GenomeNet

Database: UniProt
Entry: A0DVR6_PARTE
LinkDB: A0DVR6_PARTE
Original site: A0DVR6_PARTE 
ID   A0DVR6_PARTE            Unreviewed;       346 AA.
AC   A0DVR6;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Chromosome undetermined scaffold_66, whole genome shotgun sequence {ECO:0000313|EMBL:CAK87133.1};
GN   ORFNames=GSPATT00020786001 {ECO:0000313|EMBL:CAK87133.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK87133.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK87133.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK87133.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
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}.
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; CT868607; CAK87133.1; -; Genomic_DNA.
DR   RefSeq; XP_001454530.1; XM_001454493.1.
DR   AlphaFoldDB; A0DVR6; -.
DR   STRING; 5888.A0DVR6; -.
DR   EnsemblProtists; CAK87133; CAK87133; GSPATT00020786001.
DR   GeneID; 5040315; -.
DR   KEGG; ptm:GSPATT00020786001; -.
DR   eggNOG; KOG2603; Eukaryota.
DR   HOGENOM; CLU_781880_0_0_1; -.
DR   InParanoid; A0DVR6; -.
DR   OMA; KVPDYPY; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
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:UP000000600};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        181..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        262..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   346 AA;  40083 MW;  64F27048B3F4D58A CRC64;
     MIIILLFLVN FINADPLATQ KTNELREMQL RDGIIELNST GYFYYTMEFP RPYDIVIYFV
     APSCKLCNDL NEHYQKVAKF YADSGALYKS ESKRAVFFAT MTFNDKNKQV FEQLGFISAP
     NLFISQPHIV FVPQDERERY LRDMKWTISY TDGTVTAHKF LEFINKRTGR QVDYKASTSE
     ALTVIGVLLG ALTFGGLIFI IARPLFLNPK LWFIGSIIIF ITCLAGVVYN IIHNVPFFSQ
     NNRGGLQWKT NSGRQQLGFE GLFLSLGMTF VGLTMVLIMK FKVLVKHQKL SIFIERFIYV
     ALFAAIFIFI QFVEENYRQK SHYNPIYWPP KHYIKGPLNR DQGNSF
//
DBGET integrated database retrieval system