMTI Unreviewed; 137 AA.
AC F9XC12;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=MYCGRDRAFT_86073 {ECO:0000313|EMBL:EGP87623.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP87623.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP87623.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001200; EGP87623.1; -; Genomic_DNA.
DR RefSeq; XP_003852647.1; XM_003852599.1.
DR AlphaFoldDB; F9XC12; -.
DR STRING; 336722.F9XC12; -.
DR EnsemblFungi; Mycgr3T86073; Mycgr3P86073; Mycgr3G86073.
DR GeneID; 13393954; -.
DR KEGG; ztr:MYCGRDRAFT_86073; -.
DR eggNOG; KOG1746; Eukaryota.
DR HOGENOM; CLU_111220_0_0_1; -.
DR InParanoid; F9XC12; -.
DR OrthoDB; 206600at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008062; Chromosome 5.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblFungi.
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:UP000008062};
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 53..73
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361136"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361136"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 137 AA; 14933 MW; AF945F3C937D133E CRC64;
MSASSTAQSI KASTPTPSRS SNAKGSNSFP DIVAGVWNNY TTKTPQRVKL LDTFMGFLVV
VGVLQFVYCV IAGNYPFNAF LSGFSATVGQ FVLTASLRIQ TNPENKAEFE GISHERAFAD
FIFGSLILHF FCVNFIN
//