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Database: UniProt
Entry: A0A3N4I2N5_ASCIM
LinkDB: A0A3N4I2N5_ASCIM
Original site: A0A3N4I2N5_ASCIM 
ID   A0A3N4I2N5_ASCIM        Unreviewed;       334 AA.
AC   A0A3N4I2N5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Oligosaccharyl transferase subunit {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BJ508DRAFT_415833 {ECO:0000313|EMBL:RPA79697.1};
OS   Ascobolus immersus RN42.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Ascobolaceae; Ascobolus.
OX   NCBI_TaxID=1160509 {ECO:0000313|EMBL:RPA79697.1, ECO:0000313|Proteomes:UP000275078};
RN   [1] {ECO:0000313|EMBL:RPA79697.1, ECO:0000313|Proteomes:UP000275078}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN42 {ECO:0000313|EMBL:RPA79697.1,
RC   ECO:0000313|Proteomes:UP000275078};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(2018).
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|ARBA:ARBA00002791}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the OST3/OST6 family.
CC       {ECO:0000256|ARBA:ARBA00009561}.
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DR   EMBL; ML119696; RPA79697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4I2N5; -.
DR   STRING; 1160509.A0A3N4I2N5; -.
DR   Proteomes; UP000275078; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12692; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR12692:SF0; GH11935P; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275078};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..334
FT                   /note="Oligosaccharyl transferase subunit"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018325663"
FT   TRANSMEM        186..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   334 AA;  36948 MW;  BB25F1DFC607B502 CRC64;
     MRLLHSLLTL LPLASTLISA SSSTPADLDP KHTQLLSKST NGLIRVDDPT FEALVTGPRA
     YTSVILLTAL DKRIGCDMCH LFQPDFELLA KSWWEKGPKE ERHRLLFGST DYSKAKGTFQ
     KLGLTSAPVL YIFPPTVGPN AAPANAQPYK YDFLPTAKQG EHLARVISTQ SGLPVQLHRP
     IDYTKYYLTA ATILSILLTL KFALPYLLPV LLNRNLWAAL TLIAIFLFTS GHMFNHIRKV
     PYMASDGRGG VSYIAGGFSN QYGAETQLVA VLYAGLTFCV IALGMKVPRM EGRGRQDVAV
     LVWSVVVWLG MGYLMTVFRV KNPAYPFYLP PLVK
//
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