Q9JHI9 · S40A1_MOUSE
- ProteinFerroportin
- GeneSlc40a1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids570 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transports Fe2+ from the inside of a cell to the outside of the cell, playing a key role for maintaining systemic iron homeostasis (PubMed:16054062, PubMed:30213870).
Transports iron from intestinal, splenic, hepatic cells, macrophages and erythrocytes into the blood to provide iron to other tissues. Controls therefore dietary iron uptake, iron recycling by macrophages and erythrocytes, and release of iron stores in hepatocytes (PubMed:16054062, PubMed:30213870).
When iron is in excess in serum, circulating HAMP/hepcidin levels increase resulting in a degradation of SLC40A1, thus limiting the iron efflux to plasma (By similarity).
Transports iron from intestinal, splenic, hepatic cells, macrophages and erythrocytes into the blood to provide iron to other tissues. Controls therefore dietary iron uptake, iron recycling by macrophages and erythrocytes, and release of iron stores in hepatocytes (PubMed:16054062, PubMed:30213870).
When iron is in excess in serum, circulating HAMP/hepcidin levels increase resulting in a degradation of SLC40A1, thus limiting the iron efflux to plasma (By similarity).
Catalytic activity
- Fe2+(in) = Fe2+(out)
Features
Showing features for binding site.
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameFerroportin
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9JHI9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Basolateral cell membrane ; Multi-pass membrane protein
Note: Localized to the basolateral membrane of polarized epithelial cells.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-23 | Cytoplasmic | ||||
Sequence: MTKARDQTHQEGCCGSLANYLTS | ||||||
Transmembrane | 24-53 | Helical | ||||
Sequence: AKFLLYLGHSLSTWGDRMWHFAVSVFLVEL | ||||||
Topological domain | 54-57 | Extracellular | ||||
Sequence: YGNS | ||||||
Transmembrane | 58-84 | Helical | ||||
Sequence: LLLTAVYGLVVAGSVLVLGAIIGDWVD | ||||||
Topological domain | 85-87 | Cytoplasmic | ||||
Sequence: KNA | ||||||
Transmembrane | 88-118 | Helical | ||||
Sequence: RLKVAQTSLVVQNVSVILCGIILMMVFLHKN | ||||||
Topological domain | 119-126 | Extracellular | ||||
Sequence: ELLTMYHG | ||||||
Transmembrane | 127-162 | Helical | ||||
Sequence: WVLTVCYILIITIANIANLASTATAITIQRDWIVVV | ||||||
Topological domain | 163-164 | Cytoplasmic | ||||
Sequence: AG | ||||||
Transmembrane | 165-195 | Helical | ||||
Sequence: ENRSRLADMNATIRRIDQLTNILAPMAVGQI | ||||||
Topological domain | 196-202 | Extracellular | ||||
Sequence: MTFGSPV | ||||||
Transmembrane | 203-229 | Helical | ||||
Sequence: IGCGFISGWNLVSMCVEYFLLWKVYQK | ||||||
Topological domain | 230-306 | Cytoplasmic | ||||
Sequence: TPALAVKAALKVEESELKQLTSPKDTEPKPLEGTHLMGEKDSNIRELECEQEPTCASQMAEPFRTFRDGWVSYYNQP | ||||||
Transmembrane | 307-333 | Helical | ||||
Sequence: VFLAGMGLAFLYMTVLGFDCITTGYAY | ||||||
Topological domain | 334-338 | Extracellular | ||||
Sequence: TQGLS | ||||||
Transmembrane | 339-366 | Helical | ||||
Sequence: GSILSILMGASAITGIMGTVAFTWLRRK | ||||||
Topological domain | 367-368 | Cytoplasmic | ||||
Sequence: CG | ||||||
Transmembrane | 369-391 | Helical | ||||
Sequence: LVRTGLFSGLAQLSCLILCVISV | ||||||
Topological domain | 392-452 | Extracellular | ||||
Sequence: FMPGSPLDLSVSPFEDIRSRFVNVEPVSPTTKIPETVFTTEMHMSNMSNVHEMSTKPIPIV | ||||||
Transmembrane | 453-482 | Helical | ||||
Sequence: SVSLLFAGVIAARIGLWSFDLTVTQLLQEN | ||||||
Topological domain | 483-487 | Cytoplasmic | ||||
Sequence: VIESE | ||||||
Transmembrane | 488-512 | Helical | ||||
Sequence: RGIINGVQNSMNYLLDLLHFIMVIL | ||||||
Topological domain | 513-515 | Extracellular | ||||
Sequence: APN | ||||||
Transmembrane | 516-541 | Helical | ||||
Sequence: PEAFGLLVLISVSFVAMGHLMYFRFA | ||||||
Topological domain | 542-570 | Cytoplasmic | ||||
Sequence: QKTLGNQIFVCGPDEKEVTDENQPNTSVV |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Deficient mice exhibit embryonic lethality. These mice cannot transfer iron from the extraembryonic visceral endoderm into the embryo proper, leading to a defect in embryonic growth and consequent death (PubMed:16054062).
Erythroid-specific deletion reduces serum iron but increased tissue iron contents (PubMed:30213870).
Erythroid-specific deletion reduces serum iron but increased tissue iron contents (PubMed:30213870).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 50 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000191311 | 1-570 | Ferroportin | |||
Sequence: MTKARDQTHQEGCCGSLANYLTSAKFLLYLGHSLSTWGDRMWHFAVSVFLVELYGNSLLLTAVYGLVVAGSVLVLGAIIGDWVDKNARLKVAQTSLVVQNVSVILCGIILMMVFLHKNELLTMYHGWVLTVCYILIITIANIANLASTATAITIQRDWIVVVAGENRSRLADMNATIRRIDQLTNILAPMAVGQIMTFGSPVIGCGFISGWNLVSMCVEYFLLWKVYQKTPALAVKAALKVEESELKQLTSPKDTEPKPLEGTHLMGEKDSNIRELECEQEPTCASQMAEPFRTFRDGWVSYYNQPVFLAGMGLAFLYMTVLGFDCITTGYAYTQGLSGSILSILMGASAITGIMGTVAFTWLRRKCGLVRTGLFSGLAQLSCLILCVISVFMPGSPLDLSVSPFEDIRSRFVNVEPVSPTTKIPETVFTTEMHMSNMSNVHEMSTKPIPIVSVSLLFAGVIAARIGLWSFDLTVTQLLQENVIESERGIINGVQNSMNYLLDLLHFIMVILAPNPEAFGLLVLISVSFVAMGHLMYFRFAQKTLGNQIFVCGPDEKEVTDENQPNTSVV | ||||||
Glycosylation | 437 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Polyubiquitinated by RNF217; leading to proteasomal degradation (PubMed:33895792).
Under conditions of high systemic iron levels, both the hormone peptide hepcidin/HAMP and holo(iron bound)-transferrin/TF induce the ubiquitination, internalization and proteasomal degradation of SLC40A1 to control iron release from cells (By similarity).
Under conditions of high systemic iron levels, both the hormone peptide hepcidin/HAMP and holo(iron bound)-transferrin/TF induce the ubiquitination, internalization and proteasomal degradation of SLC40A1 to control iron release from cells (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
High expression in spleen, liver, kidney, heart and duodenum.
Gene expression databases
Interaction
Subunit
Identified in a complex with STOM. Interacts with HAMP; affinity of the peptide hormone HAMP for SLC40A1 increases by 80-fold in the presence of iron and the interaction promotes SLC40A1 ubiquitination and degradation. Part of a complex composed of SLC40A1/ferroportin, TF/transferrin and HEPH/hephaestin that transfers iron from cells to transferrin.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9JHI9 | App P12023 | 2 | EBI-2931424, EBI-78814 | |
XENO | Q9JHI9 | JAK2 O60674 | 3 | EBI-2931424, EBI-518647 | |
BINARY | Q9JHI9 | Slc40a1 Q9JHI9 | 2 | EBI-2931424, EBI-2931424 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length570
- Mass (Da)62,702
- Last updated2000-10-01 v1
- Checksum7125CC6171394A0A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C5H8V4 | C5H8V4_MOUSE | Slc40a1 | 70 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF215637 EMBL· GenBank· DDBJ | AAF80987.1 EMBL· GenBank· DDBJ | mRNA | ||
AF216834 EMBL· GenBank· DDBJ | AAF82036.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF226613 EMBL· GenBank· DDBJ | AAF36696.1 EMBL· GenBank· DDBJ | mRNA | ||
AF231120 EMBL· GenBank· DDBJ | AAF44329.1 EMBL· GenBank· DDBJ | mRNA | ||
AK008700 EMBL· GenBank· DDBJ | BAB25840.1 EMBL· GenBank· DDBJ | mRNA | ||
AK032732 EMBL· GenBank· DDBJ | BAC28001.1 EMBL· GenBank· DDBJ | mRNA | ||
AK083288 EMBL· GenBank· DDBJ | BAC38844.1 EMBL· GenBank· DDBJ | mRNA | ||
AK144780 EMBL· GenBank· DDBJ | BAE26063.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147137 EMBL· GenBank· DDBJ | BAE27707.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159294 EMBL· GenBank· DDBJ | BAE34969.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159855 EMBL· GenBank· DDBJ | BAE35431.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003438 EMBL· GenBank· DDBJ | AAH03438.1 EMBL· GenBank· DDBJ | mRNA |