MAGT1_HUMAN
ID MAGT1_HUMAN Reviewed; 335 AA.
AC Q9H0U3; B2RAR4; D3DTE3; Q53G00; Q6P577; Q8NBN6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 192.
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|HGNC:HGNC:28880}; Synonyms=IAG2;
GN ORFNames=PSEC0084, UNQ628/PRO1244;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE 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] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adrenal cortex, Ovary, and Placenta;
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 [10]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, AND TISSUE
RP SPECIFICITY.
RX PubMed=12887896; DOI=10.1016/s1097-2765(03)00243-0;
RA Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
RT "Oligosaccharyltransferase isoforms that contain different catalytic STT3
RT subunits have distinct enzymatic properties.";
RL Mol. Cell 12:101-111(2003).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP TOPOLOGY.
RX PubMed=19717468; DOI=10.1073/pnas.0908332106;
RA Zhou H., Clapham D.E.;
RT "Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and
RT vertebrate embryonic development.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15750-15755(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION, IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-87 AND CYS-90.
RX PubMed=25135935; DOI=10.1083/jcb.201404083;
RA Cherepanova N.A., Shrimal S., Gilmore R.;
RT "Oxidoreductase activity is necessary for N-glycosylation of cysteine-
RT proximal acceptor sites in glycoproteins.";
RL J. Cell Biol. 206:525-539(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP FUNCTION.
RX PubMed=26864433; DOI=10.1038/srep20946;
RA Cherepanova N.A., Gilmore R.;
RT "Mammalian cells lacking either the cotranslational or posttranslocational
RT oligosaccharyltransferase complex display substrate-dependent defects in
RT asparagine linked glycosylation.";
RL Sci. Rep. 6:20946-20946(2016).
RN [16] {ECO:0007744|PDB:6S7T}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION AS
RP COMPONENT OF THE STT3B-CONTAINING OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX,
RP FUNCTION, AND PATHWAY.
RX PubMed=31831667; DOI=10.1126/science.aaz3505;
RA Ramirez A.S., Kowal J., Locher K.P.;
RT "Cryo-electron microscopy structures of human oligosaccharyltransferase
RT complexes OST-A and OST-B.";
RL Science 366:1372-1375(2019).
RN [17]
RP VARIANT GLY-311, AND POSSIBLE ASSOCIATION WITH X-LINKED INTELLECTUAL
RP DISABILITY.
RX PubMed=18455129; DOI=10.1016/j.ajhg.2008.03.021;
RA Molinari F., Foulquier F., Tarpey P.S., Morelle W., Boissel S., Teague J.,
RA Edkins S., Futreal P.A., Stratton M.R., Turner G., Matthijs G., Gecz J.,
RA Munnich A., Colleaux L.;
RT "Oligosaccharyltransferase-subunit mutations in nonsyndromic mental
RT retardation.";
RL Am. J. Hum. Genet. 82:1150-1157(2008).
RN [18]
RP INVOLVEMENT IN XMEN, VARIANT XMEN 137-PRO--SER-335 DEL, AND
RP CHARACTERIZATION OF VARIANT XMEN 137-PRO--SER-335 DEL.
RX PubMed=21796205; DOI=10.1038/nature10246;
RA Li F.Y., Chaigne-Delalande B., Kanellopoulou C., Davis J.C., Matthews H.F.,
RA Douek D.C., Cohen J.I., Uzel G., Su H.C., Lenardo M.J.;
RT "Second messenger role for Mg2+ revealed by human T-cell
RT immunodeficiency.";
RL Nature 475:471-476(2011).
RN [19]
RP LACK OF ASSOCIATION OF VARIANT GLY-311 WITH X-LINKED INTELLECTUAL
RP DISABILITY.
RX PubMed=23871722; DOI=10.1016/j.ajhg.2013.06.013;
RA Piton A., Redin C., Mandel J.L.;
RT "XLID-causing mutations and associated genes challenged in light of data
RT from large-scale human exome sequencing.";
RL Am. J. Hum. Genet. 93:368-383(2013).
RN [20]
RP INVOLVEMENT IN XMEN, VARIANT 137-PRO--SER-335 DEL, AND CHARACTERIZATION OF
RP VARIANT 137-PRO--SER-335 DEL.
RX PubMed=24550228; DOI=10.1182/blood-2013-11-538686;
RA Li F.Y., Chaigne-Delalande B., Su H., Uzel G., Matthews H., Lenardo M.J.;
RT "XMEN disease: a new primary immunodeficiency affecting Mg2+ regulation of
RT immunity against Epstein-Barr virus.";
RL Blood 123:2148-2152(2014).
RN [21]
RP VARIANT XMEN 238-HIS--SER-335 DEL, AND CHARACTERIZATION OF VARIANT XMEN
RP 238-HIS--SER-335 DEL.
RX PubMed=25504528; DOI=10.1007/s10875-014-0116-2;
RA Dhalla F., Murray S., Sadler R., Chaigne-Delalande B., Sadaoka T.,
RA Soilleux E., Uzel G., Miller J., Collins G.P., Hatton C.S., Bhole M.,
RA Ferry B., Chapel H.M., Cohen J.I., Patel S.Y.;
RT "Identification of a novel mutation in MAGT1 and progressive multifocal
RT leucoencephalopathy in a 58-year-old man with XMEN disease.";
RL J. Clin. Immunol. 35:112-118(2015).
RN [22]
RP INVOLVEMENT IN CDG1CC, VARIANT XMEN 313-PHE--SER-335 DEL, VARIANTS CDG1CC
RP ASN-324 AND 331-SER--SER-335 DEL, CHARACTERIZATION OF VARIANT XMEN
RP 313-PHE--SER-335 DEL, CHARACTERIZATION OF VARIANTS CDG1CC ASN-324 AND
RP 331-SER--SER-335 DEL, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=31036665; DOI=10.1073/pnas.1817815116;
RA Blommaert E., Peanne R., Cherepanova N.A., Rymen D., Staels F., Jaeken J.,
RA Race V., Keldermans L., Souche E., Corveleyn A., Sparkes R.,
RA Bhattacharya K., Devalck C., Schrijvers R., Foulquier F., Gilmore R.,
RA Matthijs G.;
RT "Mutations in MAGT1 lead to a glycosylation disorder with a variable
RT phenotype.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:9865-9870(2019).
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 (PubMed:31831667). Involved in N-
CC glycosylation of STT3B-dependent substrates (PubMed:31831667).
CC Specifically required for the glycosylation of a subset of acceptor
CC sites that are near cysteine residues; in this function seems to act
CC redundantly with TUSC3. In its oxidized form proposed to form transient
CC mixed disulfides with a glycoprotein substrate to facilitate access of
CC STT3B to the unmodified acceptor site. Has also oxidoreductase-
CC independent functions in the STT3B-containing OST complex possibly
CC involving substrate recognition. {ECO:0000269|PubMed:25135935,
CC ECO:0000269|PubMed:26864433, ECO:0000269|PubMed:31036665,
CC ECO:0000269|PubMed:31831667, ECO:0000305}.
CC -!- FUNCTION: May be involved in Mg(2+) transport in epithelial cells.
CC {ECO:0000305|PubMed:15804357, ECO:0000305|PubMed:19717468}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:31831667}.
CC -!- SUBUNIT: Accessory component of the STT3B-containing form of the
CC oligosaccharyltransferase (OST) complex (PubMed:31831667). OST exists
CC in two different complex forms which contain common core subunits RPN1,
CC RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic
CC subunits, and form-specific accessory subunits (PubMed:31831667). OST
CC can form stable complexes with the Sec61 complex or with both the Sec61
CC and TRAP complexes. The association of TUSC3 or MAGT1 with the STT3B-
CC containing complex seems to be mutually exclusvice.
CC {ECO:0000269|PubMed:25135935, ECO:0000269|PubMed:31831667,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19717468};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19717468}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:25135935}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0U3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0U3-2; Sequence=VSP_056556, VSP_056557;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at very low levels in brain,
CC lung and kidney. {ECO:0000269|PubMed:12887896,
CC ECO:0000269|PubMed:15804357, ECO:0000269|PubMed:19717468,
CC ECO:0000269|PubMed:31036665}.
CC -!- INDUCTION: Up-regulated by low extracellular Mg(2+).
CC {ECO:0000269|PubMed:19717468}.
CC -!- DISEASE: Immunodeficiency, X-linked, with magnesium defect, Epstein-
CC Barr virus infection and neoplasia (XMEN) [MIM:300853]: A disease
CC characterized by CD4 lymphopenia, severe chronic viral infections, and
CC defective T-lymphocyte activation. {ECO:0000269|PubMed:21796205,
CC ECO:0000269|PubMed:24550228, ECO:0000269|PubMed:25504528,
CC ECO:0000269|PubMed:31036665}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Congenital disorder of glycosylation 1CC (CDG1CC)
CC [MIM:301031]: A form of congenital disorder of glycosylation, a
CC multisystem disorder caused by a defect in glycoprotein biosynthesis
CC and characterized by under-glycosylated serum glycoproteins. Congenital
CC disorders of glycosylation result in a wide variety of clinical
CC features, such as defects in the nervous system development,
CC psychomotor retardation, dysmorphic features, hypotonia, coagulation
CC disorders, and immunodeficiency. The broad spectrum of features
CC reflects the critical role of N-glycoproteins during embryonic
CC development, differentiation, and maintenance of cell functions. CDG1CC
CC is an X-linked recessive form mainly characterized by intellectual and
CC developmental disability. {ECO:0000269|PubMed:31036665}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
CC -!- CAUTION: Although MAGT1 has been reported to be involved in
CC intellectual disability (PubMed:18455129), its pathological role is
CC questionable (PubMed:23871722). {ECO:0000305|PubMed:18455129,
CC ECO:0000305|PubMed:23871722}.
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DR EMBL; DQ000004; AAY18811.1; -; mRNA.
DR EMBL; AY358691; AAQ89054.1; -; mRNA.
DR EMBL; AK075394; BAC11592.1; -; mRNA.
DR EMBL; AL136636; CAB66571.1; -; mRNA.
DR EMBL; AK223131; BAD96851.1; -; mRNA.
DR EMBL; AK314309; BAG36961.1; -; mRNA.
DR EMBL; AL138743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471104; EAW98608.1; -; Genomic_DNA.
DR EMBL; CH471104; EAW98609.1; -; Genomic_DNA.
DR EMBL; CH471104; EAW98610.1; -; Genomic_DNA.
DR EMBL; BC041014; AAH41014.1; -; mRNA.
DR EMBL; BC060842; AAH60842.1; -; mRNA.
DR EMBL; BC063037; AAH63037.1; -; mRNA.
DR RefSeq; NP_115497.4; NM_032121.5.
DR PDB; 6S7T; EM; 3.50 A; H=1-335.
DR PDBsum; 6S7T; -.
DR AlphaFoldDB; Q9H0U3; -.
DR SMR; Q9H0U3; -.
DR BioGRID; 123856; 256.
DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B.
DR CORUM; Q9H0U3; -.
DR IntAct; Q9H0U3; 40.
DR MINT; Q9H0U3; -.
DR STRING; 9606.ENSP00000354649; -.
DR TCDB; 1.A.76.1.1; the magnesium transporter1 (magt1) family.
DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
DR GlyGen; Q9H0U3; 1 site.
DR iPTMnet; Q9H0U3; -.
DR PhosphoSitePlus; Q9H0U3; -.
DR SwissPalm; Q9H0U3; -.
DR BioMuta; MAGT1; -.
DR DMDM; 74761391; -.
DR EPD; Q9H0U3; -.
DR jPOST; Q9H0U3; -.
DR MassIVE; Q9H0U3; -.
DR MaxQB; Q9H0U3; -.
DR PaxDb; Q9H0U3; -.
DR PeptideAtlas; Q9H0U3; -.
DR PRIDE; Q9H0U3; -.
DR ProteomicsDB; 66990; -.
DR ProteomicsDB; 80324; -. [Q9H0U3-1]
DR Antibodypedia; 43998; 123 antibodies from 22 providers.
DR DNASU; 84061; -.
DR Ensembl; ENST00000358075.11; ENSP00000354649.6; ENSG00000102158.22. [Q9H0U3-1]
DR Ensembl; ENST00000373336.3; ENSP00000362433.3; ENSG00000102158.22. [Q9H0U3-2]
DR Ensembl; ENST00000618282.5; ENSP00000480732.1; ENSG00000102158.22. [Q9H0U3-1]
DR GeneID; 84061; -.
DR KEGG; hsa:84061; -.
DR MANE-Select; ENST00000618282.5; ENSP00000480732.1; NM_001367916.1; NP_001354845.1.
DR UCSC; uc065abq.1; human. [Q9H0U3-1]
DR CTD; 84061; -.
DR DisGeNET; 84061; -.
DR GeneCards; MAGT1; -.
DR GeneReviews; MAGT1; -.
DR HGNC; HGNC:28880; MAGT1.
DR HPA; ENSG00000102158; Low tissue specificity.
DR MalaCards; MAGT1; -.
DR MIM; 300715; gene.
DR MIM; 300853; phenotype.
DR MIM; 301031; phenotype.
DR neXtProt; NX_Q9H0U3; -.
DR OpenTargets; ENSG00000102158; -.
DR Orphanet; 317476; X-linked immunodeficiency with magnesium defect, Epstein-Barr virus infection and neoplasia.
DR PharmGKB; PA162394900; -.
DR VEuPathDB; HostDB:ENSG00000102158; -.
DR eggNOG; KOG2603; Eukaryota.
DR GeneTree; ENSGT00390000012030; -.
DR HOGENOM; CLU_052855_0_0_1; -.
DR InParanoid; Q9H0U3; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q9H0U3; -.
DR TreeFam; TF314850; -.
DR PathwayCommons; Q9H0U3; -.
DR Reactome; R-HSA-446203; Asparagine N-linked glycosylation.
DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; Q9H0U3; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 84061; 20 hits in 704 CRISPR screens.
DR ChiTaRS; MAGT1; human.
DR GeneWiki; RP11-217H1.1; -.
DR GenomeRNAi; 84061; -.
DR Pharos; Q9H0U3; Tbio.
DR PRO; PR:Q9H0U3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9H0U3; protein.
DR Bgee; ENSG00000102158; Expressed in palpebral conjunctiva and 205 other tissues.
DR ExpressionAtlas; Q9H0U3; baseline and differential.
DR Genevisible; Q9H0U3; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0015693; P:magnesium ion transport; IMP:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
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 3D-structure; Alternative splicing; Cell membrane;
KW Congenital disorder of glycosylation; Disease variant; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Magnesium; Membrane;
KW Reference proteome; Signal; 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_0000246057"
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 131..134
FT /note="LNMN -> FQVF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056556"
FT VAR_SEQ 135..335
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056557"
FT VARIANT 137..335
FT /note="Missing (in XMEN; no protein expression)"
FT /evidence="ECO:0000269|PubMed:21796205,
FT ECO:0000269|PubMed:24550228"
FT /id="VAR_083418"
FT VARIANT 238..335
FT /note="Missing (in XMEN; decreased protein expression)"
FT /evidence="ECO:0000269|PubMed:25504528"
FT /id="VAR_083419"
FT VARIANT 311
FT /note="V -> G (rare variant found in patients with X-linked
FT intellectual disability; unknown pathological significance;
FT dbSNP:rs145245774)"
FT /evidence="ECO:0000269|PubMed:18455129"
FT /id="VAR_045837"
FT VARIANT 313..335
FT /note="Missing (in XMEN; no protein expression; decreased
FT protein N-linked glycosylation of STT3B-specific
FT substrates)"
FT /evidence="ECO:0000269|PubMed:31036665"
FT /id="VAR_083420"
FT VARIANT 324
FT /note="K -> N (in CDG1CC; no effect on protein expression;
FT decreased protein N-linked glycosylation of STT3B-specific
FT substrates; dbSNP:rs373260156)"
FT /evidence="ECO:0000269|PubMed:31036665"
FT /id="VAR_083421"
FT VARIANT 331..335
FT /note="Missing (in CDG1CC; no protein expression; decreased
FT protein N-linked glycosylation of STT3B-specific
FT substrates)"
FT /evidence="ECO:0000269|PubMed:31036665"
FT /id="VAR_083422"
FT MUTAGEN 87
FT /note="C->S: Reduces N-glycosylation of cysteine-proximal
FT acceptor sites; when associated with S-90."
FT /evidence="ECO:0000269|PubMed:25135935"
FT MUTAGEN 90
FT /note="C->S: Reduces N-glycosylation of cysteine-proximal
FT acceptor sites; when associated with S-87."
FT /evidence="ECO:0000269|PubMed:25135935"
FT CONFLICT 30
FT /note="Q -> K (in Ref. 4; BAC11592)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="A -> V (in Ref. 6; BAD96851)"
FT /evidence="ECO:0000305"
FT HELIX 216..230
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 266..288
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 296..324
FT /evidence="ECO:0007829|PDB:6S7T"
SQ SEQUENCE 335 AA; 38037 MW; 29B8E9888FDE593E CRC64;
MAARWRFWCV SVTMVVALLI VCDVPSASAQ RKKEMVLSEK VSQLMEWTNK 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
