Kallistatin
Details
- Name
- Kallistatin
- Synonyms
-
- Kallikrein inhibitor
- KST
- Peptidase inhibitor 4
- PI-4
- PI4
- Serpin A4
- Gene Name
- SERPINA4
- Organism
- Humans
- Amino acid sequence
-
>lcl|BSEQ0049846|Kallistatin MHLIDYLLLLLVGLLALSHGQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAF RFYYLIASETPGKNIFFSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRG FQHLLHTLNLPGHGLETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQ LINDHVKKETRGKIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTT VRVPMMLQDQEHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMR WNNLLRKRNFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEAS KSFHKATLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGK VVDPTKP
- Number of residues
- 427
- Molecular Weight
- 48541.51
- Theoretical pI
- Not Available
- GO Classification
-
Functionsserine-type endopeptidase inhibitor activityProcessesplatelet degranulationComponentsextracellular exosome/extracellular region/extracellular space/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
- Pfam Domain Function
-
- Serpin (PF00079)
- Transmembrane Regions
- Not Available
- 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
- Chromosome Location
- 14
- Locus
- 14q32.13
- External Identifiers
-
Resource Link UniProtKB ID P29622 UniProtKB条目名称 KAIN_HUMAN HGNC ID HGNC:8948 - General References
-
- 陈茶KX, LM,曹国伟J,曹国伟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. [Article]
- 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. [Article]
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- 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. [Article]
- 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. [Article]
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