SLC30A1
entrez
7779
canonical
uniprot
Q9Y6M5
canonical
ensembl
ENSG00000170385
resolver
ensp
ENSP00000355968
resolver
enst
ENST00000367001
resolver
genesymbol
SLC30A1
resolver
genesymbol_syn
ZNT1
resolver
hgnc
HGNC:11012
resolver
uniprot
Q0VAK9
resolver
uniprot
Q9BZF6
resolver
uniprot_entry
ZNT1_HUMAN
resolver
uniprot_sec
Q0VAK9
resolver
uniprot_sec
Q9BZF6
resolver
amino_acid_sequence
MGCWGRNRGRLLCMLALTFMFMVLEVVVSRVTSSLAMLSDSFHMLSDVLALVVALVAERFARRTHATQKNTFGWIRAEVMGALVNAIFLTGLCFAILLEAIERFIEPHEMQQPLVVLGVGVAGLLVNVLGLCLFHHHSGFSQDSGHGHSHGGHGHGHGLPKGPRVKSTRPGSSDINVAPGEQGPDQEETNTLVANTSNSNGLKLDPADPENPRSGDTVEVQVNGNLVREPDHMELEEDRAGQLNMRGVFLHVLGDALGSVIVVVNALVFYFSWKGCSEGDFCVNPCFPDPCKAFVEIINSTHASVYEAGPCWVLYLDPTLCVVMVCILLYTTYPLLKESALILLQTVPKQIDIRNLIKELRNVEGVEEVHELHVWQLAGSRIIATAHIKCEDPTSYMEVAKTIKDVFHNHGIHATTIQPEFASVGSKSSVVPCELACRTQCALKQCCGTLPQAPSGKDAEKTPAVSISCLELSNNLEKKPRRTKAENIPAVVIEIKNMPNKQPESSL
uniprot
proteins
function
FUNCTION: Zinc ion:proton antiporter that could function at the plasma membrane mediating zinc efflux from cells against its electrochemical gradient protecting them from intracellular zinc accumulation and toxicity (PubMed:31471319, PubMed:33996761, PubMed:39422023, PubMed:39111308, PubMed:39390258). Alternatively, could prevent the transport to the plasma membrane of CACNB2, the L-type calcium channels regulatory subunit, through a yet to be defined mechanism. By modulating the expression of these channels at the plasma membrane, could prevent calcium and zinc influx into cells. By the same mechanism, could also prevent L-type calcium channels-mediated heavy metal influx into cells (By similarity). In some cells, could also function as a zinc ion:proton antiporter mediating zinc entry into the lumen of cytoplasmic vesicles. In macrophages, can increase zinc ions concentration into the lumen of cytoplasmic vesicles containing engulfed bacteria and could help inactivate them (PubMed:32441444). Forms a complex with TMC6/EVER1 and TMC8/EVER2 at the ER membrane of keratynocytes which facilitates zinc uptake into the ER (PubMed:18158319). Down-regulates the activity of transcription factors induced by zinc and cytokines (PubMed:18158319). Also functions as a copper transporter, facilitating the entry of copper into cells, which is crucial for copper-induced cell death (cuproptosis) (PubMed:39111308). Acts as a Zn(2+)/Ca(2+) exchanger, exporting zinc in exchange for calcium influx (PubMed:38669333). {ECO:0000250|UniProtKB:Q62720, ECO:0000269|PubMed:18158319, ECO:0000269|PubMed:31471319, ECO:0000269|PubMed:32441444, ECO:0000269|PubMed:33996761, ECO:0000269|PubMed:38669333, ECO:0000269|PubMed:39111308, ECO:0000269|PubMed:39390258, ECO:0000269|PubMed:39422023}.
uniprot
proteins
mass_dalton
55300
uniprot
proteins
mutagenesis
MUTAGEN 25; /note="E->A: Significant reduction in calcium-dependent Zn(2+) transport activity."; /evidence="ECO:0000269|PubMed:38669333"; MUTAGEN 39; /note="S->A: Significant reduction in Cu(2+) transport activity."; /evidence="ECO:0000269|PubMed:39111308"; MUTAGEN 40; /note="D->A: Significant reduction in calcium-dependent Zn(2+) transport activity."; /evidence="ECO:0000269|PubMed:38669333"; MUTAGEN 43; /note="H->A: Significant reduction in Cu(2+) and Zn(2+) transport activity. Loss of calcium-dependent Zn(2+) transport activity; when associated with A-251."; /evidence="ECO:0000269|PubMed:38669333, ECO:0000269|PubMed:39111308, ECO:0000269|PubMed:39390258, ECO:0000269|PubMed:39422023"; MUTAGEN 47; /note="D->A: Significant reduction in Cu(2+) and Zn(2+) transport activity. Loss of calcium-dependent Zn(2+) transport activity; when associated with A-255."; /evidence="ECO:0000269|PubMed:38669333, ECO:0000269|PubMed:39111308, ECO:0000269|PubMed:39422023"; MUTAGEN 47; /note="D->N: Loss of calcium-dependent Zn(2+) transport activity; when associated with N-255."; /evidence="ECO:0000269|PubMed:38669333"; MUTAGEN 78; /note="E->A: 50% reduction in calcium-dependent Zn(2+) transport activity."; /evidence="ECO:0000269|PubMed:38669333"; MUTAGEN 99; /note="E->A: 50% reduction in calcium-dependent Zn(2+) transport activity. Significant reduction in Cu(2+) transport activity."; /evidence="ECO:0000269|PubMed:38669333, ECO:0000269|PubMed:39111308"; MUTAGEN 102; /note="E->A: Significant reduction in Cu(2+) transport activity."; /evidence="ECO:0000269|PubMed:39111308"; MUTAGEN 103; /note="R->A: Significant reduction in Cu(2+) transport activity."; /evidence="ECO:0000269|PubMed:39111308"; MUTAGEN 244; /note="N->A: 50% reduction in calcium-dependent Zn(2+) transport activity."; /evidence="ECO:0000269|PubMed:38669333"; MUTAGEN 251; /note="H->A: Significant reduction in Cu(2+) and Zn(2+) transport activity. Loss of calcium-dependent Zn(2+) transport activity; when associated with A-43."; /evidence="ECO:0000269|PubMed:38669333, ECO:0000269|PubMed:39111308, ECO:0000269|PubMed:39422023"; MUTAGEN 255; /note="D->A: Significant reduction in Cu(2+) and Zn(2+) transport activity. Loss of calcium-dependent Zn(2+) transport activity; when associated with A-47."; /evidence="ECO:0000269|PubMed:38669333, ECO:0000269|PubMed:39111308, ECO:0000269|PubMed:39422023"; MUTAGEN 255; /note="D->N: Loss of calcium-dependent Zn(2+) transport activity; when associated with N-47."; /evidence="ECO:0000269|PubMed:38669333"; MUTAGEN 278; /note="E->A: Significant reduction in Cu(2+) transport activity."; /evidence="ECO:0000269|PubMed:39111308"; MUTAGEN 280; /note="D->A: Significant reduction in Cu(2+) transport activity."; /evidence="ECO:0000269|PubMed:39111308"; MUTAGEN 282; /note="C->S: Significant reduction in Cu(2+) transport activity."; /evidence="ECO:0000269|PubMed:39111308"; MUTAGEN 286; /note="C->S: Significant reduction in Cu(2+) transport activity."; /evidence="ECO:0000269|PubMed:39111308"; MUTAGEN 291; /note="C->S: Significant reduction in Cu(2+) transport activity."; /evidence="ECO:0000269|PubMed:39111308"; MUTAGEN 299; /note="N->A: Loss of N-glycosylation. No effect on localization to the plasma membrane. Increased stability at the plasma membrane. No effect on resistance to zinc-induced cytotoxicity."; /evidence="ECO:0000269|PubMed:31471319"; MUTAGEN 317; /note="D->A: Loss of calcium-dependent Zn(2+) transport activity."; /evidence="ECO:0000269|PubMed:38669333
uniprot
proteins
post_translational_modification
PTM: N-glycosylated at Asn-299. N-glycosylation promotes endocytosis and degradation through the proteasomal or lysosomal pathways. {ECO:0000269|PubMed:31471319}.
uniprot
proteins
protein_family
Cation diffusion facilitator (CDF) transporter (TC 2.A.4) family
uniprot
proteins
protein_family
SLC30A subfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18158319
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
31471319
uniprot
proteins
pubmed
32441444
uniprot
proteins
pubmed
32776265
uniprot
proteins
pubmed
33996761
uniprot
proteins
pubmed
36204728
uniprot
proteins
pubmed
38669333
uniprot
proteins
pubmed
39111308
uniprot
proteins
pubmed
39390258
uniprot
proteins
pubmed
39422023
uniprot
proteins
sequence_length
507
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31471319, ECO:0000269|PubMed:32441444, ECO:0000269|PubMed:32776265}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:31471319}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:32441444}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:18158319, ECO:0000269|PubMed:32776265}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18158319}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18158319}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:18158319}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic density {ECO:0000250|UniProtKB:Q60738}. Note=Localization to the plasma membrane is regulated by cellular zinc status. Recruitment to the plasma membrane from an internal pool is stimulated by zinc while in absence of zinc the plasma membrane pool is endocytosed and degraded (PubMed:31471319). Localizes to the basolateral surface of enterocytes (By similarity). Localizes to zinc-containing intracellular vesicles in macrophages (PubMed:32441444). Localizes in the cytoplasm and to the ER, Golgi and nucleus membranes in keratinocytes (PubMed:18158319). {ECO:0000250|UniProtKB:Q62720, ECO:0000269|PubMed:18158319, ECO:0000269|PubMed:31471319, ECO:0000269|PubMed:32441444}.
uniprot
proteins
transmembrane_region
TRANSMEM 11..31; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 36..56; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 79..99; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 114..134; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 249..269; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 309..329; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins