ID A0A0R3SWU2_HYMDI Unreviewed; 313 AA.
AC A0A0R3SWU2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Magnesium transporter protein 1 {ECO:0000313|WBParaSite:HDID_0001017201-mRNA-1};
GN ORFNames=HDID_LOCUS10170 {ECO:0000313|EMBL:VDL62819.1};
OS Hymenolepis diminuta (Rat tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0001017201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HDID_0001017201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL62819.1, ECO:0000313|Proteomes:UP000274504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; UYSG01011553; VDL62819.1; -; Genomic_DNA.
DR STRING; 6216.A0A0R3SWU2; -.
DR WBParaSite; HDID_0001017201-mRNA-1; HDID_0001017201-mRNA-1; HDID_0001017201.
DR Proteomes; UP000046397; Unplaced.
DR Proteomes; UP000274504; 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:UP000274504};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..313
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040668280"
FT TRANSMEM 174..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 313 AA; 35162 MW; E9F1DD0A90D172EA CRC64;
MAIHSGFVVI LFVVLGLILS NADENVLDET VHVLKTLPRE GGLMLLSSHI FEKYIIPAQR
NFSIVFIVAS LKSQCDPCVP AMAALANIAN KWEKEHRDSS EIFFGFIDFQ DNINFIKMLN
INTAPFVYHI GPQQSMHEWD KVNEFNIVSH PALLASWISK LSNVKVEASV PVDMSLIYFG
ALFLVIAYLL YKIKLFRSVQ FVGILCLVFI CTMLSGFMWV NIHNTPFISY QGGQVTFVYP
RNGAQLGSEV LLIMSFYVMT SGGVVLLTTK CPKYRKSKFL HSIGVLVCLG LTIMGFNQMA
TYYNTKTGHT AYQ
//
