Kallistatin (KAL)

SERPINA4; KLST; KST; PI4; Serpin Peptidase Inhibitor Clade A Member 4; Tissue Kallikrein Inhibitor; Kallikrein Binding Protein; Peptidase inhibitor 4

SPN	T389
HGNC	8948
MGI	2448363
PubMed	11258665
UniProt	P29622
Wiki	SERPINA4

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.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 human alpha-1-antichymotrypsin (AACT), alpha-1-antitrypsin (PI), corticosteroid-binding globulin (CBG), thyroxine-binding globulin of serum (TBG), and protein C inhibitor (PCI). All of these except TBG, which is encoded by the X chromosome, are encoded by genes on chromosome 14.

Reference

"Kallistatin: a novel human serine proteinase inhibitor. Molecular cloning, tissue distribution, and expression in Escherichia coli."
J. Biol. Chem. 268:24498-24505(1993) [PubMed] [Europe PMC] [Abstract]

"Molecular cloning, sequence analysis, and chromosomal localization of the human protease inhibitor 4 (kallistatin) gene (PI4)."
Genomics 23:370-378(1994) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Kallistatin: a novel human tissue kallikrein inhibitor. Purification, characterization, and reactive center sequence."
J. Biol. Chem. 267:25873-25880(1992) [PubMed] [Europe PMC] [Abstract]

"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]

"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]