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 02-JUN-2021, entry version 167. DE RecName: Full=Zinc transporter 3; DE Short=ZnT-3; DE AltName: Full=Solute carrier family 30 member 3; GN Name=Slc30a3; 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], FUNCTION, 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 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 [3] 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 [4] 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: Involved in accumulation of zinc in synaptic vesicles. CC {ECO:0000269|PubMed:8962159}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic CC vesicle membrane {ECO:0000305|PubMed:21998198}; Multi-pass membrane CC protein {ECO:0000305|PubMed:21998198}. Cell junction, synapse, CC synaptosome {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}. Cytoplasmic vesicle, secretory CC vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q99726}. CC -!- TISSUE SPECIFICITY: Brain and testis. In the brain, most abundant in CC hippocampus and cerebral cortex. In the testis, expression is CC restricted to germ cells and is highest in pachytene spermatocytes and CC round spermatids. {ECO:0000269|PubMed:8962159}. 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 BioGRID; 204705; 2. DR IntAct; P97441; 3. 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; 141 antibodies. 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 eggNOG; KOG1482; Eukaryota. DR GeneTree; ENSGT00940000161480; -. DR InParanoid; P97441; -. DR OrthoDB; 973492at2759; -. DR PhylomeDB; P97441; -. DR TreeFam; TF313382; -. DR BioGRID-ORCS; 22784; 0 hits in 52 CRISPR screens. DR ChiTaRS; Slc30a3; mouse. DR PRO; PR:P97441; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; P97441; protein. DR Bgee; ENSMUSG00000029151; Expressed in primary visual cortex and 228 other tissues. DR Genevisible; P97441; MM. 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; IBA:GO_Central. 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 Cell junction; Cytoplasmic vesicle; Endosome; Ion transport; Lysosome; KW Membrane; Phosphoprotein; Reference proteome; Synapse; Synaptosome; KW Transmembrane; 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:0000255" FT TRANSMEM 76..96 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 97..105 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 106..126 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 127..145 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 146..166 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 167..177 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 178..198 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 199..235 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 236..256 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 257..263 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 264..284 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 285..388 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" 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 //