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S41A1_MOUSE
ID   S41A1_MOUSE             Reviewed;         512 AA.
AC   Q8BJA2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Solute carrier family 41 member 1;
GN   Name=Slc41a1 {ECO:0000303|PubMed:33153064, ECO:0000312|MGI:MGI:2444823};
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 [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   [3]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15713785; DOI=10.1152/physiolgenomics.00261.2004;
RA   Goytain A., Quamme G.A.;
RT   "Functional characterization of human SLC41A1, a Mg2+ transporter with
RT   similarity to prokaryotic MgtE Mg2+ transporters.";
RL   Physiol. Genomics 21:337-342(2005).
RN   [4]
RP   FUNCTION.
RX   PubMed=33153064; DOI=10.3390/ijms21218221;
RA   Tatarkova Z., de Baaij J.H.F., Grendar M., Aschenbach J.R., Racay P.,
RA   Bos C., Sponder G., Hoenderop J.G.J., Roentgen M.,
RA   Turcanova Koprusakova M., Kolisek M.;
RT   "Dietary Mg2+ Intake and the Na+/Mg2+ Exchanger SLC41A1 Influence
RT   Components of Mitochondrial Energetics in Murine Cardiomyocytes.";
RL   Int. J. Mol. Sci. 21:0-0(2020).
CC   -!- FUNCTION: Na(+)/Mg(2+) ion exchanger that acts as a predominant Mg(2+)
CC       efflux system at the plasma membrane. 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. Generates circadian cellular Mg(2+) fluxes that feed
CC       back to regulate clock-controlled gene expression and metabolism and
CC       facilitate higher energetic demands during the day (By similarity). Has
CC       a role in regulating the activity of ATP-dependent enzymes, including
CC       those operating in Krebs cycle and the electron transport chain
CC       (PubMed:33153064). {ECO:0000250|UniProtKB:Q8IVJ1,
CC       ECO:0000269|PubMed:33153064}.
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:0000250|UniProtKB:Q8IVJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66617;
CC         Evidence={ECO:0000250|UniProtKB:Q8IVJ1};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IVJ1};
CC       Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q8IVJ1}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, kidney, liver and colon.
CC       {ECO:0000269|PubMed:15713785}.
CC   -!- INDUCTION: Up-regulated in heart, brain, kidney and down-regulated in
CC       liver by low Mg(2+) diet. {ECO:0000269|PubMed:15713785}.
CC   -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q8IVJ1}.
CC   -!- SIMILARITY: Belongs to the SLC41A transporter family. {ECO:0000305}.
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DR   EMBL; AK089802; BAC40965.1; -; mRNA.
DR   EMBL; BC096596; AAH96596.1; -; mRNA.
DR   EMBL; BC116280; AAI16281.1; -; mRNA.
DR   EMBL; BC116281; AAI16282.1; -; mRNA.
DR   CCDS; CCDS15275.1; -.
DR   RefSeq; NP_776290.1; NM_173865.3.
DR   AlphaFoldDB; Q8BJA2; -.
DR   STRING; 10090.ENSMUSP00000083747; -.
DR   iPTMnet; Q8BJA2; -.
DR   PhosphoSitePlus; Q8BJA2; -.
DR   EPD; Q8BJA2; -.
DR   MaxQB; Q8BJA2; -.
DR   PaxDb; Q8BJA2; -.
DR   PeptideAtlas; Q8BJA2; -.
DR   PRIDE; Q8BJA2; -.
DR   ProteomicsDB; 256903; -.
DR   Antibodypedia; 2794; 43 antibodies from 15 providers.
DR   DNASU; 98396; -.
DR   Ensembl; ENSMUST00000086559; ENSMUSP00000083747; ENSMUSG00000013275.
DR   GeneID; 98396; -.
DR   KEGG; mmu:98396; -.
DR   UCSC; uc007cnu.3; mouse.
DR   CTD; 254428; -.
DR   MGI; MGI:2444823; Slc41a1.
DR   VEuPathDB; HostDB:ENSMUSG00000013275; -.
DR   eggNOG; KOG3788; Eukaryota.
DR   GeneTree; ENSGT00950000183042; -.
DR   HOGENOM; CLU_018207_3_1_1; -.
DR   InParanoid; Q8BJA2; -.
DR   OMA; YLERDDW; -.
DR   OrthoDB; 1059294at2759; -.
DR   PhylomeDB; Q8BJA2; -.
DR   TreeFam; TF313647; -.
DR   Reactome; R-MMU-425410; Metal ion SLC transporters.
DR   BioGRID-ORCS; 98396; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Slc41a1; mouse.
DR   PRO; PR:Q8BJA2; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8BJA2; protein.
DR   Bgee; ENSMUSG00000013275; Expressed in extra-ocular muscle and 262 other tissues.
DR   Genevisible; Q8BJA2; MM.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0061768; F:magnesium:sodium antiporter activity; ISS:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0010961; P:cellular magnesium ion homeostasis; ISO:MGI.
DR   GO; GO:0071286; P:cellular response to magnesium ion; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903830; P:magnesium ion transmembrane transport; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0015693; P:magnesium ion transport; ISO:MGI.
DR   GO; GO:0030001; P:metal ion transport; IDA:ParkinsonsUK-UCL.
DR   Gene3D; 1.10.357.20; -; 2.
DR   InterPro; IPR006667; SLC41_membr_dom.
DR   InterPro; IPR036739; SLC41_membr_dom_sf.
DR   InterPro; IPR045349; SLC41A1-3.
DR   PANTHER; PTHR16228; PTHR16228; 1.
DR   Pfam; PF01769; MgtE; 2.
DR   SUPFAM; SSF161093; SSF161093; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Ion transport; Magnesium; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..512
FT                   /note="Solute carrier family 41 member 1"
FT                   /id="PRO_0000295112"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        483..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..90
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"
SQ   SEQUENCE   512 AA;  54928 MW;  052DFE6B48AC8F7B CRC64;
     MSSKPEPKDI HQPNGTGPTP SPCSSDGPGR EPLAGTSEFL GPDGVEVVVI ESRANAKGIR
     EEDALLENGS QSNESDDVST DRGPAPPSPL KETSFSIGLQ VLFPFLLAGF GTVAAGMVLD
     IVQHWEVFQK VTEVFILVPA LLGLKGNLEM TLASRLSTAA NIGQMDTPKE LWRMITGNMA
     LIQVQATVVG FLASIAAVVF GWIPDGHFSI PHAFLLCASS VATAFIASLV LGMIMIGVII
     GSRKIGINPD NVATPIAASL GDLITLALLS GISWGLYLEL KHWRYIYPLV CAFFVALLPV
     WVVLARRSPA TREVLYSGWE PVIIAMAISS VGGLILDKTV SDPNFAGMAV FTPVINGVGG
     NLVAVQASRI STFLHMNGMP GENSEPTPRR CPSPCTTFFS PDVNSRSARV LFLLVVPGHL
     VFLYTISCMQ GGHTTLTLIF IIFYMTAALL QVLILLYIAD WMVHWMWGRG LDPDNFSIPY
     LTALGDLLGT GLLALSFHVL WLIGDRDTDV GD
 
 
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