ID A0A3P7B5F9_SCHSO Unreviewed; 246 AA.
AC A0A3P7B5F9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Tumor suppressor candidate 3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=SSLN_LOCUS133 {ECO:0000313|EMBL:VDL82039.1};
OS Schistocephalus solidus (Tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX NCBI_TaxID=70667 {ECO:0000313|EMBL:VDL82039.1, ECO:0000313|Proteomes:UP000275846};
RN [1] {ECO:0000313|EMBL:VDL82039.1, ECO:0000313|Proteomes:UP000275846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NST_G2 {ECO:0000313|EMBL:VDL82039.1,
RC ECO:0000313|Proteomes:UP000275846};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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: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; UYSU01000069; VDL82039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P7B5F9; -.
DR STRING; 70667.A0A3P7B5F9; -.
DR Proteomes; UP000275846; 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:UP000275846};
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 153..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 246 AA; 27861 MW; 6A7013FE65F4BFE1 CRC64;
MSILASKFRQ LTELSDKSPI LRLNYEQFTD LVRGAPRNYS VFSMLTALAD QRKCHSCQAA
NDEFNTLASS WQKLKNAKSK IFLLLVDFDE NPKIFKELNQ NTVPVFIHFP PSGSPSGADF
LDISRSGFGA ETLARWIFSR TSVEIPIIRQ TSYAGAILLL IIAGLVGAML FLRPDNLEFI
IHRSTLSYAV LIFYIISGQV WNSIRRPPFF HSPPQGGIVS SNTSQTSTFR HFYTQEATFS
SFRKRY
//
