MAGT1_CHICK
ID MAGT1_CHICK Reviewed; 328 AA.
AC Q5ZJ06;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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}; ORFNames=RCJMB04_22a7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 its
CC oxidized form proposed to form transient mixed disulfides with a
CC glycoprotein substrate to facilitate access of STT3B to the unmodified
CC acceptor site. Has also oxidoreductase-independent functions in the
CC STT3B-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.
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; AJ720628; CAG32287.1; -; mRNA.
DR RefSeq; NP_001006435.1; NM_001006435.1.
DR AlphaFoldDB; Q5ZJ06; -.
DR SMR; Q5ZJ06; -.
DR STRING; 9031.ENSGALP00000012744; -.
DR PaxDb; Q5ZJ06; -.
DR GeneID; 422332; -.
DR KEGG; gga:422332; -.
DR CTD; 84061; -.
DR VEuPathDB; HostDB:geneid_422332; -.
DR eggNOG; KOG2603; Eukaryota.
DR InParanoid; Q5ZJ06; -.
DR OrthoDB; 1460433at2759; -.
DR PhylomeDB; Q5ZJ06; -.
DR BRENDA; 7.2.2.14; 1306.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5ZJ06; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..328
FT /note="Magnesium transporter protein 1"
FT /id="PRO_0000246060"
FT TOPO_DOM 23..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..328
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 40..168
FT /note="Thioredoxin"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..83
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 328 AA; 36762 MW; 2C915B132A092B05 CRC64;
MAALPVLVLV LLLACGGPRA AGQKRKEMVL SEKVSQLMEW TSKRSVIRMN GDKFRRLVKA
PPRNYSVIVM FTALQPHRQC VVCKQADEEY QVLANSWRYS SAFTNKIFFA MVDFDEGSDV
FQMLNMNSAP TFINFPAKGK PKRGDTYELQ VRGFAAEQLA RWVADRTDVN IRVIRPPNYA
GPLMLGLLLA VIGGLVYLRG SNLDFLYNKT GWAFAALCFV LAMTSGQMWN HIRGPPYAHK
NPHTGQVNYI HGSSQAQFVA ETHIVLLFNG GVTLGMVLLH EAATSDMDVG KRKIMCIAGI
GLVVFFFSWL LSVFRSKYHG YPYSFLMS
