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transferrin
ProteinQ410473· pop 28· linked from 303 articles

transferrin

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Also known as beta-1 metal-binding globulin, epididymis secretory sperm binding protein Li 71p, TF, siderophilin, serotransferrin

Transferrins are glycoproteins found in vertebrates which bind and consequently mediate the transport of iron (Fe) through blood plasma. They are produced in the liver and contain binding sites for two Fe3+ ions. Human transferrin is encoded by the TF gene and produced as a 76 kDa glycoprotein.

Key facts

Protein family.Symbol
Transferrin
Protein family.Name
Transferrin
Protein family.Pfam
PF00405
Protein family.InterPro
IPR001156
Protein family.Prosite
PDOC00182
Protein family.SCOP
1lcf

via Wikipedia infobox

Protein · UniProt

Serotransferrin

Gene
TF
Organism
Homo sapiens (Human)
Length
698 aa
Molecular mass
77,064 Da
Evidence
1: Evidence at protein level

Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation

3D-structureDirect protein sequencingDisease variantDisulfide bondGlycoproteinIon transportIronIron transport
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Swiss-Prot (reviewed) · via UniProt

Clinical Trials

42 registered

via ClinicalTrials.gov

Wikidata facts

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Commons category
Transferrin
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via Wikidata · CC0

~10 min read

Article

16 sections
Contents
  • Occurrence and function
  • Humans and other mammals
  • Other species
  • Structure
  • Immune system
  • Role in disease
  • Transferrin and nanomedicine
  • Other effects
  • Pathology
  • Reference ranges
  • Interactions
  • Related proteins
  • See also
  • References
  • Further reading
  • External links

Transferrins are glycoproteins found in vertebrates which bind and consequently mediate the transport of iron (Fe) through blood plasma. They are produced in the liver and contain binding sites for two Fe3+ ions. Human transferrin is encoded by the TF gene and produced as a 76 kDa glycoprotein.

Transferrin glycoproteins bind iron tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of total body iron, it forms the most vital iron pool with the highest rate of turnover (25 mg/24 h). Transferrin has a molecular weight of around 80 kDa and contains two specific high-affinity Fe(III) binding sites. The affinity of transferrin for Fe(III) is extremely high (association constant is 1020 M−1 at pH 7.4) but decreases progressively with decreasing pH below neutrality. Transferrins are not limited to only binding to iron but also to different metal ions. These glycoproteins are located in various bodily fluids of vertebrates. Some invertebrates have proteins that act like transferrin found in the hemolymph.

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