Slc39a8
entrez
295455
canonical
uniprot
Q5FVQ0
canonical
ensembl
ENSRNOG00000012508
resolver
ensembl
ENSRNOG00055011373
resolver
ensembl
ENSRNOG00060021601
resolver
ensembl
ENSRNOG00065025333
resolver
ensp
ENSRNOP00000030977
resolver
ensp
ENSRNOP00055015555
resolver
ensp
ENSRNOP00060030841
resolver
ensp
ENSRNOP00065035829
resolver
enst
ENSRNOT00000033413
resolver
enst
ENSRNOT00055019283
resolver
enst
ENSRNOT00060037410
resolver
enst
ENSRNOT00065043650
resolver
genesymbol
Slc39a8
resolver
genesymbol_syn
Zip8
resolver
uniprot_entry
S39A8_RAT
resolver
amino_acid_sequence
MAPGRAVAGLLLLAATGLGRPSEGPELAFTEDVLRVFGANQSLSAAQLGRLLERLGAAPQQGALELGQLHFNQCLSAEDIFSLHGFSNVTQITSSNFTAICPAILQQLNFHPCEDPQKHSVKPSFSEVWGYGFLSVTIINLASLLGLILTPLIKKSYFPKILTYFVGLAIGTLFSNAIFQLIPEAFGFNPKIDNYVEKAVAVFGGFYMLFFVERTLKMLLKTYGQNDHTHFRNDDFGSKEKAHQPKTLPLPPVNGVTCYANPAVTEPNGHIHFDTVSVVSLQDGKAESSSCTCLKGPKLSEIGTIAWMITLCDALHNFIDGLAIGASYTLSLLQGLSTSIAILCEEFPHELGDFVILLNAGMSTRQALLFNFLSACSCYVGLAFGILVGNNFAPNIIFALAGGMFLYISLADMFPEMNDMLREKVTGRQTDFTFFMIQNAGMLTGFTAILLITLYAGDIELQ
uniprot
proteins
function
FUNCTION: Electroneutral divalent metal cation:bicarbonate symporter of the plasma membrane mediating the cellular uptake of zinc and manganese, two divalent metal cations important for development, tissue homeostasis and immunity (PubMed:22898811). Transports an electroneutral complex composed of a divalent metal cation and two bicarbonate anions or alternatively a bicarbonate and a selenite anion (PubMed:22898811). Thereby, it also contributes to the cellular uptake of selenium, an essential trace metal and micronutrient (PubMed:22898811). Also imports cadmium a non-essential metal which is cytotoxic and carcinogenic (PubMed:22898811). May also transport iron and cobalt through membranes (PubMed:22898811). Through zinc import, indirectly regulates the metal-dependent transcription factor MTF1 and the expression of some metalloproteases involved in cartilage catabolism and also probably heart development. Also indirectly regulates the expression of proteins involved in cell morphology and cytoskeleton organization. Indirectly controls innate immune function and inflammatory response by regulating zinc cellular uptake which in turn modulates the expression of genes specific of these processes. Protects, for instance, cells from injury and death at the onset of inflammation (By similarity). By regulating zinc influx into monocytes also directly modulates their adhesion to endothelial cells and arteries (By similarity). Reclaims manganese from the bile at the apical membrane of hepatocytes, thereby regulating the activity of the manganese-dependent enzymes through the systemic levels of the nutrient. Also participates in manganese reabsorption in the proximal tubule of the kidney. By mediating the extracellular uptake of manganese by cells of the blood-brain barrier, may also play a role in the transport of the micronutrient to the brain. With manganese cellular uptake also participates in mitochondrial proper function (By similarity). Finally, also probably functions intracellularly, translocating zinc from lysosome to cytosol to indirectly enhance the expression of specific genes during TCR-mediated T cell activation (By similarity). {ECO:0000250|UniProtKB:Q91W10, ECO:0000250|UniProtKB:Q9C0K1, ECO:0000269|PubMed:22898811}.
uniprot
proteins
mass_dalton
50171
uniprot
proteins
mutagenesis
MUTAGEN 40; /note="N->D: Decreased glycosylation."; /evidence="ECO:0000269|PubMed:22898811"; MUTAGEN 88; /note="N->Q: Decreased glycosylation."; /evidence="ECO:0000269|PubMed:22898811"; MUTAGEN 96; /note="N->Q: Decreased glycosylation."; /evidence="ECO:0000269|PubMed:22898811
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. N-glycosylation is not required for proper iron and zinc transport. {ECO:0000269|PubMed:22898811}.
uniprot
proteins
protein_family
ZIP transporter (TC 2.A.5) family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22898811
uniprot
proteins
sequence_length
462
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22898811}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9C0K1}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q9C0K1}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9C0K1}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the lysosome of activated T-cells. A large fraction of the protein is found intracellularly in microvascular capillary endothelial cells that constitute the blood-brain barrier. Localized and functional at both apical and basolateral membranes of microvascular capillary endothelial cells that constitute the blood-brain barrier. {ECO:0000250|UniProtKB:Q9C0K1}.
uniprot
proteins
transmembrane_region
TRANSMEM 133..153; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 161..181; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 192..212; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 368..388; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 391..411; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 432..452; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins