SLC39A14
entrez
23516
canonical
uniprot
Q15043
canonical
ensembl
ENSG00000104635
resolver
ensp
ENSP00000240095
resolver
ensp
ENSP00000289952
resolver
ensp
ENSP00000352779
resolver
ensp
ENSP00000370635
resolver
ensp
ENSP00000521628
resolver
ensp
ENSP00000521629
resolver
ensp
ENSP00000521632
resolver
ensp
ENSP00000521644
resolver
ensp
ENSP00000521661
resolver
genesymbol
SLC39A14
resolver
genesymbol_syn
KIAA0062
resolver
genesymbol_syn
ZIP14
resolver
hgnc
HGNC:20858
resolver
uniprot
A0A0S2Z534
resolver
uniprot
A6NH98
resolver
uniprot
B4DIW3
resolver
uniprot
B6EU88
resolver
uniprot
D3DSR4
resolver
uniprot
Q6ZME8
resolver
uniprot
Q96BB3
resolver
uniprot_entry
A0A0S2Z534_HUMAN
resolver
uniprot_entry
S39AE_HUMAN
resolver
uniprot_sec
A6NH98
resolver
uniprot_sec
B4DIW3
resolver
uniprot_sec
B6EU88
resolver
uniprot_sec
D3DSR4
resolver
uniprot_sec
Q6ZME8
resolver
uniprot_sec
Q96BB3
resolver
amino_acid_sequence
MKLLLLHPAFQSCLLLTLLGLWRTTPEAHASSLGAPAISAASFLQDLIHRYGEGDSLTLQQLKALLNHLDVGVGRGNVTQHVQGHRNLSTCFSSGDLFTAHNFSEQSRIGSSELQEFCPTILQQLDSRACTSENQENEENEQTEEGRPSAVEVWGYGLLCVTVISLCSLLGASVVPFMKKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFNPLEDYYVSKSAVVFGGFYLFFFTEKILKILLKQKNEHHHGHSHYASESLPSKKDQEEGVMEKLQNGDLDHMIPQHCSSELDGKAPMVDEKVIVGSLSVQDLQASQSACYWLKGVRYSDIGTLAWMITLSDGLHNFIDGLAIGASFTVSVFQGISTSVAILCEEFPHELGDFVILLNAGMSIQQALFFNFLSACCCYLGLAFGILAGSHFSANWIFALAGGMFLYISLADMFPEMNEVCQEDERKGSILIPFIIQNLGLLTGFTIMVVLTMYSGQIQIG
uniprot
proteins
disease_involvement
DISEASE: Hypermanganesemia with dystonia 2 (HMNDYT2) [MIM:617013]: A metabolic autosomal recessive disorder characterized by increased blood manganese levels, neurodegeneration, and rapidly progressive parkinsonism and dystonia. Affected individuals present with loss of developmental milestones, progressive dystonia and bulbar dysfunction in infancy or early childhood. Towards the end of the first decade, they manifest severe generalized pharmacoresistant dystonia, spasticity, limb contractures and scoliosis, and loss of independent ambulation. Cognition may be impaired, but is better preserved than motor function. {ECO:0000269|PubMed:27231142}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hyperostosis cranialis interna (HCIN) [MIM:144755]: An autosomal dominant bone disorder characterized by endosteal hyperostosis and osteosclerosis of the calvaria and the skull base. The progressive bone overgrowth causes entrapment and dysfunction of cranial nerves I, II, V, VII, and VIII, its first symptoms often presenting during the second decade of life. {ECO:0000269|PubMed:29621230}. Note=The disease is caused by variants affecting the gene represented in this entry. Conditional knockin mice overexpressing Arg-438 variant, which is the mouse equivalent of human variant Leu-441, in osteoblasts have a severe skeletal phenotype marked by a drastic increase in cortical thickness due to an enhanced endosteal bone formation, resembling the underlying pathology in HCI patients. {ECO:0000269|PubMed:29621230}.
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:15642354, PubMed:27231142, PubMed:29621230). Functions as an energy-dependent symporter, transporting through the membranes an electroneutral complex composed of a divalent metal cation and two bicarbonate anions (By similarity). Beside these endogenous cellular substrates, can also import cadmium a non-essential metal which is cytotoxic and carcinogenic (By similarity). Controls the cellular uptake by the intestinal epithelium of systemic zinc, which is in turn required to maintain tight junctions and the intestinal permeability (By similarity). Modifies the activity of zinc-dependent phosphodiesterases, thereby indirectly regulating G protein-coupled receptor signaling pathways important for gluconeogenesis and chondrocyte differentiation (By similarity). 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 (By similarity). 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 (PubMed:31699897). May also play a role in manganese and zinc homeostasis participating in their elimination from the blood through the hepatobiliary excretion (By similarity). Also functions in the extracellular uptake of free iron. 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 (PubMed:23052185). {ECO:0000250|UniProtKB:Q75N73, ECO:0000269|PubMed:15642354, ECO:0000269|PubMed:20682781, ECO:0000269|PubMed:23052185, ECO:0000269|PubMed:27231142, ECO:0000269|PubMed:27703010, ECO:0000269|PubMed:29621230, ECO:0000269|PubMed:31028174, ECO:0000269|PubMed:31699897}.
uniprot
proteins
mass_dalton
54212
uniprot
proteins
mutagenesis
MUTAGEN 77; /note="N->A: Decreased N-glycosylation."; /evidence="ECO:0000269|PubMed:24927598"; MUTAGEN 87; /note="N->A: Decreased N-glycosylation."; /evidence="ECO:0000269|PubMed:24927598"; MUTAGEN 102; /note="N->A: Decreased N-glycosylation."; /evidence="ECO:0000269|PubMed:24927598
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. Ubiquitination occurs upon iron depletion. The ubiquitinated form undergoes proteasomal degradation. {ECO:0000269|PubMed:24927598}.; PTM: N-glycosylated. N-glycosylation at Asn-102 is required for iron-regulated extraction of the transporter from membranes and subsequent proteasomal degradation. {ECO:0000269|PubMed:24927598}.
uniprot
proteins
protein_family
ZIP transporter (TC 2.A.5) family
uniprot
proteins
pubmed
12659941
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15642354
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
18270315
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
20682781
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23052185
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24927598
uniprot
proteins
pubmed
27231142
uniprot
proteins
pubmed
27703010
uniprot
proteins
pubmed
28673968
uniprot
proteins
pubmed
29621230
uniprot
proteins
pubmed
31028174
uniprot
proteins
pubmed
31699897
uniprot
proteins
pubmed
7584044
uniprot
proteins
sequence_length
492
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15642354, ECO:0000269|PubMed:27231142, ECO:0000269|PubMed:27703010, ECO:0000269|PubMed:29621230}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:31699897}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:31028174, ECO:0000269|PubMed:31699897}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:20682781, ECO:0000269|PubMed:27703010}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:27703010}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:20682781}; Multi-pass membrane protein {ECO:0000255}. Note=Localized and functional at both apical and basolateral membranes of microvascular capillary endothelial cells that constitute the blood-brain barrier (PubMed:31699897). Localized at the basolateral membrane of enterocytes (PubMed:31028174). Enriched at the plasma membrane upon glucose uptake (PubMed:27703010). {ECO:0000269|PubMed:27703010, ECO:0000269|PubMed:31028174, ECO:0000269|PubMed:31699897}.
uniprot
proteins
transmembrane_region
TRANSMEM 158..178; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 187..207; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 225..245; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 398..418; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 425..445; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 461..481; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins