ID   S41A1_HUMAN             Reviewed;         513 AA.
AC   Q8IVJ1; Q63HJ4; Q658Z5; Q659A4; Q6MZK2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Solute carrier family 41 member 1;
GN   Name=SLC41A1 {ECO:0000303|PubMed:22031603,
GN   ECO:0000312|HGNC:HGNC:19429};
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], AND TISSUE SPECIFICITY.
RX   PubMed=12810078; DOI=10.1016/s0006-291x(03)01030-1;
RA   Wabakken T., Rian E., Kveine M., Aasheim H.-C.;
RT   "The human solute carrier SLC41A1 belongs to a novel eukaryotic subfamily
RT   with homology to prokaryotic MgtE Mg2+ transporters.";
RL   Biochem. Biophys. Res. Commun. 306:718-724(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Endometrial tumor, Skeletal muscle, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=18367447; DOI=10.1074/jbc.m707276200;
RA   Kolisek M., Launay P., Beck A., Sponder G., Serafini N., Brenkus M.,
RA   Froschauer E.M., Martens H., Fleig A., Schweigel M.;
RT   "SLC41A1 is a novel mammalian Mg2+ carrier.";
RL   J. Biol. Chem. 283:16235-16247(2008).
RN   [4]
RP   FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND PHOSPHORYLATION.
RX   PubMed=22031603; DOI=10.1152/ajpcell.00289.2011;
RA   Kolisek M., Nestler A., Vormann J., Schweigel-Roentgen M.;
RT   "Human gene SLC41A1 encodes for the Na+/Mg2+ exchanger.";
RL   Am. J. Physiol. 302:C318-C326(2012).
RN   [5]
RP   FUNCTION.
RX   PubMed=27074515; DOI=10.1038/nature17407;
RA   Feeney K.A., Hansen L.L., Putker M., Olivares-Yanez C., Day J., Eades L.J.,
RA   Larrondo L.F., Hoyle N.P., O'Neill J.S., van Ooijen G.;
RT   "Daily magnesium fluxes regulate cellular timekeeping and energy balance.";
RL   Nature 532:375-379(2016).
RN   [6]
RP   VARIANT NPHPL2 VAL-233, INVOLVEMENT IN NPHPL2, CHARACTERIZATION OF VARIANT
RP   NPHPL2 VAL-233, SUBCELLULAR LOCATION, FUNCTION, TRANSPORTER ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=23661805; DOI=10.1681/asn.2012101034;
RA   Hurd T.W., Otto E.A., Mishima E., Gee H.Y., Inoue H., Inazu M., Yamada H.,
RA   Halbritter J., Seki G., Konishi M., Zhou W., Yamane T., Murakami S.,
RA   Caridi G., Ghiggeri G., Abe T., Hildebrandt F.;
RT   "Mutation of the Mg2+ transporter SLC41A1 results in a nephronophthisis-
RT   like phenotype.";
RL   J. Am. Soc. Nephrol. 24:967-977(2013).
RN   [7]
RP   VARIANT VAL-350, CHARACTERIZATION OF VARIANT VAL-350, FUNCTION, TRANSPORTER
RP   ACTIVITY, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX   PubMed=23976986; DOI=10.1371/journal.pone.0071096;
RA   Kolisek M., Sponder G., Mastrototaro L., Smorodchenko A., Launay P.,
RA   Vormann J., Schweigel-Roentgen M.;
RT   "Substitution p.A350V in Na+/Mg2+ exchanger SLC41A1, potentially associated
RT   with Parkinson's disease, is a gain-of-function mutation.";
RL   PLoS ONE 8:e71096-e71096(2013).
CC   -!- FUNCTION: Na(+)/Mg(2+) ion exchanger that acts as a predominant Mg(2+)
CC       efflux system at the plasma membrane (PubMed:22031603, PubMed:23661805,
CC       PubMed:18367447, PubMed:23976986). Transporter activity is driven by
CC       the inwardly directed electrochemical gradient for Na(+) ions, thus
CC       directly depends on the extracellular Na(+) ion concentration set by
CC       Na(+)/K(+) pump (PubMed:22031603, PubMed:23661805). Generates circadian
CC       cellular Mg(2+) fluxes that feed back to regulate clock-controlled gene
CC       expression and metabolism and facilitate higher energetic demands
CC       during the day (PubMed:27074515). Has a role in regulating the activity
CC       of ATP-dependent enzymes, including those operating in Krebs cycle and
CC       the electron transport chain (By similarity).
CC       {ECO:0000250|UniProtKB:Q8BJA2, ECO:0000269|PubMed:18367447,
CC       ECO:0000269|PubMed:22031603, ECO:0000269|PubMed:23661805,
CC       ECO:0000269|PubMed:23976986, ECO:0000269|PubMed:27074515}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Mg(2+)(in) + 2 Na(+)(out) = Mg(2+)(out) + 2 Na(+)(in);
CC         Xref=Rhea:RHEA:66616, ChEBI:CHEBI:18420, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000269|PubMed:18367447, ECO:0000269|PubMed:22031603,
CC         ECO:0000269|PubMed:23661805, ECO:0000269|PubMed:23976986};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66617;
CC         Evidence={ECO:0000305|PubMed:22031603};
CC   -!- ACTIVITY REGULATION: The exchange activity is regulated by
CC       phosphorylation in a cyclic AMP signaling-dependent way
CC       (PubMed:22031603, PubMed:23661805). Temperature-sensitive, reduction or
CC       elevation of the temperature significantly decreases or increases its
CC       activity respectively (PubMed:18367447). {ECO:0000269|PubMed:18367447,
CC       ECO:0000269|PubMed:22031603, ECO:0000269|PubMed:23976986}.
CC   -!- INTERACTION:
CC       Q8IVJ1; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-12266234, EBI-19125216;
CC       Q8IVJ1; Q13520: AQP6; NbExp=3; IntAct=EBI-12266234, EBI-13059134;
CC       Q8IVJ1; P30518: AVPR2; NbExp=3; IntAct=EBI-12266234, EBI-11675746;
CC       Q8IVJ1; P11912: CD79A; NbExp=3; IntAct=EBI-12266234, EBI-7797864;
CC       Q8IVJ1; A0A024R644: CLN5; NbExp=3; IntAct=EBI-12266234, EBI-12838990;
CC       Q8IVJ1; A1L3X0: ELOVL7; NbExp=3; IntAct=EBI-12266234, EBI-10285373;
CC       Q8IVJ1; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12266234, EBI-781551;
CC       Q8IVJ1; O15552: FFAR2; NbExp=3; IntAct=EBI-12266234, EBI-2833872;
CC       Q8IVJ1; O14843: FFAR3; NbExp=3; IntAct=EBI-12266234, EBI-17762181;
CC       Q8IVJ1; P36382: GJA5; NbExp=3; IntAct=EBI-12266234, EBI-750433;
CC       Q8IVJ1; O95377: GJB5; NbExp=3; IntAct=EBI-12266234, EBI-3909454;
CC       Q8IVJ1; Q96P66: GPR101; NbExp=3; IntAct=EBI-12266234, EBI-17935713;
CC       Q8IVJ1; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12266234, EBI-13345167;
CC       Q8IVJ1; O15529: GPR42; NbExp=3; IntAct=EBI-12266234, EBI-18076404;
CC       Q8IVJ1; Q9BZJ8: GPR61; NbExp=3; IntAct=EBI-12266234, EBI-12808020;
CC       Q8IVJ1; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-12266234, EBI-749265;
CC       Q8IVJ1; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-12266234, EBI-2820517;
CC       Q8IVJ1; P35372-10: OPRM1; NbExp=3; IntAct=EBI-12266234, EBI-12807478;
CC       Q8IVJ1; O15127: SCAMP2; NbExp=3; IntAct=EBI-12266234, EBI-712703;
CC       Q8IVJ1; Q14973: SLC10A1; NbExp=3; IntAct=EBI-12266234, EBI-3923031;
CC       Q8IVJ1; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12266234, EBI-18159983;
CC       Q8IVJ1; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-12266234, EBI-12808018;
CC       Q8IVJ1; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12266234, EBI-17280858;
CC       Q8IVJ1; Q9H7V2: SYNDIG1; NbExp=3; IntAct=EBI-12266234, EBI-726331;
CC       Q8IVJ1; Q5VXT5-2: SYPL2; NbExp=3; IntAct=EBI-12266234, EBI-18196631;
CC       Q8IVJ1; Q96RI9: TAAR9; NbExp=3; IntAct=EBI-12266234, EBI-12908048;
CC       Q8IVJ1; Q0VAB0: TBXA2R; NbExp=3; IntAct=EBI-12266234, EBI-18271435;
CC       Q8IVJ1; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-12266234, EBI-12947623;
CC       Q8IVJ1; Q96Q45-2: TMEM237; NbExp=5; IntAct=EBI-12266234, EBI-10982110;
CC       Q8IVJ1; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-12266234, EBI-10314986;
CC       Q8IVJ1; P34981: TRHR; NbExp=3; IntAct=EBI-12266234, EBI-18055230;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18367447,
CC       ECO:0000269|PubMed:23976986}; Multi-pass membrane protein
CC       {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:23661805};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highest expression levels in heart and testis,
CC       slightly less in skeletal muscles, prostate, adrenal gland and thyroid,
CC       and weakest in the hematopoietic tissues bones marrow, lymph node,
CC       thymus and spleen. In the kidney, it is expressed in the distal
CC       convoluted tubules, macula densa, and thick ascending limb tubular
CC       segments of the nephrons (PubMed:23661805).
CC       {ECO:0000269|PubMed:12810078, ECO:0000269|PubMed:23661805}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:22031603}.
CC   -!- DISEASE: Nephronophthisis-like nephropathy 2 (NPHPL2) [MIM:619468]: A
CC       disorder with features of nephronophthisis, a cystic kidney disease
CC       leading to end-stage renal failure. Nephronophthisis is histologically
CC       characterized by modifications of the tubules with thickening of the
CC       basement membrane, interstitial fibrosis and, in the advanced stages,
CC       medullary cysts. Typical clinical manifestation are chronic renal
CC       failure, anemia, polyuria, polydipsia, isosthenuria, and growth
CC       retardation. Associations with extrarenal symptoms are frequent. NPHPL2
CC       is an autosomal recessive form characterized by onset of progressive
CC       renal insufficiency in the first decades of life.
CC       {ECO:0000269|PubMed:23661805}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the SLC41A transporter family. {ECO:0000305}.
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DR   EMBL; AJ514402; CAD58404.1; -; mRNA.
DR   EMBL; AL831974; CAH56217.1; -; mRNA.
DR   EMBL; AL832001; CAH56211.1; -; mRNA.
DR   EMBL; AL832362; CAH56213.1; -; mRNA.
DR   EMBL; BX641054; CAE46028.1; -; mRNA.
DR   EMBL; BX648979; CAH56135.1; -; mRNA.
DR   CCDS; CCDS30988.1; -.
DR   RefSeq; NP_776253.3; NM_173854.5.
DR   RefSeq; XP_005245126.1; XM_005245069.2.
DR   AlphaFoldDB; Q8IVJ1; -.
DR   BioGRID; 129036; 38.
DR   IntAct; Q8IVJ1; 32.
DR   STRING; 9606.ENSP00000356105; -.
DR   DrugBank; DB14513; Magnesium.
DR   TCDB; 1.A.26.2.1; the mg(2+) transporter-e (mgte) family.
DR   iPTMnet; Q8IVJ1; -.
DR   PhosphoSitePlus; Q8IVJ1; -.
DR   SwissPalm; Q8IVJ1; -.
DR   BioMuta; SLC41A1; -.
DR   DMDM; 152112285; -.
DR   EPD; Q8IVJ1; -.
DR   jPOST; Q8IVJ1; -.
DR   MassIVE; Q8IVJ1; -.
DR   MaxQB; Q8IVJ1; -.
DR   PaxDb; 9606-ENSP00000356105; -.
DR   PeptideAtlas; Q8IVJ1; -.
DR   ProteomicsDB; 70715; -.
DR   Antibodypedia; 2794; 45 antibodies from 15 providers.
DR   DNASU; 254428; -.
DR   Ensembl; ENST00000367137.4; ENSP00000356105.3; ENSG00000133065.11.
DR   GeneID; 254428; -.
DR   KEGG; hsa:254428; -.
DR   MANE-Select; ENST00000367137.4; ENSP00000356105.3; NM_173854.6; NP_776253.3.
DR   UCSC; uc001hdh.2; human.
DR   AGR; HGNC:19429; -.
DR   CTD; 254428; -.
DR   DisGeNET; 254428; -.
DR   GeneCards; SLC41A1; -.
DR   HGNC; HGNC:19429; SLC41A1.
DR   HPA; ENSG00000133065; Tissue enhanced (heart muscle, pancreas, tongue).
DR   MalaCards; SLC41A1; -.
DR   MIM; 610801; gene.
DR   MIM; 619468; phenotype.
DR   neXtProt; NX_Q8IVJ1; -.
DR   OpenTargets; ENSG00000133065; -.
DR   PharmGKB; PA134889327; -.
DR   VEuPathDB; HostDB:ENSG00000133065; -.
DR   eggNOG; KOG3788; Eukaryota.
DR   GeneTree; ENSGT00950000183042; -.
DR   HOGENOM; CLU_018207_3_1_1; -.
DR   InParanoid; Q8IVJ1; -.
DR   OMA; WDPDNVT; -.
DR   OrthoDB; 5124745at2759; -.
DR   PhylomeDB; Q8IVJ1; -.
DR   TreeFam; TF313647; -.
DR   PathwayCommons; Q8IVJ1; -.
DR   Reactome; R-HSA-425410; Metal ion SLC transporters.
DR   SignaLink; Q8IVJ1; -.
DR   BioGRID-ORCS; 254428; 20 hits in 1160 CRISPR screens.
DR   ChiTaRS; SLC41A1; human.
DR   GenomeRNAi; 254428; -.
DR   Pharos; Q8IVJ1; Tbio.
DR   PRO; PR:Q8IVJ1; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q8IVJ1; Protein.
DR   Bgee; ENSG00000133065; Expressed in left ventricle myocardium and 170 other cell types or tissues.
DR   ExpressionAtlas; Q8IVJ1; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0032991; C:protein-containing complex; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0022890; F:inorganic cation transmembrane transporter activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0061768; F:magnesium:sodium antiporter activity; IMP:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0071286; P:cellular response to magnesium ion; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0010961; P:intracellular magnesium ion homeostasis; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903830; P:magnesium ion transmembrane transport; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0015693; P:magnesium ion transport; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0030001; P:metal ion transport; ISS:ParkinsonsUK-UCL.
DR   Gene3D; 1.10.357.20; SLC41 divalent cation transporters, integral membrane domain; 2.
DR   InterPro; IPR006667; SLC41_membr_dom.
DR   InterPro; IPR036739; SLC41_membr_dom_sf.
DR   InterPro; IPR045349; SLC41A1-3.
DR   PANTHER; PTHR16228; DIVALENT CATION TRANSPORTER SOLUTE CARRIER FAMILY 41; 1.
DR   PANTHER; PTHR16228:SF23; SOLUTE CARRIER FAMILY 41 MEMBER 1; 1.
DR   Pfam; PF01769; MgtE; 2.
DR   SUPFAM; SSF161093; MgtE membrane domain-like; 2.
DR   Genevisible; Q8IVJ1; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Disease variant; Ion transport; Magnesium; Membrane;
KW   Nephronophthisis; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..513
FT                   /note="Solute carrier family 41 member 1"
FT                   /id="PRO_0000295111"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         233
FT                   /note="G -> V (in NPHPL2; results in exon 6 skipping;
FT                   results in loss of magnesium ion transmembrane transporter
FT                   activity; does not affect localization to basolateral cell
FT                   membrane)"
FT                   /evidence="ECO:0000269|PubMed:23661805"
FT                   /id="VAR_086146"
FT   VARIANT         350
FT                   /note="A -> V (increased magnesium ion transmembrane
FT                   transporter activity; no effect on plasma membrane
FT                   localization; dbSNP:rs1305279636)"
FT                   /evidence="ECO:0000269|PubMed:23976986"
FT                   /id="VAR_086248"
FT   CONFLICT        3
FT                   /note="S -> P (in Ref. 2; CAH56135)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="I -> T (in Ref. 2; CAH56213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="I -> V (in Ref. 2; CAH56213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="G -> D (in Ref. 2; CAH56135)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="L -> P (in Ref. 2; CAH56135)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272..275
FT                   /note="GISW -> ASAG (in Ref. 1; CAD58404)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365
FT                   /note="A -> T (in Ref. 2; CAE46028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="V -> A (in Ref. 1; CAD58404)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464
FT                   /note="V -> A (in Ref. 2; CAH56135)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        511
FT                   /note="V -> A (in Ref. 2; CAH56135)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   513 AA;  54901 MW;  2B6676F9C3AF6136 CRC64;
     MSSKPEPKDV HQLNGTGPSA SPCSSDGPGR EPLAGTSEFL GPDGAGVEVV IESRANAKGV
     REEDALLENG SQSNESDDVS TDRGPAPPSP LKETSFSIGL QVLFPFLLAG FGTVAAGMVL
     DIVQHWEVFQ KVTEVFILVP ALLGLKGNLE MTLASRLSTA ANIGHMDTPK ELWRMITGNM
     ALIQVQATVV GFLASIAAVV FGWIPDGHFS IPHAFLLCAS SVATAFIASL VLGMIMIGVI
     IGSRKIGINP DNVATPIAAS LGDLITLALL SGISWGLYLE LNHWRYIYPL VCAFFVALLP
     VWVVLARRSP ATREVLYSGW EPVIIAMAIS SVGGLILDKT VSDPNFAGMA VFTPVINGVG
     GNLVAVQASR ISTFLHMNGM PGENSEQAPR RCPSPCTTFF SPDVNSRSAR VLFLLVVPGH
     LVFLYTISCM QGGHTTLTLI FIIFYMTAAL LQVLILLYIA DWMVHWMWGR GLDPDNFSIP
     YLTALGDLLG TGLLALSFHV LWLIGDRDTD VGD
//