Slc39a14
entrez
213053
canonical
uniprot
Q75N73
canonical
ensembl
ENSMUSG00000022094
resolver
ensp
ENSMUSP00000022688
resolver
ensp
ENSMUSP00000066108
resolver
ensp
ENSMUSP00000119040
resolver
ensp
ENSMUSP00000255919
resolver
genesymbol
Slc39a14
resolver
genesymbol_syn
Fad123
resolver
genesymbol_syn
Kiaa0062
resolver
genesymbol_syn
Zip14
resolver
uniprot
A0A0R4J1V1
resolver
uniprot
Q80U85
resolver
uniprot
Q8VDL0
resolver
uniprot_entry
S39AE_MOUSE
resolver
uniprot_sec
A0A0R4J1V1
resolver
uniprot_sec
Q80U85
resolver
uniprot_sec
Q8VDL0
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by cyanide and therefore dependent of an energy source (PubMed:18270315). Inhibited by DIDS/4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid, an inhibitor hydrogencarbonate-dependent transporters (PubMed:18270315). {ECO:0000269|PubMed:18270315}.
uniprot
proteins
amino_acid_sequence
MKRLHPALPSCLLLVLFGIWRTAPQTHASSAGLPPLSATSFLEDLMDRYGKNDSLTLTQLKSLLDHLHVGVGRDNVSQPKEGPRNLSTCFSSGDLFAAHNLSERSQIGASEFQEFCPTILQQLDSQACTSENQKSEENEQTEEGKPSAIEVWGYGFLCVTVISLCSLMGASVVPFMKKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFNPQDNYVSKSAVVFGGFYLFFFTEKILKMLLKQKNEHHHGHNHFTSETLPSKKDQEEGVTEKLQNGDLDHMIPQHCNSELDGKAPGTDEKVIVNSMSVQDLQASQSACYWLKGVRYSDIGTLAWMITLSDGLHNFIDGLAIGASFTVSVFQGISTSVAILCEEFPHELGDFVILLNAGMSIQQALFFNFLSACCCYLGLAFGILAGSHFSANWIFALAGGMFLYIALADMFPEMNEVCQEDEKNDSFLVPFVIQNLGLLTGFSIMLVLTMYSGQIQIG
uniprot
proteins
function
FUNCTION: Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, development and immunity (PubMed:15863613, PubMed:16950869, PubMed:18270315, PubMed:19179618, PubMed:21653899, PubMed:28673968). Functions as an energy-dependent symporter, transporting through the membranes an electroneutral complex composed of a divalent metal cation and two bicarbonate anions (PubMed:18270315). Beside these endogenous cellular substrates, can also import cadmium a non-essential metal which is cytotoxic and carcinogenic (PubMed:18270315). Controls the cellular uptake by the intestinal epithelium of systemic zinc, which is in turn required to maintain tight junctions and the intestinal permeability (PubMed:25428902). Modifies the activity of zinc-dependent phosphodiesterases, thereby indirectly regulating G protein-coupled receptor signaling pathways important for gluconeogenesis and chondrocyte differentiation (PubMed:21445361). Regulates insulin receptor signaling, glucose uptake, glycogen synthesis and gluconeogenesis in hepatocytes through the zinc-dependent intracellular catabolism of insulin (PubMed:27703010). Through zinc cellular uptake also plays a role in the adaptation of cells to endoplasmic reticulum stress (PubMed:28673968). Major manganese transporter of the basolateral membrane of intestinal epithelial cells, it plays a central role in manganese systemic homeostasis through intestinal manganese uptake (PubMed:31028174). Also involved in manganese extracellular uptake by cells of the blood-brain barrier (By similarity). May also play a role in manganese and zinc homeostasis participating in their elimination from the blood through the hepatobiliary excretion (PubMed:28536273). Also functions in the extracellular uptake of free iron (PubMed:16950869, PubMed:19179618, PubMed:21653899, PubMed:23110240, PubMed:26028554). May also function intracellularly and mediate the transport from endosomes to cytosol of iron endocytosed by transferrin (PubMed:20682781). Plays a role in innate immunity by regulating the expression of cytokines by activated macrophages (By similarity). {ECO:0000250|UniProtKB:Q15043, ECO:0000269|PubMed:15863613, ECO:0000269|PubMed:16950869, ECO:0000269|PubMed:18270315, ECO:0000269|PubMed:19179618, ECO:0000269|PubMed:20682781, ECO:0000269|PubMed:21445361, ECO:0000269|PubMed:21653899, ECO:0000269|PubMed:23110240, ECO:0000269|PubMed:25428902, ECO:0000269|PubMed:26028554, ECO:0000269|PubMed:27703010, ECO:0000269|PubMed:28536273, ECO:0000269|PubMed:28673968, ECO:0000269|PubMed:31028174}.
uniprot
proteins
mass_dalton
53962
uniprot
proteins
mutagenesis
MUTAGEN 438; /note="L->R: When overexpressed ubiquitously in conditional knockin mice, perinatally lethal; when overexpressed in osteoblasts in conditional knockin mice, produces a severe skeletal phenotype marked by a drastic increase in cortical thickness due to an enhanced endosteal bone formation; when overexpressed in osteoclasts in conditional knockin mice, no effect on bone hemostasis."; /evidence="ECO:0000269|PubMed:29621230
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. Ubiquitination occurs upon iron depletion. The ubiquitinated form undergoes proteasomal degradation. {ECO:0000250|UniProtKB:Q15043}.; PTM: N-glycosylated (PubMed:18270315, PubMed:21445361). N-glycosylation at Asn-100 is required for iron-regulated extraction of the transporter from membranes and subsequent proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q15043, ECO:0000269|PubMed:18270315, ECO:0000269|PubMed:21445361}.
uniprot
proteins
protein_family
ZIP transporter (TC 2.A.5) family
uniprot
proteins
pubmed
12693553
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15794747
uniprot
proteins
pubmed
15863613
uniprot
proteins
pubmed
16950869
uniprot
proteins
pubmed
17065364
uniprot
proteins
pubmed
18270315
uniprot
proteins
pubmed
19179618
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19656770
uniprot
proteins
pubmed
20682781
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21445361
uniprot
proteins
pubmed
21653899
uniprot
proteins
pubmed
23110240
uniprot
proteins
pubmed
25428902
uniprot
proteins
pubmed
26028554
uniprot
proteins
pubmed
27703010
uniprot
proteins
pubmed
28057442
uniprot
proteins
pubmed
28536273
uniprot
proteins
pubmed
28673968
uniprot
proteins
pubmed
29621230
uniprot
proteins
pubmed
29632817
uniprot
proteins
pubmed
31028174
uniprot
proteins
sequence_length
489
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15794747, ECO:0000269|PubMed:15863613, ECO:0000269|PubMed:16950869, ECO:0000269|PubMed:19179618}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:18270315}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:25428902, ECO:0000269|PubMed:28536273}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at the basolateral membrane of enterocytes (PubMed:25428902, PubMed:28536273). Enriched at the plasma membrane upon glucose uptake (By similarity). Localized and functional at both apical and basolateral membranes of microvascular capillary endothelial cells that constitute the blood-brain barrier (By similarity). {ECO:0000250|UniProtKB:Q15043, ECO:0000269|PubMed:25428902, ECO:0000269|PubMed:28536273}.
uniprot
proteins
transmembrane_region
TRANSMEM 156..176; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 185..205; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 222..242; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 350..370; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 395..415; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 422..442; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 458..478; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins