Ferritin

Ferritin is a universal intracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including archaea, bacteria, algae, higher plants, and animals. It is the primary intracellular iron-storage protein in both prokaryotes and eukaryotes, keeping iron in a soluble and non-toxic form. In humans, it acts as a buffer against iron deficiency and iron overload.

Ferritin
Structure of the murine ferritin complex
Identifiers
SymbolFerritin
PfamPF00210
Pfam clanCL0044
InterProIPR008331
SCOP21fha / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
ferritin, light polypeptide
Identifiers
SymbolFTL
NCBI gene2512
HGNC3999
OMIM134790
RefSeqNM_000146
UniProtP02792
Other data
LocusChr. 19 q13.3–13.4
Search for
StructuresSwiss-model
DomainsInterPro
ferritin, heavy polypeptide 1
Identifiers
SymbolFTH1
Alt. symbolsFTHL6
NCBI gene2495
HGNC3976
OMIM134770
RefSeqNM_002032
UniProtP02794
Other data
LocusChr. 11 q13
Search for
StructuresSwiss-model
DomainsInterPro
ferritin mitochondrial
Crystallographic structure of mitochondrial ferritin.
Identifiers
SymbolFTMT
NCBI gene94033
HGNC17345
OMIM608847
RefSeqNM_177478
UniProtQ8N4E7
Other data
LocusChr. 5 q23.1
Search for
StructuresSwiss-model
DomainsInterPro

Ferritin is found in most tissues as a cytosolic protein, but small amounts are secreted into the serum where it functions as an iron carrier. Plasma ferritin is also an indirect marker of the total amount of iron stored in the body; hence, serum ferritin is used as a diagnostic test for iron-deficiency anemia. Aggregated ferritin transforms into a toxic form of iron called hemosiderin.

Ferritin is a globular protein complex consisting of 24 protein subunits forming a hollow nanocage with multiple metal–protein interactions. Ferritin that is not combined with iron is called apoferritin.

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