MAGT1_RAT
ID MAGT1_RAT Reviewed; 335 AA.
AC O35777;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Magnesium transporter protein 1 {ECO:0000305};
DE Short=MagT1;
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1;
DE Short=Oligosaccharyl transferase subunit MAGT1;
DE AltName: Full=Implantation-associated protein;
DE Short=IAP;
DE Flags: Precursor;
GN Name=Magt1 {ECO:0000312|RGD:620094}; Synonyms=Iag2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Uterus;
RA Barkai U., Amit A., Lessing J.B., Kraicer P.F., Kidron T.;
RT "Implantation-associated uterine protein.";
RL Submitted (MAR-1999) 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. Involved in N-glycosylation of STT3B-
CC dependent substrates. Specifically required for the glycosylation of a
CC subset of acceptor sites that are near cysteine residues; in this
CC function seems to act redundantly with TUSC3. In its oxidized form
CC proposed to form transient mixed disulfides with a glycoprotein
CC substrate to facilitate access of STT3B to the unmodified acceptor
CC site. Has also oxidoreductase-independent functions in the STT3B-
CC containing OST complex possibly involving substrate recognition.
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. OST exists in two different
CC complex forms which contain common core subunits RPN1, RPN2, OST48,
CC OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits,
CC and form-specific accessory subunits. OST can form stable complexes
CC with the Sec61 complex or with both the Sec61 and TRAP complexes. The
CC association of TUSC3 or MAGT1 with the STT3B-containing complex seems
CC to be mutually exclusvice. {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; AF008554; AAB63294.2; -; mRNA.
DR RefSeq; NP_446398.1; NM_053946.1.
DR AlphaFoldDB; O35777; -.
DR SMR; O35777; -.
DR STRING; 10116.ENSRNOP00000062502; -.
DR GlyGen; O35777; 1 site.
DR jPOST; O35777; -.
DR PaxDb; O35777; -.
DR PeptideAtlas; O35777; -.
DR PRIDE; O35777; -.
DR GeneID; 116967; -.
DR KEGG; rno:116967; -.
DR UCSC; RGD:620094; rat.
DR CTD; 84061; -.
DR RGD; 620094; Magt1.
DR eggNOG; KOG2603; Eukaryota.
DR InParanoid; O35777; -.
DR OrthoDB; 1460433at2759; -.
DR PhylomeDB; O35777; -.
DR Reactome; R-RNO-5223345; Miscellaneous transport and binding events.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR UniPathway; UPA00378; -.
DR PRO; PR:O35777; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0015693; P:magnesium ion transport; ISO:RGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:RGD.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISO:RGD.
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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..335
FT /note="Magnesium transporter protein 1"
FT /id="PRO_0000215301"
FT TOPO_DOM 30..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 47..175
FT /note="Thioredoxin"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..90
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 37993 MW; AFB9DB35F1A06091 CRC64;
MASPRWLWCV CATAAVTLLL VSKVPSASAQ RKKEKVLVEK VIQLMEWTNQ RPVIRMNGDK
FRPLVKAPPR NYSVIVMFTA LQLHRQCVVC KQADEEFQIL ANFWRYSSAF TNRIFFAMVD
FDEGSDVFQM LNMNSAPTFI NFPPKGKPKR ADTYELQVRG FSAEQIARWI ADRTDVNIRV
IRPPNYAGPL MLGLLLAVIG GLVYLRRSNM EFLFNKTGWA FAALCFVLAM TSGQMWNHIR
GPPYAHKNPH TGHVNYIHGS SQAQFVAETH IVLLFNGGVT LGMVLLCEAA ASDMDIGKRR
MMCIAGIGLV VLFFSWMLSI FRSKYHGYPY SFLMS
