NIPA1_MOUSE
ID NIPA1_MOUSE Reviewed; 323 AA.
AC Q8BHK1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Magnesium transporter NIPA1;
DE AltName: Full=Non-imprinted in Prader-Willi/Angelman syndrome region protein 1 homolog;
GN Name=Nipa1; Synonyms=Spg6;
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.
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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=Adipose tissue;
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].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF THR-39 AND GLY-100.
RX PubMed=17166836; DOI=10.1074/jbc.m610314200;
RA Goytain A., Hines R.M., El-Husseini A., Quamme G.A.;
RT "NIPA1(SPG6), the basis for autosomal dominant form of hereditary spastic
RT paraplegia, encodes a functional Mg2+ transporter.";
RL J. Biol. Chem. 282:8060-8068(2007).
CC -!- FUNCTION: Acts as a Mg(2+) transporter. Can also transport other
CC divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but
CC to a much less extent than Mg(2+). {ECO:0000269|PubMed:17166836}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.69 mM for magnesium ions {ECO:0000269|PubMed:17166836};
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Early endosome {ECO:0000269|PubMed:17166836}.
CC Note=Recruited to the cell membrane in response to low extracellular
CC magnesium.
CC -!- TISSUE SPECIFICITY: Widely expressed. Predominantly expressed in
CC neuronal tissues. Brain, heart, kidney, liver and colon (at protein
CC level). {ECO:0000269|PubMed:14508708, ECO:0000269|PubMed:17166836}.
CC -!- INDUCTION: Up-regulated by low magnesium ion levels.
CC {ECO:0000269|PubMed:17166836}.
CC -!- SIMILARITY: Belongs to the NIPA family. {ECO:0000305}.
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DR EMBL; AY098645; AAM34534.1; -; mRNA.
DR EMBL; AK046619; BAC32809.1; -; mRNA.
DR EMBL; BC055828; AAH55828.1; -; mRNA.
DR CCDS; CCDS21317.1; -.
DR RefSeq; NP_705806.1; NM_153578.2.
DR AlphaFoldDB; Q8BHK1; -.
DR STRING; 10090.ENSMUSP00000053871; -.
DR PhosphoSitePlus; Q8BHK1; -.
DR MaxQB; Q8BHK1; -.
DR PaxDb; Q8BHK1; -.
DR PRIDE; Q8BHK1; -.
DR ProteomicsDB; 252896; -.
DR Antibodypedia; 8965; 30 antibodies from 13 providers.
DR DNASU; 233280; -.
DR Ensembl; ENSMUST00000052204; ENSMUSP00000053871; ENSMUSG00000047037.
DR GeneID; 233280; -.
DR KEGG; mmu:233280; -.
DR UCSC; uc009hdu.1; mouse.
DR CTD; 123606; -.
DR MGI; MGI:2442058; Nipa1.
DR VEuPathDB; HostDB:ENSMUSG00000047037; -.
DR eggNOG; KOG2922; Eukaryota.
DR GeneTree; ENSGT00940000159067; -.
DR HOGENOM; CLU_012349_1_1_1; -.
DR InParanoid; Q8BHK1; -.
DR OMA; YLTDVVW; -.
DR OrthoDB; 754939at2759; -.
DR PhylomeDB; Q8BHK1; -.
DR TreeFam; TF313214; -.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR SABIO-RK; Q8BHK1; -.
DR BioGRID-ORCS; 233280; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Nipa1; mouse.
DR PRO; PR:Q8BHK1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BHK1; protein.
DR Bgee; ENSMUSG00000047037; Expressed in cerebellar nuclear complex and 208 other tissues.
DR Genevisible; Q8BHK1; 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..323
FT /note="Magnesium transporter NIPA1"
FT /id="PRO_0000191742"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 39
FT /note="T->R: Failure to correctly traffic to the cell
FT membrane and diminished Mg(2+) transport."
FT /evidence="ECO:0000269|PubMed:17166836"
FT MUTAGEN 100
FT /note="G->R: Failure to correctly traffic to the cell
FT membrane and complete loss of Mg(2+) transport."
FT /evidence="ECO:0000269|PubMed:17166836"
SQ SEQUENCE 323 AA; 34105 MW; 0F5C2A35559A27E1 CRC64;
MGTAAAAAAA GEGARGPSPA AVSLGLGVAV VSSLVNGSTF VLQKKGIVRA KRRGTSYLTD
IVWWAGTIAM AVGQIGNFLA YTAVPTVLVT PLGALGVPFG SILASYLLKE KLNILGKLGC
LLSCAGSVVL IIHSPKSESV TTQAELEEKL TNPVFVGYLC IVLLMLLLLI FWIAPAHGPT
NIMVYISICS LLGSFTVPST KGIGLAAQDI LHNNPSSQRA LCLCLVLLAV LGCSIIVQFR
YINKALECFD SSVFGAIYYV VFTTLVLLAS AILFREWSNV GLVDFLGMAC GFTTVSVGIV
LIQVFKEFNF NLGEMNKSNM KTD
