ZNT10_MOUSE
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 03-AUG-2022, entry version 117.
DE RecName: Full=Zinc transporter 10;
DE Short=ZnT-10;
DE AltName: Full=Solute carrier family 30 member 10;
GN Name=Slc30a10; Synonyms=Znt10;
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).
CC -!- FUNCTION: Plays a pivotal role in manganese transport. Manganese is an
CC essential cation for the function of several enzymes, including some
CC crucially important for the metabolism of neurotransmitters and other
CC neuronal metabolic pathways. However, elevated levels of manganese are
CC cytotoxic and induce oxidative stress, mitochondrial dysfunction and
CC apoptosis. Acts as manganese efflux transporter and confers protection
CC against manganese-induced cell death. Also acts as zinc transporter
CC involved in zinc homeostasis. Seems to mediate zinc transport into
CC early endosomes and recycling endosomes to prevent zinc toxicity; the
CC function may be regulated by heterodimerization with other zinc
CC transporters of the SLC30A subfamily. The SLC30A3:SLC30A10 heterodimer
CC is involved in zinc transport-dependent regulation of the EGFR/ERK
CC transduction pathway in endosomes. May be involved in regulation of
CC zinc-dependent senescence of vascular smooth muscle cells.
CC {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 and occurs probably in a
CC tissue-specific manner. {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:0000305}. Golgi apparatus, trans-Golgi
CC network {ECO:0000250|UniProtKB:Q6XR72}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q6XR72}. Early endosome
CC {ECO:0000250|UniProtKB:Q6XR72}. Note=Relocalized from the trans-Golgi
CC network to the plasma membrane upon elevated extracellular Zn
CC concentrations. {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 -!- 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; Q3UVU3; -.
DR PeptideAtlas; Q3UVU3; -.
DR PRIDE; Q3UVU3; -.
DR ProteomicsDB; 275103; -. [Q3UVU3-1]
DR ProteomicsDB; 275104; -. [Q3UVU3-2]
DR Antibodypedia; 3072; 114 antibodies from 19 providers.
DR DNASU; 226781; -.
DR Ensembl; ENSMUST00000061093; ENSMUSP00000053181; ENSMUSG00000026614. [Q3UVU3-1]
DR GeneID; 226781; -.
DR KEGG; mmu:226781; -.
DR UCSC; uc007dzk.1; mouse. [Q3UVU3-1]
DR UCSC; uc007dzl.2; mouse. [Q3UVU3-2]
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; IFHHAGI; -.
DR OrthoDB; 820567at2759; -.
DR PhylomeDB; Q3UVU3; -.
DR TreeFam; TF313924; -.
DR Reactome; R-MMU-425410; Metal ion SLC transporters.
DR BioGRID-ORCS; 226781; 1 hit in 71 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 104 other tissues.
DR ExpressionAtlas; Q3UVU3; baseline and differential.
DR Genevisible; Q3UVU3; MM.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; 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:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
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:0071421; P:manganese ion transmembrane transport; ISO:MGI.
DR GO; GO:0006828; P:manganese ion transport; ISS:UniProtKB.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:1905802; P:regulation of cellular response to manganese ion; ISO:MGI.
DR GO; GO:0071579; P:regulation of zinc ion transport; ISO:MGI.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
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="Zinc transporter 10"
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 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
