Q9D856 · S39A5_MOUSE
- ProteinZinc transporter ZIP5
- GeneSlc39a5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids535 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Uniporter that transports zinc2+ into polarized cells of enterocytes, pancreatic acinar and endoderm cells across the basolateral membrane and participates, notably, in zinc excretion from the intestine by the uptake of zinc from the blood into the intestine (PubMed:15322118, PubMed:24303081).
The transport mechanism is temperature- and concentration-dependent and saturable (PubMed:15322118).
In addition, is also a high affinity copper transporter in vitro (By similarity).
Also may regulate glucose-stimulated insulin secretion (GSIS) in islets primarily through the zinc-activated SIRT1-PPARGC1A axis (PubMed:30324491).
Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera (By similarity).
Plays a role in eye development (By similarity).
The transport mechanism is temperature- and concentration-dependent and saturable (PubMed:15322118).
In addition, is also a high affinity copper transporter in vitro (By similarity).
Also may regulate glucose-stimulated insulin secretion (GSIS) in islets primarily through the zinc-activated SIRT1-PPARGC1A axis (PubMed:30324491).
Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera (By similarity).
Plays a role in eye development (By similarity).
Catalytic activity
- Zn2+(in) = Zn2+(out)
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.7 μM | Zn2+ | in HEK293 cells transfected | ||||
2.1 μM | Zn2+ | in the endogenous system in HEK293 cells |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
13.2 pmol/min/mg | undefined (in HEK293 cells transfected) | ||||
4.1 pmol/min/mg | undefined (in the endogenous system in HEK293 cells) |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | basolateral plasma membrane | |
Cellular Component | plasma membrane | |
Molecular Function | monoatomic cation:bicarbonate symporter activity | |
Molecular Function | zinc ion transmembrane transporter activity | |
Biological Process | angiogenesis | |
Biological Process | BMP signaling pathway | |
Biological Process | cellular response to zinc ion starvation | |
Biological Process | eye development | |
Biological Process | intracellular monoatomic cation homeostasis | |
Biological Process | intracellular zinc ion homeostasis | |
Biological Process | positive regulation of mRNA splicing, via spliceosome | |
Biological Process | zinc ion import across plasma membrane | |
Biological Process | zinc ion transmembrane transport | |
Biological Process | zinc ion transport |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameZinc transporter ZIP5
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9D856
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Basolateral cell membrane ; Multi-pass membrane protein
Note: Localized to the basolateral surfaces of enterocytes, pancreatic acinar and endoderm cells (PubMed:15358787).
During zinc deficiency diet, the basolateral cell membrane localization is lost in the intestine, the visceral yolk sac and acinar cell (PubMed:15358787).
During zinc repletion, is relocalized to the basolateral membrane of enterocytes, visceral endoderm cells and pancreatic acinar cells (PubMed:18020946).
Zinc can regulate the turnover of protein at the membrane (PubMed:18020946).
During zinc deficiency, is internalized and degraded in enterocytes, acinar cells and endoderm cells (PubMed:18020946).
Endocytosed through the endolysosomal degradation pathway RAB5A pathway (PubMed:24039764).
During zinc deficiency diet, the basolateral cell membrane localization is lost in the intestine, the visceral yolk sac and acinar cell (PubMed:15358787).
During zinc repletion, is relocalized to the basolateral membrane of enterocytes, visceral endoderm cells and pancreatic acinar cells (PubMed:18020946).
Zinc can regulate the turnover of protein at the membrane (PubMed:18020946).
During zinc deficiency, is internalized and degraded in enterocytes, acinar cells and endoderm cells (PubMed:18020946).
Endocytosed through the endolysosomal degradation pathway RAB5A pathway (PubMed:24039764).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-210 | Extracellular | ||||
Sequence: WVGGSVPNLGPAEQEQNHYLAQLFGLYGENGTLTAGGLARLLHSLGLGRVQGLRLGHHEPPTGRAAPTSGDNFTHRLQEPELSVDIWAGMPLGPSGWGDQEESKAPDLHGSGPSSLDLFQRLLLLDHSLADHLNEDCLNGSQLLVNFGLSPVAPLTPRQFALLCPALLYQIDSRVCIKTPAPAPPGDVLSA | ||||||
Transmembrane | 211-231 | Helical | ||||
Sequence: LLHSGLAVLFLSLPAPLSLLL | ||||||
Topological domain | 232-242 | Cytoplasmic | ||||
Sequence: LRLLGPRLLRP | ||||||
Transmembrane | 243-263 | Helical | ||||
Sequence: VLGFLGALAVGTLCGDALLHL | ||||||
Topological domain | 264-285 | Extracellular | ||||
Sequence: LPHAQGGRHTGPSEQSEEDLGP | ||||||
Transmembrane | 286-306 | Helical | ||||
Sequence: GLSVLGGLFLLFMLENTLGLV | ||||||
Topological domain | 307-439 | Cytoplasmic | ||||
Sequence: RHRGLRPRCCRNKRDLGEPNPDPEDGSGMVLRPLQAASEPEVQGQRENRQSSPSLAPPGHQGHSHEHRGGSIAWMVLLGDCLHNLTDGLALGAAFSDGFSSGLSTTLAVFCHELPHELGDFAMLLQEGLSFRK | ||||||
Transmembrane | 440-460 | Helical | ||||
Sequence: LLLLSLVSGALGLGGAALGVG | ||||||
Topological domain | 461-465 | Extracellular | ||||
Sequence: LSLGP | ||||||
Transmembrane | 466-486 | Helical | ||||
Sequence: VPLTPWVFGTTAGVFLYVALV | ||||||
Topological domain | 487-503 | Cytoplasmic | ||||
Sequence: DMLPTLLRPPEPLPVFH | ||||||
Transmembrane | 504-524 | Helical | ||||
Sequence: VLLQGLGLLLGGSLMFTIALL | ||||||
Topological domain | 525-535 | Extracellular | ||||
Sequence: EEQLVPTVPDG |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Homozygous knockout mice lacking Slc39a5 display normal fecondity and seem normal.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 38 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MGPPVHHLLTGLCVGVALG | ||||||
Chain | PRO_0000045796 | 20-535 | Zinc transporter ZIP5 | |||
Sequence: WVGGSVPNLGPAEQEQNHYLAQLFGLYGENGTLTAGGLARLLHSLGLGRVQGLRLGHHEPPTGRAAPTSGDNFTHRLQEPELSVDIWAGMPLGPSGWGDQEESKAPDLHGSGPSSLDLFQRLLLLDHSLADHLNEDCLNGSQLLVNFGLSPVAPLTPRQFALLCPALLYQIDSRVCIKTPAPAPPGDVLSALLHSGLAVLFLSLPAPLSLLLLRLLGPRLLRPVLGFLGALAVGTLCGDALLHLLPHAQGGRHTGPSEQSEEDLGPGLSVLGGLFLLFMLENTLGLVRHRGLRPRCCRNKRDLGEPNPDPEDGSGMVLRPLQAASEPEVQGQRENRQSSPSLAPPGHQGHSHEHRGGSIAWMVLLGDCLHNLTDGLALGAAFSDGFSSGLSTTLAVFCHELPHELGDFAMLLQEGLSFRKLLLLSLVSGALGLGGAALGVGLSLGPVPLTPWVFGTTAGVFLYVALVDMLPTLLRPPEPLPVFHVLLQGLGLLLGGSLMFTIALLEEQLVPTVPDG | ||||||
Glycosylation | 49 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 158 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 333 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 371 | Pros-methylhistidine | ||||
Sequence: H |
Post-translational modification
N-Glycosylated.
Methylated at His-371 by METTL9.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all stages of eye development and primarily in the sclera and several layers of the retina, including the inner segment, outer plexiform layer and ganglion cell layer (PubMed:24891338).
Expressed in pancreas, kidney and the proximal and distal small intestine as well as in the embryonic visceral yolk sac (PubMed:15358787).
In the proximal intestine, expression is predominant in the crypts but diminishes toward the apical regions of the villi (PubMed:15358787).
Expressed in pancreas, kidney and the proximal and distal small intestine as well as in the embryonic visceral yolk sac (PubMed:15358787).
In the proximal intestine, expression is predominant in the crypts but diminishes toward the apical regions of the villi (PubMed:15358787).
Induction
Induced in a zinc-responsive manner (PubMed:18020946).
During zinc deficiency, the transcript remains associated with polysomes and is rapidly resynthesized and targeted to the basolateral membranes of these cell types after zinc-repletion (PubMed:18020946).
During zinc deficiency, the transcript remains associated with polysomes and is rapidly resynthesized and targeted to the basolateral membranes of these cell types after zinc-repletion (PubMed:18020946).
Developmental stage
Expressed at 10 dpc, postnatal day P0, P13 and adult.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 316-373 | Disordered | ||||
Sequence: CRNKRDLGEPNPDPEDGSGMVLRPLQAASEPEVQGQRENRQSSPSLAPPGHQGHSHEH | ||||||
Compositional bias | 347-364 | Polar residues | ||||
Sequence: EVQGQRENRQSSPSLAPP |
Sequence similarities
Belongs to the ZIP transporter (TC 2.A.5) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length535
- Mass (Da)56,275
- Last updated2001-06-01 v1
- Checksum272204D17B2E66CD
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1W2P7Q2 | A0A1W2P7Q2_MOUSE | Slc39a5 | 114 | ||
A0A1W2P7R0 | A0A1W2P7R0_MOUSE | Slc39a5 | 176 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 137 | in Ref. 1; BAB25054 | ||||
Sequence: L → R | ||||||
Sequence conflict | 332 | in Ref. 1; BAB25054 | ||||
Sequence: G → V | ||||||
Compositional bias | 347-364 | Polar residues | ||||
Sequence: EVQGQRENRQSSPSLAPP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK007473 EMBL· GenBank· DDBJ | BAB25054.1 EMBL· GenBank· DDBJ | mRNA | ||
AK008448 EMBL· GenBank· DDBJ | BAB25675.1 EMBL· GenBank· DDBJ | mRNA | ||
BC028990 EMBL· GenBank· DDBJ | AAH28990.1 EMBL· GenBank· DDBJ | mRNA |