Klk1b27
entrez
16619
canonical
uniprot
Q9JM71
canonical
ensembl
ENSMUSG00000063177
resolver
ensp
ENSMUSP00000078786
resolver
enst
ENSMUST00000079859
resolver
genesymbol
Klk1b27
resolver
genesymbol_syn
Klk-27
resolver
genesymbol_syn
Klk27
resolver
uniprot
A2RSF8
resolver
uniprot_entry
K1B27_MOUSE
resolver
uniprot_sec
A2RSF8
resolver
activity_regulation
ACTIVITY REGULATION: Strongly inhibited by protease inhibitors diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride and SBTI. {ECO:0000269|PubMed:11082197}.
uniprot
proteins
amino_acid_sequence
MRFLILFLALSLGGIDAAPPVQSRIIGGFKCKKNSQPWHVAVLRSNKYICGGVLLDPNWVLTAAHCYGNDTSQHNVWLGKNKLFQREPSAQHRWVSKSFPHPDYNMSLLNDHIPHPEDKSNDLMLLRLSKPADITDAVKPIDLPTEEPKLGSTCLASGWGSITPTKYQIPNDLQCVFIKLLPNENCAKAYVHKVTDVMLCVGETGGGKGTCKGDSGGPLICDGVLHGITSWGSIPCAKPNAPGVFTKLIKFTSWIKDTMAKNP
uniprot
proteins
ec_number
3.4.21.-
uniprot
proteins
function
FUNCTION: Serine protease with chymotrypsin-like cleavage specificity. Shows activity towards casein, gelatin, IGFBP3 and fibronectin but not towards laminin or collagens I and IV. Does not hydrolyze kininogin to release Lys-bradykinin.
uniprot
proteins
mass_dalton
28742
uniprot
proteins
mutagenesis
MUTAGEN 209; /note="G->D: Loss of chymotryptic specificity and acquisition of trypsin-like cleavage specificity."; /evidence="ECO:0000269|PubMed:11082197
uniprot
proteins
protein_family
Kallikrein subfamily
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
11082197
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
263
uniprot
proteins