NIPA2_MOUSE
ID NIPA2_MOUSE Reviewed; 359 AA.
AC Q9JJC8; Q3U3I0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Magnesium transporter NIPA2;
DE AltName: Full=Non-imprinted in Prader-Willi/Angelman syndrome region protein 2 homolog;
GN Name=Nipa2; ORFNames=MNCb-2146;
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], AND TISSUE SPECIFICITY.
RX PubMed=14508708; DOI=10.1086/378816;
RA Chai J.-H., Locke D.P., Greally J.M., Knoll J.H.M., Ohta T., Dunai J.,
RA Yavor A., Eichler E.E., Nicholls R.D.;
RT "Identification of four highly conserved genes between breakpoint hotspots
RT BP1 and BP2 of the Prader-Willi/Angelman syndromes deletion region that
RT have undergone evolutionary transposition mediated by flanking duplicons.";
RL Am. J. Hum. Genet. 73:898-925(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18667602; DOI=10.1152/ajpcell.00091.2008;
RA Goytain A., Hines R.M., Quamme G.A.;
RT "Functional characterization of NIPA2, a selective Mg2+ transporter.";
RL Am. J. Physiol. 295:C944-C953(2008).
CC -!- FUNCTION: Acts as a selective Mg(2+) transporter.
CC {ECO:0000269|PubMed:18667602}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.31 mM for magnesium ions {ECO:0000269|PubMed:18667602};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Early endosome {ECO:0000269|PubMed:18667602}.
CC Note=Recruited to the cell membrane in response to low extracellular
CC magnesium.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the
CC kidney. {ECO:0000269|PubMed:14508708, ECO:0000269|PubMed:18667602}.
CC -!- INDUCTION: Up-regulated by low magnesium ion levels.
CC {ECO:0000269|PubMed:18667602}.
CC -!- SIMILARITY: Belongs to the NIPA family. {ECO:0000305}.
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DR EMBL; BK001121; DAA01178.1; -; mRNA.
DR EMBL; AB041581; BAA95065.1; -; mRNA.
DR EMBL; AK028734; BAC26089.1; -; mRNA.
DR EMBL; AK041427; BAC30943.1; -; mRNA.
DR EMBL; AK076051; BAC36149.1; -; mRNA.
DR EMBL; AK154755; BAE32806.1; -; mRNA.
DR EMBL; BC038499; AAH38499.1; -; mRNA.
DR CCDS; CCDS21316.1; -.
DR RefSeq; NP_001243059.1; NM_001256130.1.
DR RefSeq; NP_001243060.1; NM_001256131.1.
DR RefSeq; NP_001243061.1; NM_001256132.1.
DR RefSeq; NP_001243062.1; NM_001256133.1.
DR RefSeq; NP_076136.2; NM_023647.6.
DR RefSeq; XP_006541387.1; XM_006541324.3.
DR AlphaFoldDB; Q9JJC8; -.
DR IntAct; Q9JJC8; 1.
DR MINT; Q9JJC8; -.
DR STRING; 10090.ENSMUSP00000114020; -.
DR iPTMnet; Q9JJC8; -.
DR PhosphoSitePlus; Q9JJC8; -.
DR MaxQB; Q9JJC8; -.
DR PaxDb; Q9JJC8; -.
DR PRIDE; Q9JJC8; -.
DR ProteomicsDB; 252966; -.
DR Antibodypedia; 22214; 41 antibodies from 16 providers.
DR DNASU; 93790; -.
DR Ensembl; ENSMUST00000032635; ENSMUSP00000032635; ENSMUSG00000030452.
DR Ensembl; ENSMUST00000117812; ENSMUSP00000113727; ENSMUSG00000030452.
DR Ensembl; ENSMUST00000119041; ENSMUSP00000112394; ENSMUSG00000030452.
DR Ensembl; ENSMUST00000119201; ENSMUSP00000114020; ENSMUSG00000030452.
DR GeneID; 93790; -.
DR KEGG; mmu:93790; -.
DR UCSC; uc009hdp.2; mouse.
DR CTD; 81614; -.
DR MGI; MGI:1913918; Nipa2.
DR VEuPathDB; HostDB:ENSMUSG00000030452; -.
DR eggNOG; KOG2922; Eukaryota.
DR GeneTree; ENSGT00940000155651; -.
DR HOGENOM; CLU_012349_1_1_1; -.
DR InParanoid; Q9JJC8; -.
DR OMA; IWWAGMI; -.
DR OrthoDB; 754939at2759; -.
DR PhylomeDB; Q9JJC8; -.
DR TreeFam; TF313214; -.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR BioGRID-ORCS; 93790; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Nipa2; mouse.
DR PRO; PR:Q9JJC8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JJC8; protein.
DR Bgee; ENSMUSG00000030452; Expressed in epithelium of small intestine and 241 other tissues.
DR ExpressionAtlas; Q9JJC8; baseline and differential.
DR Genevisible; Q9JJC8; MM.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015693; P:magnesium ion transport; IDA:UniProtKB.
DR InterPro; IPR008521; Mg_trans_NIPA.
DR PANTHER; PTHR12570; PTHR12570; 1.
DR Pfam; PF05653; Mg_trans_NIPA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endosome; Ion transport; Magnesium; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..359
FT /note="Magnesium transporter NIPA2"
FT /id="PRO_0000191744"
FT TOPO_DOM 1..9
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 359 AA; 39091 MW; CAFFAA474D414253 CRC64;
MSLGRGKYDF YIGLGLAMTS SIFIGGSFIL KKKGLLRLAR KGSMRAGQGG HAYLKEWLWW
AGLLSMGAGE VANFAAYAFA PATLVTPLGA LSVLVSAILS SYFLNERLNL HGKIGCLLSI
LGSTVMVIHA PKEEEIETLN EMSHKLGDPG FVVFATFVVI VALIFIFVVG PRHGQTNILV
YITICSVIGA FSVSCVKGLG IAIKELLAGK PVLQHPLAWI LLFSLVVCVS TQINYLNRAL
DIFNTSIVTP IYYVFFTTSV LTCSAILFKE WQDMPVDDVI GTLSGFFTII VGIFLLHAFK
DVSFSLASLP VSFRKDEKAM NGNLSSMYEV LNNNEDDLPC GIEHTGENIS RRNGNLPSF
