Q9NP59: Ferroportin (SLC40A1)

Ferroportin (SLC40A1) is a 571-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NP59.

Gene
SLC40A1
Organism
Homo sapiens
Length
571 residues
Mean pLDDT
80.3
Model
AF-Q9NP59-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate54%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Transports Fe(2+) from the inside of a cell to the outside of the cell, playing a key role for maintaining systemic iron homeostasis (PubMed:15692071, PubMed:22178646, PubMed:22682227, PubMed:24304836, PubMed:29237594, PubMed:29599243, PubMed:30247984). Transports iron from intestinal, splenic, hepatic cells, macrophages and erythrocytes into the blood to provide iron to other tissues (By similarity). Controls therefore dietary iron uptake, iron recycling by macrophages and erythrocytes, and release of iron stores in hepatocytes (By similarity). When iron is in excess in serum, circulating HAMP/hepcidin levels increase resulting in a degradation of SLC40A1, thus limiting the iron efflux to…

Subunit structure

Identified in a complex with STOM (PubMed:23219802). 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 (PubMed:22682227, PubMed:29237594, PubMed:32814342). Part of a complex composed of SLC40A1/ferroportin, TF/transferrin and HEPH/hephaestin that transfers iron…

Subcellular location

Cell membrane, Basolateral cell membrane

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6WBVEM2.5 ÅA=1-571
8DL7EM2.7 ÅA=1-571
8DL6EM3.0 ÅA=1-571
8DL8EM3.0 ÅA=1-571
6W4SEM3.2 ÅF=1-571
8BZYEM3.24 ÅA=2-571
8C03EM3.89 ÅA=2-571
8C02EM4.09 ÅA=2-571

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