Kallistatin (SERPINA4)
The protein contains 427 amino acids for an estimated molecular weight of 48542 Da.
Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein. (updated: March 4, 2015)
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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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.
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No binding partner found
Cellular Component
Extracellular exosome
Extracellular region
Extracellular space
Platelet dense granule lumen
The reference OMIM entry for this protein is 147935
Serpin peptidase inhibitor, clade a, member 4; serpina4
Kallistatin; kst
Tissue kallikrein inhibitor
Protease inhibitor 4; pi4
CLONING
Zhou et al. (1992) purified and characterized a human tissue kallikrein inhibitor from plasma which rapidly bound to tissue kallikrein and inhibited its activity. Designated kallistatin, this tissue kallikrein inhibitor is a member of the serpin superfamily and represents a major inhibitor of human tissue kallikrein in the circulation. Chai et al. (1993) cloned a full-length SERPINA4 cDNA encoding kallistatin from human liver RNA by PCR. The 1,284-bp cDNA encodes 427 amino acid residues, including a 26-residue signal peptide and a 401-residue mature peptide. The translated amino acid sequence of kallistatin matches the protein sequence and shares 44 to 46% sequence identity with other serpin family members including, human alpha-1-antichymotrypsin (AACT; 107280), alpha-1-antitrypsin (PI; 107400), corticosteroid-binding globulin (CBG; 122500), thyroxine-binding globulin of serum (TBG; 314200), and protein C inhibitor (PCI; 601841).MAPPING
By screening a chromosome 14-specific genomic DNA library, Chai et al. (1993) localized the SERPINA4 gene to chromosome 14. By FISH analysis, Chai et al. (1994) localized the SERPINA4 gene to chromosome 14q31-q32.1, close to the serpin genes AACT, PCI, PI, and CBG.GENE FUNCTION
Kallistatin is a serine proteinase inhibitor (serpin) and a heparin-binding protein. It is localized in vascular smooth muscle cells and endothelial cells of blood vessels, suggesting that it may be involved in the regulation of vascular function. Miao et al. (2000) showed that kallistatin plays a role in neointima hyperplasia. Miao et al. (2002) investigated the potential role of kallistatin in angiogenesis in vitro and in vivo, and presented results demonstrating a novel role of the protein in the inhibition of angiogenesis and tumor growth. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for SERPINA4
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 147935 was added.