Serotransferrin (TF)
The protein contains 698 amino acids for an estimated molecular weight of 77064 Da.
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.', '(Microbial infection) Serves as an iron source for Neisseria species, which capture the protein and extract its iron for their own use. (updated: Oct. 7, 2020)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
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No binding partner found
Biological Process
Actin filament organization
Activation of JUN kinase activity
Antibacterial humoral response
Blood coagulation
Cellular iron ion homeostasis
Cellular protein metabolic process
Cellular response to iron ion
ERK1 and ERK2 cascade
Ferrous iron import across plasma membrane
Iron ion homeostasis
Iron ion transport
Membrane organization
Osteoclast differentiation
Platelet activation
Platelet degranulation
Positive regulation of bone resorption
Positive regulation of cell motility
Positive regulation of receptor-mediated endocytosis
Positive regulation of transcription, DNA-templated
Post-translational protein modification
Regulation of iron ion import
Regulation of iron ion transport
Regulation of protein stability
Response to bacterium
Retina homeostasis
SMAD protein signal transduction
Transferrin transport
Transmembrane transport
Cellular Component
Apical plasma membrane
Basal part of cell
Basal plasma membrane
Blood microparticle
Cell surface
Clathrin-coated endocytic vesicle membrane
Clathrin-coated pit
Clathrin-coated vesicle membrane
Cytoplasmic vesicle
Cytoplasmic, membrane-bounded vesicle
Early endosome
Endocytic vesicle
Endoplasmic reticulum lumen
Endosome membrane
Extracellular exosome
Extracellular region
Extracellular space
Extrinsic component of external side of plasma membrane
HFE-transferrin receptor complex
Late endosome
Obsolete cell
Perinuclear region of cytoplasm
Plasma membrane
Recycling endosome
Secretory granule lumen
Vesicle
The reference OMIM entry for this protein is 190000
Transferrin; tf
DESCRIPTION
The TF gene encodes transferrin, a circulating serum protein responsible for delivering iron to cells (Hershberger et al., 1991).CLONING
Uzan et al. (1984) isolated a clone corresponding to the human transferrin gene from a human liver cDNA library. A single major 2.4-kb mRNA species was identified. Yang et al. (1984) isolated recombinant plasmids containing human cDNA encoding TF by screening an adult human liver library with a mixed oligonucleotide probe. Sequence analysis indicated that 3 areas of the homologous amino and carboxyl domains were strongly conserved in evolution. Bost et al. (1985) identified short regions in the nucleotide and amino acid sequences of epidermal growth factor (EGF; 131530), interleukin-2 (IL2; 147680), and transferrin that matched short regions in their respective receptor complements (antisense strand) and their deduced amino acid sequences. In each case, the region of homology of the receptor was in sequences external to the cytoplasmic membrane that might qualify for the ligand binding site. Hershberger et al. (1991) cloned the human TF gene and determined that the deduced protein contains 678 residues and 19 disulfide bonds, with a molecular mass of about 80 kD.MAPPING
Robson et al. (1966) presented evidence of linkage between the transferrin locus and the pseudocholinesterase locus E1 (CHE1, BCHE; 177400). Naylor et al. (1980) suggested that the TF-CHE1 linkage group may be on chromosome 3 in man since aminoacylase (ACY1; 104620) and beta-galactosidase-1 (GLB1; 611458) are on chromosome 3 in man and on chromosome 9 in the mouse, and since Tf is closely linked to Acy1 and Glb1 in the mouse, By somatic cell hybridization, using a monoclonal antibody to demonstrate the synthesis of transferrin, Bodmer (1981) assigned transferrin to chromosome 3. Lactotransferrin (LTF; 150210), found in milk of many mammals including man, is structurally similar to serum transferrin and is coded by a gene on chromosome 3p. Interestingly and perhaps significantly, the gene for the transferrin receptor (TFRC; 190010) is also on chromosome 3q29. Eiberg et al. (1984) found a low positive lod score at a recombination fraction of about 0.23 for linkage of TF to heteromorphism at the centromere of chromosome 3. Since CHE1 and A2HS (104210) showed negative lod scores, these are possibly distal to TF on chromosome 3. Yang et al. (1984) mapped the TF gene to chromosome 3q21-q25 by in situ hybridization and analysis of somatic cell hybrids. Huerre et al. (1984) confirmed these findings. Through linkage studies in a large Newfoundland kindred segregating for an inversion, inv(3)(p25q21), McAlpine et al. (1987) determined the order to be: cen--3q21--TF--CHE1--AHSG (138680)--qter. By in situ hybridization, Baranov et al. (1987) assigned the TF gene to 3q21. They mapped both the CP (117700) and TF genes to chromosome 9 in the mouse and chromosome 7 in rats. In rats, they also observed a concentration of silver grains over chromosome 15 after hybridization with both CP and TF probes, suggesting the presence of a related pseudogene cluster on rat chromosome 15 and favoring partial homeology to rat chromosome 7. Use of a rat CP DNA probe appeared to contradict synteny of CP and TF in man and suggested the existence of a related DNA sequence on 15q11-q13.GENE FUNCTION
Transferrin is the product of an ancient intragenic duplication that led to homologous carboxyl and amino domains, ... More on the omim web site
Oct. 20, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for TF
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 190000 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed