P09528 · FRIH_MOUSE
- ProteinFerritin heavy chain
- GeneFth1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids182 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Stores iron in a soluble, non-toxic, readily available form (By similarity).
Important for iron homeostasis (By similarity).
Has ferroxidase activity (By similarity).
Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).
Also plays a role in delivery of iron to cells (PubMed:19154717).
Mediates iron uptake in capsule cells of the developing kidney (PubMed:19154717).
Degraded to release iron upon autophagy activation by nutrient starvation (PubMed:25327288).
Important for iron homeostasis (By similarity).
Has ferroxidase activity (By similarity).
Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).
Also plays a role in delivery of iron to cells (PubMed:19154717).
Mediates iron uptake in capsule cells of the developing kidney (PubMed:19154717).
Degraded to release iron upon autophagy activation by nutrient starvation (PubMed:25327288).
Catalytic activity
- 4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 28 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 63 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 63 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 66 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 108 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 142 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | autolysosome | |
Cellular Component | autophagosome | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endocytic vesicle lumen | |
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Cellular Component | mitochondrion | |
Molecular Function | ferric iron binding | |
Molecular Function | ferrous iron binding | |
Molecular Function | ferroxidase activity | |
Molecular Function | identical protein binding | |
Molecular Function | iron ion binding | |
Molecular Function | iron ion sequestering activity | |
Biological Process | immune response | |
Biological Process | intracellular sequestering of iron ion | |
Biological Process | iron ion transport | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | negative regulation of ferroptosis | |
Biological Process | negative regulation of fibroblast proliferation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFerritin heavy chain
- EC number
- Short namesFerritin H subunit
- Cleaved into 1 chains
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 accessionP09528
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Homozygous mutant embryos die in utero between 3.5 and 9.5 dpc (PubMed:10652280).
Heterozygous animals are healthy and fertile and do not present any apparent abnormalities. They show slightly elevated tissue light chain ferritin content and 7- to 10-fold more light chain ferritin in the serum than normal mice, but their serum iron remains unchanged
Heterozygous animals are healthy and fertile and do not present any apparent abnormalities. They show slightly elevated tissue light chain ferritin content and 7- to 10-fold more light chain ferritin in the serum than normal mice, but their serum iron remains unchanged
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 21 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed; alternate | ||||
Sequence: M | ||||||
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000424473 | 1-182 | Ferritin heavy chain | |||
Sequence: MTTASPSQVRQNYHQDAEAAINRQINLELYASYVYLSMSCYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDRDDWESGLNAMECALHLEKSVNQSLLELHKLATDKNDPHLCDFIETYYLSEQVKSIKELGDHVTNLRKMGAPEAGMAEYLFDKHTLGHGDES | ||||||
Modified residue | 2 | N-acetylthreonine; in Ferritin heavy chain, N-terminally processed | ||||
Sequence: T | ||||||
Chain | PRO_0000201049 | 2-182 | Ferritin heavy chain, N-terminally processed | |||
Sequence: TTASPSQVRQNYHQDAEAAINRQINLELYASYVYLSMSCYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDRDDWESGLNAMECALHLEKSVNQSLLELHKLATDKNDPHLCDFIETYYLSEQVKSIKELGDHVTNLRKMGAPEAGMAEYLFDKHTLGHGDES |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Developmental stage
At 9.5 dpc, detected at low levels in the developing heart and central nervous system. At later stages of development, widely expressed, predominantly in the heart and brown fat tissue.
Gene expression databases
Interaction
Subunit
Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited. Interacts with NCOA4; NCOA4 promotes targeting of the iron-binding ferritin complex to autolysosomes following starvation or iron depletion (PubMed:25327288).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P09528 | Fth1 P09528 | 3 | EBI-308950, EBI-308950 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-160 | Ferritin-like diiron | ||||
Sequence: QNYHQDAEAAINRQINLELYASYVYLSMSCYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDRDDWESGLNAMECALHLEKSVNQSLLELHKLATDKNDPHLCDFIETYYLSEQVKSIKELGDHVTNLRKMG |
Sequence similarities
Belongs to the ferritin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length182
- Mass (Da)21,067
- Last updated2007-01-23 v2
- Checksum129A8887A2BC650B
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A494B9D4 | A0A494B9D4_MOUSE | Fth1 | 116 | ||
A0A494BAP3 | A0A494BAP3_MOUSE | Fth1 | 59 | ||
A0A494BA92 | A0A494BA92_MOUSE | Fth1 | 136 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 17 | in Ref. 5; AAA37612 | ||||
Sequence: A → S | ||||||
Sequence conflict | 137 | in Ref. 5; AAA37612 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 140 | in Ref. 5; AAA37612 | ||||
Sequence: S → N | ||||||
Sequence conflict | 164 | in Ref. 5; AAA37612 | ||||
Sequence: A → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X52561 EMBL· GenBank· DDBJ | CAA36795.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X12812 EMBL· GenBank· DDBJ | CAA31300.1 EMBL· GenBank· DDBJ | mRNA | ||
J03941 EMBL· GenBank· DDBJ | AAA37611.1 EMBL· GenBank· DDBJ | mRNA | ||
M60170 EMBL· GenBank· DDBJ | AAA37613.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M24509 EMBL· GenBank· DDBJ | AAA37612.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027998 EMBL· GenBank· DDBJ | BAC25694.1 EMBL· GenBank· DDBJ | mRNA | ||
AK139622 EMBL· GenBank· DDBJ | BAE24084.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147082 EMBL· GenBank· DDBJ | BAE27662.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150262 EMBL· GenBank· DDBJ | BAE29419.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150508 EMBL· GenBank· DDBJ | BAE29621.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150628 EMBL· GenBank· DDBJ | BAE29718.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150679 EMBL· GenBank· DDBJ | BAE29759.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150693 EMBL· GenBank· DDBJ | BAE29772.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151192 EMBL· GenBank· DDBJ | BAE30189.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151241 EMBL· GenBank· DDBJ | BAE30233.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151399 EMBL· GenBank· DDBJ | BAE30367.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151609 EMBL· GenBank· DDBJ | BAE30548.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151675 EMBL· GenBank· DDBJ | BAE30600.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152071 EMBL· GenBank· DDBJ | BAE30924.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152542 EMBL· GenBank· DDBJ | BAE31297.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152702 EMBL· GenBank· DDBJ | BAE31431.1 EMBL· GenBank· DDBJ | mRNA | ||
AK153017 EMBL· GenBank· DDBJ | BAE31651.1 EMBL· GenBank· DDBJ | mRNA | ||
AK153195 EMBL· GenBank· DDBJ | BAE31795.1 EMBL· GenBank· DDBJ | mRNA | ||
AK153199 EMBL· GenBank· DDBJ | BAE31799.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159243 EMBL· GenBank· DDBJ | BAE34925.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168601 EMBL· GenBank· DDBJ | BAE40468.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169004 EMBL· GenBank· DDBJ | BAE40803.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012314 EMBL· GenBank· DDBJ | AAH12314.1 EMBL· GenBank· DDBJ | mRNA |