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Magnesium transporter protein 1 (MagT1) (Implantation-associated protein) (IAP)

 MAGT1_MOUSE             Reviewed;         335 AA.
Q9CQY5; Q3UW45; Q9CWX5; Q9CZT3;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-FEB-2018, entry version 118.
RecName: Full=Magnesium transporter protein 1;
Short=MagT1;
AltName: Full=Implantation-associated protein;
Short=IAP;
Flags: Precursor;
Name=Magt1; Synonyms=Iag2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, AND
TISSUE SPECIFICITY.
PubMed=15804357; DOI=10.1186/1471-2164-6-48;
Goytain A., Quamme G.A.;
"Identification and characterization of a novel mammalian Mg2+
transporter with channel-like properties.";
BMC Genomics 6:48-48(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Cecum, Epididymis, and Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Acts as accessory component of the N-oligosaccharyl
transferase (OST) complex which catalyzes the transfer of a high
mannose oligosaccharide from a lipid-linked oligosaccharide donor
to an asparagine residue within an Asn-X-Ser/Thr consensus motif
in nascent polypeptide chains. Involved in N-glycosylation of
STT3B-dependent substrates. Specifically required for the
glycosylation of a subset of acceptor sites that are near cysteine
residues; in this function seems to act redundantly with TUSC3. In
its oxidized form proposed to form transient mixed disulfides with
a glycoprotein substrate to facilitate access of STT3B to the
unmodified acceptor site. Has also oxidoreductase-independent
functions in the STT3B-containing OST complex possibly involving
substrate recognition. {ECO:0000250|UniProtKB:Q9H0U3}.
-!- FUNCTION: May be involved in Mg(2+) transport in epithelial cells.
{ECO:0000305|PubMed:15804357}.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Accessory component of the STT3B-containing form of the
oligosaccharyltransferase (OST) complex. OST exists in two
different complex forms which contain common core subunits RPN1,
RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as
catalytic subunits, and form-specific accessory subunits. OST can
form stable complexes with the Sec61 complex or with both the
Sec61 and TRAP complexes. The association of TUSC3 or MAGT1 with
the STT3B-containing complex seems to be mutually exclusvice.
{ECO:0000250|UniProtKB:Q9H0U3}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q9H0U3}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q9H0U3}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q9H0U3}. Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9CQY5-1; Sequence=Displayed;
Name=2;
IsoId=Q9CQY5-2; Sequence=VSP_019822;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9CQY5-3; Sequence=VSP_019823;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at high levels in kidney, colon,
heart and liver. Expressed at lower levels in intestine, spleen,
brain and lung. {ECO:0000269|PubMed:15804357}.
-!- INDUCTION: Induced by low magnesium levels.
{ECO:0000269|PubMed:15804357}.
-!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DQ000005; AAY18812.1; -; mRNA.
EMBL; AK010320; BAB26851.1; -; mRNA.
EMBL; AK018623; BAB31313.1; -; mRNA.
EMBL; AK012185; BAB28085.1; -; mRNA.
EMBL; AK136622; BAE23074.1; -; mRNA.
EMBL; AK144696; BAE26020.1; -; mRNA.
EMBL; AK013243; BAB28739.1; -; mRNA.
EMBL; BC003881; AAH03881.1; -; mRNA.
UniGene; Mm.275943; -.
ProteinModelPortal; Q9CQY5; -.
SMR; Q9CQY5; -.
STRING; 10090.ENSMUSP00000033583; -.
PhosphoSitePlus; Q9CQY5; -.
PaxDb; Q9CQY5; -.
PRIDE; Q9CQY5; -.
MGI; MGI:1914325; Magt1.
eggNOG; KOG2603; Eukaryota.
eggNOG; ENOG410XR1F; LUCA.
HOGENOM; HOG000231301; -.
HOVERGEN; HBG002493; -.
InParanoid; Q9CQY5; -.
UniPathway; UPA00378; -.
PRO; PR:Q9CQY5; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MAGT1; -.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:HGNC.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISO:MGI.
GO; GO:0050890; P:cognition; ISO:MGI.
GO; GO:0015693; P:magnesium ion transport; ISO:MGI.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISO:MGI.
InterPro; IPR006844; Mg_transporter-1.
InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR12692:SF2; PTHR12692:SF2; 1.
Pfam; PF04756; OST3_OST6; 1.
SUPFAM; SSF52833; SSF52833; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Magnesium;
Membrane; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 335 Magnesium transporter protein 1.
/FTId=PRO_0000246058.
TOPO_DOM 30 184 Extracellular. {ECO:0000255}.
TRANSMEM 185 205 Helical. {ECO:0000255}.
TOPO_DOM 206 209 Cytoplasmic. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
TOPO_DOM 231 270 Extracellular. {ECO:0000255}.
TRANSMEM 271 291 Helical. {ECO:0000255}.
TOPO_DOM 292 300 Cytoplasmic. {ECO:0000255}.
TRANSMEM 301 321 Helical. {ECO:0000255}.
TOPO_DOM 322 335 Extracellular. {ECO:0000255}.
DOMAIN 47 175 Thioredoxin.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 87 90 Redox-active. {ECO:0000250}.
VAR_SEQ 301 335 MMCIAGIGLVVLFFSWMLSIFRSKYHGYPYSFLMS -> NN
FCQA (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_019822.
VAR_SEQ 301 335 MMCIAGIGLVVLFFSWMLSIFRSKYHGYPYSFLMS -> TK
SHVTMVQFCL (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_019823.
CONFLICT 249 249 P -> T (in Ref. 2; BAE23074).
{ECO:0000305}.
CONFLICT 307 307 I -> N (in Ref. 1; AAY18812 and 2;
BAB28085). {ECO:0000305}.
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


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