ID   MAGT1_XENLA             Reviewed;         329 AA.
AC   Q63ZR0;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Magnesium transporter protein 1 {ECO:0000250|UniProtKB:Q9H0U3};
DE            Short=MagT1;
DE   AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1;
DE            Short=Oligosaccharyl transferase subunit MAGT1;
DE   Flags: Precursor;
GN   Name=magt1 {ECO:0000250|UniProtKB:Q9H0U3};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Accessory component of the STT3B-containing form of the N-
CC       oligosaccharyl transferase (OST) complex which catalyzes the transfer
CC       of a high mannose oligosaccharide from a lipid-linked oligosaccharide
CC       donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif
CC       in nascent polypeptide chains. May be involved in substrate-specific N-
CC       glycosylation involving acceptor sites that are near cysteine residues.
CC       {ECO:0000250|UniProtKB:Q9H0U3}.
CC   -!- FUNCTION: May be involved in Mg(2+) transport in epithelial cells.
CC       {ECO:0000250|UniProtKB:Q9CQY5, ECO:0000250|UniProtKB:Q9H0U3}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9H0U3}.
CC   -!- SUBUNIT: Accessory component of the STT3B-containing form of the
CC       oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:Q9H0U3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H0U3};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H0U3}. Endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:Q9H0U3}. Endoplasmic reticulum
CC       membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
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DR   EMBL; BC082850; AAH82850.1; -; mRNA.
DR   RefSeq; NP_001088056.1; NM_001094587.1.
DR   AlphaFoldDB; Q63ZR0; -.
DR   SMR; Q63ZR0; -.
DR   BioGRID; 104830; 1.
DR   DNASU; 494750; -.
DR   GeneID; 494750; -.
DR   KEGG; xla:494750; -.
DR   CTD; 494750; -.
DR   Xenbase; XB-GENE-998609; magt1.L.
DR   OrthoDB; 1460433at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 494750; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
DR   InterPro; IPR006844; Mg_transporter-1.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12692; PTHR12692; 1.
DR   PANTHER; PTHR12692:SF2; PTHR12692:SF2; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   Magnesium; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..329
FT                   /note="Magnesium transporter protein 1"
FT                   /id="PRO_0000246062"
FT   TOPO_DOM        24..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..212
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..258
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..294
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..329
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          41..169
FT                   /note="Thioredoxin"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        81..84
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   329 AA;  36918 MW;  9D03E232CF4C5AE4 CRC64;
     MAGLKGLLFG GILFAMCGGL SEGQKKKEMV LSDKVGQLMD WASKRPVIRM NGDKFRRFIK
     SPPRNYSVVV MFTALQAHRQ CVVCKQADEE YQILANSWRY SSAFTNRIFF AVVDFDEGSD
     VFQMLNMNSA PTFINFPPKG KPKKGDTYEL QVRGFAAEQL ARWVADRTDV NIRVIRPPNY
     AGPLMLGLLL AVIGGLVYLR RSNLDFLNNK TGWALAALCF VLAMTSGQMW NHIRGPPYAH
     KNPHTNQVNY IHGSSQAQFV AETHIVLLFN GAVTLGMVLL HEAATSDLDV GKRKIMCIAG
     ITLVVIFFSW LLSVFRSKYH GYPYSFLMT