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MAGT1_PONAB
ID   MAGT1_PONAB             Reviewed;         335 AA.
AC   Q5RE31; Q5REG3;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
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   AltName: Full=Implantation-associated protein;
DE            Short=IAP;
DE   Flags: Precursor;
GN   Name=MAGT1 {ECO:0000250|UniProtKB:Q9H0U3}; Synonyms=IAG2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain cortex, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-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. 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5RE31-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5RE31-2; Sequence=VSP_019824;
CC   -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
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DR   EMBL; CR857566; CAH89844.1; -; mRNA.
DR   EMBL; CR857707; CAH89976.1; -; mRNA.
DR   RefSeq; NP_001124931.1; NM_001131459.2. [Q5RE31-1]
DR   RefSeq; NP_001128755.1; NM_001135283.1.
DR   AlphaFoldDB; Q5RE31; -.
DR   SMR; Q5RE31; -.
DR   STRING; 9601.ENSPPYP00000022939; -.
DR   GeneID; 100171802; -.
DR   GeneID; 100189651; -.
DR   KEGG; pon:100171802; -.
DR   CTD; 84061; -.
DR   eggNOG; KOG2603; Eukaryota.
DR   InParanoid; Q5RE31; -.
DR   OrthoDB; 1460433at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001595; Unplaced.
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   Alternative splicing; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Magnesium; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..335
FT                   /note="Magnesium transporter protein 1"
FT                   /id="PRO_0000246059"
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"
FT   VAR_SEQ         1..34
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_019824"
FT   CONFLICT        42
FT                   /note="C -> S (in Ref. 1; CAH89844)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="S -> C (in Ref. 1; CAH89844)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="C -> G (in Ref. 1; CAH89844)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  37952 MW;  C71B5C8B1B24B759 CRC64;
     MAAGWWFWCV SVTVAVALLI VCDVPSVSAQ RKKEMVLSEK VCQLMEWTNK RPVIRMNGDK
     FRRLVKAPPR NYSVIVMFTA LQLHRQCVVC KQADEEFQIL ANSWRYSSAF TNRIFFAMVD
     FDEGSDVFQM LNMNSAPTFI NFPAKGKPKR GDTYELQVRG FSAEQIARWI ADRTDVNIRV
     IRPPNYAGPL MLGLLLAVIG GLVYLRRSNM EFLFNKTGWA FAALCFVLAM TSGQMWNHIR
     GPPYAHKNPH TGHVNYIHGS SQAQFVAETH IVLLFNGGVT LGMVLLCEAA TSDMDIGKRK
     IMCVAGIGLV VLFFSWMLSI FRSKYHGYPY SFLMS
 
 
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