ZNT3_RAT
ID ZNT3_RAT Reviewed; 388 AA.
AC Q6QIX3; Q5RJT1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Zinc transporter 3 {ECO:0000250|UniProtKB:P97441};
DE Short=ZnT-3 {ECO:0000250|UniProtKB:P97441};
DE AltName: Full=Solute carrier family 30 member 3 {ECO:0000312|RGD:1359689};
GN Name=Slc30a3 {ECO:0000312|RGD:1359689};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RA Cowie T.F., Kanellakis S., Masters C.L., Bush A.I.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-66, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000250|UniProtKB:Q99726}.
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 could regulate efficiency of zinc
CC transport. {ECO:0000250|UniProtKB:Q99726}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q99726}; Multi-pass membrane
CC protein {ECO:0000255}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P97441}. 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6QIX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6QIX3-2; Sequence=VSP_036043;
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; AY538655; AAS46250.1; -; mRNA.
DR EMBL; CH473947; EDM02934.1; -; Genomic_DNA.
DR EMBL; BC086513; AAH86513.1; -; mRNA.
DR RefSeq; NP_001013261.1; NM_001013243.1. [Q6QIX3-1]
DR RefSeq; XP_008762748.1; XM_008764526.2. [Q6QIX3-2]
DR RefSeq; XP_008762749.1; XM_008764527.2. [Q6QIX3-2]
DR RefSeq; XP_008762750.1; XM_008764528.1. [Q6QIX3-2]
DR AlphaFoldDB; Q6QIX3; -.
DR SMR; Q6QIX3; -.
DR BioGRID; 266006; 1.
DR IntAct; Q6QIX3; 2.
DR MINT; Q6QIX3; -.
DR STRING; 10116.ENSRNOP00000008126; -.
DR iPTMnet; Q6QIX3; -.
DR PhosphoSitePlus; Q6QIX3; -.
DR PaxDb; Q6QIX3; -.
DR PRIDE; Q6QIX3; -.
DR Ensembl; ENSRNOT00000008126; ENSRNOP00000008126; ENSRNOG00000006204. [Q6QIX3-1]
DR GeneID; 366568; -.
DR KEGG; rno:366568; -.
DR CTD; 7781; -.
DR RGD; 1359689; Slc30a3.
DR eggNOG; KOG1482; Eukaryota.
DR GeneTree; ENSGT00940000161480; -.
DR HOGENOM; CLU_013430_0_1_1; -.
DR InParanoid; Q6QIX3; -.
DR OMA; RTWGWAR; -.
DR OrthoDB; 973492at2759; -.
DR PhylomeDB; Q6QIX3; -.
DR TreeFam; TF313382; -.
DR PRO; PR:Q6QIX3; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000006204; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q6QIX3; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0097457; C:hippocampal mossy fiber; ISO:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0051050; P:positive regulation of transport; ISO:RGD.
DR GO; GO:0061088; P:regulation of sequestering of zinc ion; ISO:RGD.
DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central.
DR GO; GO:0099180; P:zinc ion import into synaptic vesicle; ISO:RGD.
DR GO; GO:0071577; P:zinc ion transmembrane transport; ISS:UniProtKB.
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 Alternative splicing; Cytoplasmic vesicle; Endosome; Ion transport;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..388
FT /note="Zinc transporter 3"
FT /id="PRO_0000357045"
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..42
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:0007744|PubMed:22673903"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036043"
SQ SEQUENCE 388 AA; 41898 MW; 767F8165AF1533F7 CRC64;
MEPSPASGGS ETTRLVSPRD RSSAGGGLRL KSLFTEPSEP LPEGPKLEGM AFHHCHKNRV
SQSGLSPERA QARRQLYAAC VVCFIFMAGE VVGGYLAHSL AIMTDAAHLL ADIGSMMASL
FSLWLSTRPA TRTMTFGWHR SETLGALASV VSLWIVTGIL LYLAFLRLLH SDYHIEAGAM
LLTASIAVCA NMIMAFVLHQ TGAPHSHGPR GAEYAPLEEG HGHPLSLGNT SVRAAFVHVL
GDLLQSLGVL AASILIYFKP QYKVADPIST FLFSICALGS TAPTLRDVLL VLMEGAPRSV
EFEPVRDTLL SVPGVRATHD LHLWALTLTY HVASAHLAID STADPEAILA EASSRLYSRF
GFSSCTLQVE KYRSEMAHCL RCREPPKA
