ID   ZNT10_MOUSE             Reviewed;         470 AA.
AC   Q3UVU3; Q32NY2;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Calcium/manganese antiporter SLC30A10 {ECO:0000305|PubMed:28461334};
DE   AltName: Full=Solute carrier family 30 member 10 {ECO:0000312|MGI:MGI:2685058};
GN   Name=Slc30a10 {ECO:0000312|MGI:MGI:2685058};
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] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
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] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   IDENTIFICATION BY 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   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28461334; DOI=10.1074/jbc.m117.783605;
RA   Hutchens S., Liu C., Jursa T., Shawlot W., Chaffee B.K., Yin W., Gore A.C.,
RA   Aschner M., Smith D.R., Mukhopadhyay S.;
RT   "Deficiency in the manganese efflux transporter SLC30A10 induces severe
RT   hypothyroidism in mice.";
RL   J. Biol. Chem. 292:9760-9773(2017).
CC   -!- FUNCTION: Calcium:manganese antiporter of the plasma membrane mediating
CC       the efflux of intracellular manganese coupled to an active
CC       extracellular calcium exchange. Required for intracellular manganese
CC       homeostasis, an essential cation for the function of several enzymes,
CC       including some crucially important for the metabolism of
CC       neurotransmitters and other neuronal metabolic pathways. Manganese can
CC       also be cytotoxic and induce oxidative stress, mitochondrial
CC       dysfunction and apoptosis (PubMed:28461334). Could also have an
CC       intracellular zinc ion transporter activity, directly regulating
CC       intracellular zinc ion homeostasis and more indirectly various
CC       signaling pathway and biological processes (By similarity).
CC       {ECO:0000250|UniProtKB:Q6XR72, ECO:0000269|PubMed:28461334}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) + Mn(2+)(out) = Ca(2+)(out) + Mn(2+)(in);
CC         Xref=Rhea:RHEA:73059, ChEBI:CHEBI:29035, ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:28461334};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351,
CC         ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6XR72};
CC   -!- SUBUNIT: Forms homodimers. Forms heterodimers and high-molecular weight
CC       oligomers with SLC30A3, SLC30A2 and SLC30A4; heterodimerization is
CC       mediated by covalent-bound tyrosine residues, occurs probably in a
CC       tissue-specific manner and could mediate the intracellular zinc
CC       transport activity into early endosomes and recycling endosomes.
CC       {ECO:0000250|UniProtKB:Q6XR72}.
CC   -!- INTERACTION:
CC       Q3UVU3; Q2HJ10: Slc30a2; NbExp=2; IntAct=EBI-13945374, EBI-13945312;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6XR72};
CC       Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q6XR72}; Multi-pass membrane protein
CC       {ECO:0000255}. Recycling endosome membrane
CC       {ECO:0000250|UniProtKB:Q6XR72}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q6XR72}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localization to the Golgi and plasma membrane is
CC       regulated by zinc. {ECO:0000250|UniProtKB:Q6XR72}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UVU3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UVU3-2; Sequence=VSP_029867;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in fetal liver and fetal
CC       brain.
CC   -!- DISRUPTION PHENOTYPE: Homozygous knockout mice lacking Slc30a10 are
CC       born at expected Mendelian ratios and do not display overt phenotype
CC       until postnatal day 16 to 18 (PubMed:28461334). After weaning they fail
CC       to gain weight, are smaller, and die prematurely (PubMed:28461334).
CC       Manganese levels are elevated in the tested tissues including brain,
CC       liver, blood and thyroid and manganese toxicity induces an
CC       hypothyroidism phenotype (PubMed:28461334).
CC       {ECO:0000269|PubMed:28461334}.
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; AK136932; BAE23176.1; -; mRNA.
DR   EMBL; BC108419; AAI08420.1; -; mRNA.
DR   CCDS; CCDS15599.1; -. [Q3UVU3-1]
DR   RefSeq; NP_001028458.1; NM_001033286.2. [Q3UVU3-1]
DR   AlphaFoldDB; Q3UVU3; -.
DR   SMR; Q3UVU3; -.
DR   IntAct; Q3UVU3; 1.
DR   STRING; 10090.ENSMUSP00000053181; -.
DR   iPTMnet; Q3UVU3; -.
DR   PhosphoSitePlus; Q3UVU3; -.
DR   SwissPalm; Q3UVU3; -.
DR   MaxQB; Q3UVU3; -.
DR   PaxDb; 10090-ENSMUSP00000053181; -.
DR   PeptideAtlas; Q3UVU3; -.
DR   ProteomicsDB; 275103; -. [Q3UVU3-1]
DR   ProteomicsDB; 275104; -. [Q3UVU3-2]
DR   Antibodypedia; 3072; 141 antibodies from 19 providers.
DR   DNASU; 226781; -.
DR   Ensembl; ENSMUST00000061093.7; ENSMUSP00000053181.7; ENSMUSG00000026614.8. [Q3UVU3-1]
DR   GeneID; 226781; -.
DR   KEGG; mmu:226781; -.
DR   UCSC; uc007dzk.1; mouse. [Q3UVU3-1]
DR   UCSC; uc007dzl.2; mouse. [Q3UVU3-2]
DR   AGR; MGI:2685058; -.
DR   CTD; 55532; -.
DR   MGI; MGI:2685058; Slc30a10.
DR   VEuPathDB; HostDB:ENSMUSG00000026614; -.
DR   eggNOG; KOG1483; Eukaryota.
DR   GeneTree; ENSGT00940000159967; -.
DR   HOGENOM; CLU_013430_4_3_1; -.
DR   InParanoid; Q3UVU3; -.
DR   OMA; FQDCASW; -.
DR   OrthoDB; 5482779at2759; -.
DR   PhylomeDB; Q3UVU3; -.
DR   TreeFam; TF313924; -.
DR   Reactome; R-MMU-425410; Metal ion SLC transporters.
DR   BioGRID-ORCS; 226781; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Slc30a10; mouse.
DR   PRO; PR:Q3UVU3; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q3UVU3; Protein.
DR   Bgee; ENSMUSG00000026614; Expressed in duodenum and 105 other cell types or tissues.
DR   ExpressionAtlas; Q3UVU3; baseline and differential.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR   GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR   GO; GO:0140983; F:calcium:manganese antiporter activity; ISS:UniProtKB.
DR   GO; GO:0005384; F:manganese ion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:1904385; P:cellular response to angiotensin; ISO:MGI.
DR   GO; GO:0010312; P:detoxification of zinc ion; IBA:GO_Central.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI.
DR   GO; GO:0030026; P:intracellular manganese ion homeostasis; ISO:MGI.
DR   GO; GO:0006882; P:intracellular zinc ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0140048; P:manganese ion export across plasma membrane; ISS:UniProtKB.
DR   GO; GO:0055071; P:manganese ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0006828; P:manganese ion transport; ISO:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
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   Gene3D; 1.20.1510.10; Cation efflux protein transmembrane domain; 1.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   NCBIfam; TIGR01297; CDF; 1.
DR   PANTHER; PTHR45820; FI23527P1; 1.
DR   PANTHER; PTHR45820:SF3; ZINC TRANSPORTER 10; 1.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   SUPFAM; SSF161111; Cation efflux protein transmembrane domain-like; 1.
DR   Genevisible; Q3UVU3; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Endosome; Golgi apparatus;
KW   Ion transport; Manganese; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Zinc; Zinc transport.
FT   CHAIN           1..470
FT                   /note="Calcium/manganese antiporter SLC30A10"
FT                   /id="PRO_0000312581"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..34
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..81
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..233
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..270
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..470
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          146..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..470
FT                   /note="Required for plasma membrane localization"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XR72"
FT   REGION          451..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            43
FT                   /note="Important for coupling of manganese to calcium
FT                   transport"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XR72"
FT   VAR_SEQ         1..237
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029867"
FT   CONFLICT        339
FT                   /note="A -> S (in Ref. 2; AAI08420)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   470 AA;  50911 MW;  E2DF53D5890CEE2B CRC64;
     MGRYSGKTCR LLFMLVLTAA FFVAELVSGY LGNSIALLSD SFNMLSDLIS LCVGLGSGYI
     ARRGPRGSSA TYGYVRAEVV GALSNAVFLT ALCFTIFVEA VLRLARPERI DDPELVLIVG
     ALGLAVNVVG LLIFQDCGAC FSRCTRGRRT RPSQQPSQGD PRGALGCPQE AATATAPGSG
     TAVTLRGSSA GRKQQEGATV FSNVAGDSLN TENEPEETTK KEKKSEALNI RGVLLHVMGD
     ALGSVVVVIT AIIFYVQPLR REDPCNWQCY IDPSLTVVMV IIILSSAFPL IKETAVILLQ
     MVPKGVNMEE LMSQLSTVPG ISSVHEVHIW ELISGKIIAT LHIKHQKGTE YQDASRKIRE
     IFHHAGIHNV TIQFETLDLK EALEQKDFLL TCSAPCITQS CAKKLCCPPG TLPLALVNGC
     AEHNGRSSRE SYRSIEAPEV AIDVDGCPRE QGQTLSKTQE RQHYENSTHF
//