ZNT3_MOUSE
ID ZNT3_MOUSE Reviewed; 388 AA.
AC P97441; P97511;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc transporter 3 {ECO:0000305|PubMed:9990090};
DE Short=ZnT-3 {ECO:0000303|PubMed:8962159};
DE AltName: Full=Solute carrier family 30 member 3 {ECO:0000312|MGI:MGI:1345280};
GN Name=Slc30a3 {ECO:0000312|MGI:MGI:1345280}; Synonyms=Znt3;
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 / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129; TISSUE=Brain;
RX PubMed=8962159; DOI=10.1073/pnas.93.25.14934;
RA Palmiter R.D., Cole T.B., Quaife C.J., Findley S.D.;
RT "ZnT-3, a putative transporter of zinc into synaptic vesicles.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14934-14939(1996).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=9356509; DOI=10.1073/pnas.94.23.12676;
RA Wenzel H.J., Cole T.B., Born D.E., Schwartzkroin P.A., Palmiter R.D.;
RT "Ultrastructural localization of zinc transporter-3 (ZnT-3) to synaptic
RT vesicle membranes within mossy fiber boutons in the hippocampus of mouse
RT and monkey.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12676-12681(1997).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=9990090; DOI=10.1073/pnas.96.4.1716;
RA Cole T.B., Wenzel H.J., Kafer K.E., Schwartzkroin P.A., Palmiter R.D.;
RT "Elimination of zinc from synaptic vesicles in the intact mouse brain by
RT disruption of the ZnT3 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1716-1721(1999).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP SUBUNIT.
RX PubMed=19521526; DOI=10.1371/journal.pone.0005896;
RA Salazar G., Falcon-Perez J.M., Harrison R., Faundez V.;
RT "SLC30A3 (ZnT3) oligomerization by dityrosine bonds regulates its
RT subcellular localization and metal transport capacity.";
RL PLoS ONE 4:e5896-e5896(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21998198; DOI=10.1091/mbc.e11-07-0592;
RA Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B.,
RA Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
RT "The schizophrenia susceptibility factor dysbindin and its associated
RT complex sort cargoes from cell bodies to the synapse.";
RL Mol. Biol. Cell 22:4854-4867(2011).
CC -!- FUNCTION: Zinc ion transporter mediating the import of zinc from
CC cytoplasm into synaptic vesicles and participating to cellular zinc ion
CC homeostasis in the brain. {ECO:0000269|PubMed:9990090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351,
CC ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q99726};
CC -!- SUBUNIT: Homodimer. Homodimerization is negligible compared to the
CC human protein. It could explain the lower efficiency of zinc transport.
CC {ECO:0000269|PubMed:19521526}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:9356509,
CC ECO:0000305|PubMed:21998198, ECO:0000305|PubMed:9990090}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:21998198}. Synapse, synaptosome
CC {ECO:0000269|PubMed:21998198}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q99726}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q99726}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to brain (at protein
CC level). In the brain, most abundant in hippocampus and cerebral cortex.
CC The mRNA is also detected in testis, expression being restricted to
CC germ cells and highest in pachytene spermatocytes and round spermatids.
CC {ECO:0000269|PubMed:8962159, ECO:0000269|PubMed:9990090}.
CC -!- DEVELOPMENTAL STAGE: In brain expression is negligible at birth, then
CC increases linearly, reaching a maximum at about 3 weeks postpartum.
CC {ECO:0000269|PubMed:9990090}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice lacking Slc30a3 do not
CC display overt phenotype with morphology, body weight, lifespan,
CC fertility, litter size being normal (PubMed:9990090). Zinc ions are
CC eliminated from synaptic vesicles in brain of the knockout mice and the
CC overall levels of zinc in brain is decreased (PubMed:9990090).
CC {ECO:0000269|PubMed:9990090}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U76007; AAB39731.1; -; mRNA.
DR EMBL; U76009; AAB39733.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U76008; AAB39733.1; JOINED; Genomic_DNA.
DR CCDS; CCDS51455.1; -.
DR RefSeq; NP_035903.2; NM_011773.3.
DR AlphaFoldDB; P97441; -.
DR SMR; P97441; -.
DR BioGRID; 204705; 2.
DR IntAct; P97441; 2.
DR MINT; P97441; -.
DR STRING; 10090.ENSMUSP00000031037; -.
DR iPTMnet; P97441; -.
DR PhosphoSitePlus; P97441; -.
DR SwissPalm; P97441; -.
DR PaxDb; P97441; -.
DR PeptideAtlas; P97441; -.
DR PRIDE; P97441; -.
DR ProteomicsDB; 302147; -.
DR Antibodypedia; 47345; 154 antibodies from 25 providers.
DR DNASU; 22784; -.
DR Ensembl; ENSMUST00000031037; ENSMUSP00000031037; ENSMUSG00000029151.
DR GeneID; 22784; -.
DR KEGG; mmu:22784; -.
DR UCSC; uc008wxa.2; mouse.
DR CTD; 7781; -.
DR MGI; MGI:1345280; Slc30a3.
DR VEuPathDB; HostDB:ENSMUSG00000029151; -.
DR eggNOG; KOG1482; Eukaryota.
DR GeneTree; ENSGT00940000161480; -.
DR InParanoid; P97441; -.
DR OMA; RTWGWAR; -.
DR OrthoDB; 973492at2759; -.
DR PhylomeDB; P97441; -.
DR TreeFam; TF313382; -.
DR BioGRID-ORCS; 22784; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Slc30a3; mouse.
DR PRO; PR:P97441; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P97441; protein.
DR Bgee; ENSMUSG00000029151; Expressed in entorhinal cortex and 142 other tissues.
DR ExpressionAtlas; P97441; baseline and differential.
DR Genevisible; P97441; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0097457; C:hippocampal mossy fiber; IDA:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0010312; P:detoxification of zinc ion; TAS:BHF-UCL.
DR GO; GO:0051050; P:positive regulation of transport; IGI:MGI.
DR GO; GO:0061088; P:regulation of sequestering of zinc ion; ISO:MGI.
DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central.
DR GO; GO:0032119; P:sequestering of zinc ion; TAS:BHF-UCL.
DR GO; GO:0099180; P:zinc ion import into synaptic vesicle; IDA:SynGO.
DR GO; GO:0071577; P:zinc ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006829; P:zinc ion transport; TAS:BHF-UCL.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF160240; SSF160240; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endosome; Ion transport; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..388
FT /note="Zinc transporter 3"
FT /id="PRO_0000206097"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..105
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..177
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..263
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6QIX3"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6QIX3"
SQ SEQUENCE 388 AA; 41824 MW; 3CCDD0A37074EF41 CRC64;
MEPSLATGGS ETTRLVSARD RSSAGGGLRL KSLFTEPSEP LPEEPKLEGM AFHHCHKDPV
PQSGLSPERV QARRQLYAAC AVCFIFMAGE VVGGYLAHSL AIMTDAAHLL ADIGSMLASL
FSLWLSTRPA TRTMTFGWHR SETLGALASV VSLWIVTGIL LYLAFLRLLH SDYHIEAGAM
LLTASIAVCA NLLMAFVLHQ TGAPHSHGST GAEYAPLEEG HGYPMSLGNT SVRAAFVHVL
GDLLQSFGVL AASILIYFKP QYKVADPIST FLFSICALGS TAPTLRDVLL VLMEGAPRSV
EFEPVRDTLL SVPGVRATHD LHLWALTLTY HVASAHLAID STADPEAVLA EASSRLYSRF
GFSSCTLQVE QYQPEMAQCL RCQEPSQA
