Kallistatin

Name	Kallistatin
Synonyms	Kallikrein inhibitor KST Peptidase inhibitor 4 PI-4 PI4 Serpin A4
Gene Name	SERPINA4
Organism	Human
Amino acid sequence	>lcl\|BSEQ0049846\|Kallistatin MHLIDYLLLLLVGLLALSHGQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAF RFYYLIASETPGKNIFFSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRG FQHLLHTLNLPGHGLETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQ LINDHVKKETRGKIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTT VRVPMMLQDQEHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMR WNNLLRKRNFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEAS KSFHKATLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGK VVDPTKP
Number of residues	None
Molecular Weight	48541.51
Theoretical pI	None
GO Classification	Functions serine-type endopeptidase inhibitor activity Processes platelet degranulation Components extracellular region extracellular space extracellular exosome platelet dense granule lumen
General Function	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.
Specific Function	Serine-type endopeptidase inhibitor activity
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P29622
UniProtKB Entry Name
Cellular Location	Secreted
Gene sequence	>lcl\|BSEQ0049847\|Kallistatin (SERPINA4) ATGCATCTTATCGACTACCTGCTCCTCCTGCTGGTTGGACTACTGGCCCTTTCTCATGGC CAGCTGCACGTTGAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGCAGATTCTG GAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGACTTTGCCTTC CGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTTTTCTCCCCGCTG AGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCACACAGCCGCAGCCAG ATCCTTGAGGGCCTGGGCTTCAACCTCACCGAGCTGTCTGAGTCCGATGTCCATAGGGGC TTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGGCTGGAAACACGCGTGGGC AGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAAAATTCCTGAATGACACCATG GCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTACGACACTGTGGGCACAATCCAG CTTATCAACGACCACGTCAAGAAGGAAACTCGAGGGAAGATTGTGGATTTGGTCAGTGAG CTCAAGAAGGACGTCTTGATGGTGCTGGTGAATTACATTTACTTCAAAGCCCTGTGGGAG AAACCATTCATTTCCTCAAGGACCACTCCCAAAGACTTCTATGTTGATGAGAACACAACA GTCCGGGTGCCCATGATGCTGCAGGACCAGGAGCATCACTGGTATCTTCATGACAGATAC TTGCCCTGCTCGGTGCTACGGATGGATTACAAAGGAGACGCAACCGTGTTTTTCATTCTC CCTAACCAAGGCAAAATGAGGGAGATTGAAGAGGTTCTGACTCCAGAGATGCTAATGAGG TGGAACAACTTGTTGCGGAAGAGGAATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAG TTCTCCATTTCTGGCTCCTATGTATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGAT CTGTTCTCCAAGTGGGCTGACTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCC AAAAGTTTCCACAAGGCCACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCC ACCAGCTTCGCGATCAAATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAAC CGGCCCTTCCTTGTGGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAG GTCGTCGACCCCACGAAACCATAG
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	14
Locus	14q32.13
References	Chai KX, Chen LM, Chao J, Chao L: Kallistatin: a novel human serine proteinase inhibitor. Molecular cloning, tissue distribution, and expression in Escherichia coli. J Biol Chem. 1993 Nov 15;268(32):24498-505. [8227002 ] Chai KX, Ward DC, Chao J, Chao L: Molecular cloning, sequence analysis, and chromosomal localization of the human protease inhibitor 4 (kallistatin) gene (PI4). Genomics. 1994 Sep 15;23(2):370-8. [7835886 ] Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [15489334 ] Zhou GX, Chao L, Chao J: Kallistatin: a novel human tissue kallikrein inhibitor. Purification, characterization, and reactive center sequence. J Biol Chem. 1992 Dec 25;267(36):25873-80. [1334488 ] Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [12754519 ] Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [16335952 ] Jia W, Lu Z, Fu Y, Wang HP, Wang LH, Chi H, Yuan ZF, Zheng ZB, Song LN, Han HH, Liang YM, Wang JL, Cai Y, Zhang YK, Deng YL, Ying WT, He SM, Qian XH: A strategy for precise and large scale identification of core fucosylated glycoproteins. Mol Cell Proteomics. 2009 May;8(5):913-23. doi: 10.1074/mcp.M800504-MCP200. Epub 2009 Jan 12. [19139490 ]

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