MAGT1_MOUSE
ID MAGT1_MOUSE Reviewed; 335 AA.
AC Q9CQY5; Q3UW45; Q9CWX5; Q9CZT3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
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|MGI:MGI:1914325}; Synonyms=Iag2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15804357; DOI=10.1186/1471-2164-6-48;
RA Goytain A., Quamme G.A.;
RT "Identification and characterization of a novel mammalian Mg2+ transporter
RT with channel-like properties.";
RL BMC Genomics 6:48-48(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Cecum, Epididymis, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000305|PubMed:15804357}.
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=3;
CC Name=1;
CC IsoId=Q9CQY5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQY5-2; Sequence=VSP_019822;
CC Name=3;
CC IsoId=Q9CQY5-3; Sequence=VSP_019823;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in kidney, colon, heart
CC and liver. Expressed at lower levels in intestine, spleen, brain and
CC lung. {ECO:0000269|PubMed:15804357}.
CC -!- INDUCTION: Induced by low magnesium levels.
CC {ECO:0000269|PubMed:15804357}.
CC -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
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; DQ000005; AAY18812.1; -; mRNA.
DR EMBL; AK010320; BAB26851.1; -; mRNA.
DR EMBL; AK018623; BAB31313.1; -; mRNA.
DR EMBL; AK012185; BAB28085.1; -; mRNA.
DR EMBL; AK136622; BAE23074.1; -; mRNA.
DR EMBL; AK144696; BAE26020.1; -; mRNA.
DR EMBL; AK013243; BAB28739.1; -; mRNA.
DR EMBL; BC003881; AAH03881.1; -; mRNA.
DR CCDS; CCDS53168.2; -. [Q9CQY5-1]
DR RefSeq; NP_001177338.1; NM_001190409.1. [Q9CQY5-1]
DR RefSeq; NP_080228.4; NM_025952.4. [Q9CQY5-1]
DR AlphaFoldDB; Q9CQY5; -.
DR SMR; Q9CQY5; -.
DR ComplexPortal; CPX-5822; Oligosaccharyltransferase complex B.
DR STRING; 10090.ENSMUSP00000120994; -.
DR GlyConnect; 2498; 1 N-Linked glycan (1 site).
DR GlyGen; Q9CQY5; 1 site, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q9CQY5; -.
DR EPD; Q9CQY5; -.
DR jPOST; Q9CQY5; -.
DR MaxQB; Q9CQY5; -.
DR PaxDb; Q9CQY5; -.
DR PRIDE; Q9CQY5; -.
DR ProteomicsDB; 252721; -. [Q9CQY5-1]
DR ProteomicsDB; 252722; -. [Q9CQY5-2]
DR ProteomicsDB; 252723; -. [Q9CQY5-3]
DR Antibodypedia; 43998; 123 antibodies from 22 providers.
DR DNASU; 67075; -.
DR Ensembl; ENSMUST00000113566; ENSMUSP00000109196; ENSMUSG00000031232. [Q9CQY5-1]
DR Ensembl; ENSMUST00000139421; ENSMUSP00000115579; ENSMUSG00000031232. [Q9CQY5-2]
DR Ensembl; ENSMUST00000151689; ENSMUSP00000120994; ENSMUSG00000031232. [Q9CQY5-1]
DR GeneID; 67075; -.
DR KEGG; mmu:67075; -.
DR CTD; 84061; -.
DR MGI; MGI:1914325; Magt1.
DR VEuPathDB; HostDB:ENSMUSG00000031232; -.
DR eggNOG; KOG2603; Eukaryota.
DR GeneTree; ENSGT00390000012030; -.
DR InParanoid; Q9CQY5; -.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR UniPathway; UPA00378; -.
DR ChiTaRS; Magt1; mouse.
DR PRO; PR:Q9CQY5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9CQY5; protein.
DR Bgee; ENSMUSG00000031232; Expressed in parotid gland and 240 other tissues.
DR ExpressionAtlas; Q9CQY5; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
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:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0015693; P:magnesium ion transport; ISO:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISO:MGI.
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 1: Evidence at protein 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_0000246058"
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 301..335
FT /note="MMCIAGIGLVVLFFSWMLSIFRSKYHGYPYSFLMS -> NNFCQA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019822"
FT VAR_SEQ 301..335
FT /note="MMCIAGIGLVVLFFSWMLSIFRSKYHGYPYSFLMS -> TKSHVTMVQFCL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019823"
FT CONFLICT 249
FT /note="P -> T (in Ref. 2; BAE23074)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="I -> N (in Ref. 1; AAY18812 and 2; BAB28085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 37970 MW; 420D7808F31792B0 CRC64;
MASPRWFWSV CAIAAVALLL VSKVPSASAQ RKKEMVLSEK VSQLMEWANK RPVIRMNGDK
FRRLVKAPPR NYSVVVMFTA LQLHRQCVVC KQADEEFQIL ANSWRYSNAF TNRIFFAMVD
FDEGSDVFQM LNMNSAPTFI NFPPKGKPKR ADTYELQVRG FSAEQIARWI ADRTDVNIRV
IRPPNYAGPL MLGLLLAVIG GLVYLRRSNM EFLFNKTGWA FAALCFVLAM TSGQMWNHIR
GPPYAHKNPH TGHVNYIHGS SQAQFVAETH IVLLFNGGVT LGMVLLCEAA TSDMDIGKRR
MMCIAGIGLV VLFFSWMLSI FRSKYHGYPY SFLMS
