ID   ZNT1_MOUSE              Reviewed;         503 AA.
AC   Q60738;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 176.
DE   RecName: Full=Proton-coupled zinc antiporter SLC30A1 {ECO:0000305|PubMed:15451416};
DE   AltName: Full=Solute carrier family 30 member 1 {ECO:0000312|MGI:MGI:1345281};
DE   AltName: Full=Zinc transporter 1 {ECO:0000303|PubMed:15452870};
DE            Short=ZnT-1 {ECO:0000303|PubMed:15451416};
GN   Name=Slc30a1 {ECO:0000312|MGI:MGI:1345281};
GN   Synonyms=Znt1 {ECO:0000303|PubMed:15452870};
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 [GENOMIC DNA].
RC   TISSUE=Brain;
RX   PubMed=7882967; DOI=10.1002/j.1460-2075.1995.tb07042.x;
RA   Palmiter R.D., Findley S.D.;
RT   "Cloning and functional characterization of a mammalian zinc transporter
RT   that confers resistance to zinc.";
RL   EMBO J. 14:639-649(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
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   FUNCTION.
RX   PubMed=15451416; DOI=10.1016/j.bbrc.2004.08.211;
RA   Segal D., Ohana E., Besser L., Hershfinkel M., Moran A., Sekler I.;
RT   "A role for ZnT-1 in regulating cellular cation influx.";
RL   Biochem. Biophys. Res. Commun. 323:1145-1150(2004).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15452870; DOI=10.1002/gene.20067;
RA   Andrews G.K., Wang H., Dey S.K., Palmiter R.D.;
RT   "Mouse zinc transporter 1 gene provides an essential function during early
RT   embryonic development.";
RL   Genesis 40:74-81(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Zinc ion:proton antiporter that could function at the plasma
CC       membrane mediating zinc efflux from cells against its electrochemical
CC       gradient protecting them from intracellular zinc accumulation and
CC       toxicity (Probable). Alternatively, could prevent the transport to the
CC       plasma membrane of CACNB2, the L-type calcium channels regulatory
CC       subunit, through a yet to be defined mechanism. By modulating the
CC       expression of these channels at the plasma membrane, could prevent
CC       calcium and zinc influx into cells. By the same mechanism, could also
CC       prevent L-type calcium channels-mediated heavy metal influx into cells
CC       (PubMed:15451416). In some cells, could also function as a zinc
CC       ion:proton antiporter mediating zinc entry into the lumen of
CC       cytoplasmic vesicles. In macrophages, can increase zinc ions
CC       concentration into the lumen of cytoplasmic vesicles containing
CC       engulfed bacteria and could help inactivate them (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y6M5, ECO:0000269|PubMed:15451416,
CC       ECO:0000305|PubMed:15452870}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out);
CC         Xref=Rhea:RHEA:72627, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q62720};
CC   -!- SUBUNIT: Homodimer. Interacts with TMEM163 (By similarity).
CC       {ECO:0000250|UniProtKB:Q62720, ECO:0000250|UniProtKB:Q9Y6M5}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q62720};
CC       Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q62720}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q9Y6M5}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localization to the plasma membrane is regulated by
CC       cellular zinc status. Recruitment to the plasma membrane from an
CC       internal pool is stimulated by zinc while in absence of zinc the plasma
CC       membrane pool is endocytosed and degraded (By similarity). Localizes to
CC       the basolateral surface of enterocytes (By similarity). Localizes to
CC       zinc-containing intracellular vesicles in macrophages (By similarity).
CC       {ECO:0000250|UniProtKB:Q62720, ECO:0000250|UniProtKB:Q9Y6M5}.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DISRUPTION PHENOTYPE: Knockout of Slc30a1 is embryonic lethal.
CC       {ECO:0000269|PubMed:15452870}.
CC   -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC       transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR   EMBL; U17132; AAA79233.1; -; Genomic_DNA.
DR   EMBL; BC052166; AAH52166.1; -; mRNA.
DR   CCDS; CCDS15625.1; -.
DR   PIR; S54302; S54302.
DR   RefSeq; NP_033605.1; NM_009579.3.
DR   AlphaFoldDB; Q60738; -.
DR   SMR; Q60738; -.
DR   BioGRID; 204704; 3.
DR   STRING; 10090.ENSMUSP00000042410; -.
DR   GlyCosmos; Q60738; 1 site, No reported glycans.
DR   GlyGen; Q60738; 1 site.
DR   iPTMnet; Q60738; -.
DR   PhosphoSitePlus; Q60738; -.
DR   SwissPalm; Q60738; -.
DR   EPD; Q60738; -.
DR   jPOST; Q60738; -.
DR   MaxQB; Q60738; -.
DR   PaxDb; 10090-ENSMUSP00000042410; -.
DR   ProteomicsDB; 275308; -.
DR   Pumba; Q60738; -.
DR   Antibodypedia; 20709; 273 antibodies from 26 providers.
DR   DNASU; 22782; -.
DR   Ensembl; ENSMUST00000044954.7; ENSMUSP00000042410.7; ENSMUSG00000037434.8.
DR   GeneID; 22782; -.
DR   KEGG; mmu:22782; -.
DR   UCSC; uc007edc.1; mouse.
DR   AGR; MGI:1345281; -.
DR   CTD; 7779; -.
DR   MGI; MGI:1345281; Slc30a1.
DR   VEuPathDB; HostDB:ENSMUSG00000037434; -.
DR   eggNOG; KOG1483; Eukaryota.
DR   GeneTree; ENSGT00940000156484; -.
DR   HOGENOM; CLU_013430_4_3_1; -.
DR   InParanoid; Q60738; -.
DR   OMA; TYTYGWQ; -.
DR   OrthoDB; 5482779at2759; -.
DR   PhylomeDB; Q60738; -.
DR   TreeFam; TF313924; -.
DR   Reactome; R-MMU-435368; Zinc efflux and compartmentalization by the SLC30 family.
DR   BioGRID-ORCS; 22782; 1 hit in 79 CRISPR screens.
DR   PRO; PR:Q60738; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q60738; Protein.
DR   Bgee; ENSMUSG00000037434; Expressed in ectoplacental cone and 91 other cell types or tissues.
DR   ExpressionAtlas; Q60738; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR   GO; GO:0030315; C:T-tubule; ISO:MGI.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; IDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0140826; F:zinc:proton antiporter activity; ISS:UniProtKB.
DR   GO; GO:0070574; P:cadmium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR   GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR   GO; GO:0071585; P:detoxification of cadmium ion; ISO:MGI.
DR   GO; GO:0010312; P:detoxification of zinc ion; IBA:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IDA:BHF-UCL.
DR   GO; GO:0006882; P:intracellular zinc ion homeostasis; IDA:BHF-UCL.
DR   GO; GO:0090281; P:negative regulation of calcium ion import; IDA:BHF-UCL.
DR   GO; GO:0046929; P:negative regulation of neurotransmitter secretion; ISO:MGI.
DR   GO; GO:0071584; P:negative regulation of zinc ion transmembrane import; IDA:BHF-UCL.
DR   GO; GO:0140882; P:zinc export across plasma membrane; ISS:UniProtKB.
DR   GO; GO:0062111; P:zinc ion import into organelle; ISS:UniProtKB.
DR   GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006829; P:zinc ion transport; IDA:BHF-UCL.
DR   Gene3D; 1.20.1510.10; Cation efflux protein transmembrane domain; 1.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR036837; Cation_efflux_CTD_sf.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   NCBIfam; TIGR01297; CDF; 1.
DR   PANTHER; PTHR45820; FI23527P1; 1.
DR   PANTHER; PTHR45820:SF1; ZINC TRANSPORTER 1; 1.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   SUPFAM; SSF160240; Cation efflux protein cytoplasmic domain-like; 1.
DR   SUPFAM; SSF161111; Cation efflux protein transmembrane domain-like; 1.
DR   Genevisible; Q60738; MM.
PE   1: Evidence at protein level;
KW   Antiport; Cell membrane; Cytoplasmic vesicle; Glycoprotein; Ion transport;
KW   Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
FT   CHAIN           1..503
FT                   /note="Proton-coupled zinc antiporter SLC30A1"
FT                   /id="PRO_0000206092"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6M5"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..35
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6M5"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..78
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6M5"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6M5"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..243
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6M5"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        265..303
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6M5"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..503
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6M5"
FT   REGION          140..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..156
FT                   /note="6 X 2 AA approximate repeats of H-G"
FT   COMPBIAS        183..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="transported zinc"
FT                   /evidence="ECO:0000250|UniProtKB:Q62720"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="transported zinc"
FT                   /evidence="ECO:0000250|UniProtKB:P69380"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="transported zinc"
FT                   /evidence="ECO:0000250|UniProtKB:P69380"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="transported zinc"
FT                   /evidence="ECO:0000250|UniProtKB:Q62720"
FT   MOD_RES         502
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   503 AA;  54716 MW;  7C4FF93FC13CDA22 CRC64;
     MGCWGRNRGR LLCMLLLTFM FMVLEVVVSR VTASLAMLSD SFHMLSDVLA LVVALVAERF
     ARRTHATQKN TFGWIRAEVM GALVNAIFLT GLCFAILLEA VERFIEPHEM QQPLVVLSVG
     VAGLLVNVLG LCLFHHHSGE GQGAGHGHSH GHGHGHLAKG ARKAGRAGVE AGAPPGRAPD
     QEETNTLVAN TSNSNGLKAD QAEPEKLRSD DPVDVQVNGN LIQESDNLEA EDNRAGQLNM
     RGVFLHVLGD ALGSVIVVVN ALVFYFNWKG CTEDDFCTNP CFPDPCKSSV EIINSTQAPM
     RDAGPCWVLY LDPTLCIIMV CILLYTTYPL LKESALILLQ TVPKQIDIKH LVKELRDVDG
     VEEVHELHVW QLAGSRIIAT AHIKCEDPAS YMQVAKTIKD VFHNHGIHAT TIQPEFASVG
     SKSSVLPCEL ACRTQCALKQ CCGTRPQVHS GKDAEKAPTV SISCLELSEN LEKKARRTKA
     EGSLPAVVIE IKNVPNKQPE SSL
//