Q5K2P9
uniprot
Q5K2P9
canonical
activity_regulation
ACTIVITY REGULATION: Inhibited by serine proteinase inhibitor 4-(2-aminoethyl)-benzenesulfonyl fluoride, but not with EDTA or E-64.
uniprot
proteins
amino_acid_sequence
MSHHLFLPVVIMVVSPIPPGAFQDSVVSPTQGEFEDLDCGDCGRPEPSSRIVGGSDAHPGTWPWQVSLHQGGGHICGGSLIAPSWVLSAAHCFVTNGTLEPADELSVLLGVHSQDGPLEGAHMRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPLPLPWVLQEVELRLLGEAACQCLYSRPGPFNLTFQLLPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAPYESWIREHVMGSEPGPVFPSQLQKPQSGPWEPREENCTFAQPECGKAPRPGTWPWEAQVTVPGSTPCYGALVSDRWVLAPASCFLDSPHDFETWRVLLPSRPEEERVARLVAHENASRDFASDLALLQLRTRVNLTAAPSAVCLPHHEHYFLPGSHCRLARWGRGELAPGSSAQLEAQLLNGWWCHCLYGRQGETVPRPGDPPHLLCPAYQEEEEAGLCWVDSSWSLLCREEGTWFLAGYRTLSDGCLRPRAFSPMQTHGPWIRHVTQGAYLEDQLTWDWGPEGEETEKQTCPTHTEHGACGLRPKSTPAGVLWPWLTEVHVTGDRVCTGILVAPGWVLAATHCILRLGSTTVPYIEVYLGRAGVSSLPQGHQVSRSVVSIRLPRHLGLRPPLALLELNSRVEPSPSALPICLHPGGIPSGASCWVLGWKNPQDRVPVVAAVSILTPRLCHCLYPGILTPGTFCVLYSEGQEDRCEVTSAPPLLCQTEEGPWVLVGMAVRGNRELFAAIGPEATWISQTVGEAHFLHLGGSSYWSPEGSDLCPQDLAGSASSPKVTALLLLLLLAPLIPR
uniprot
proteins
ec_number
3.4.21.-
uniprot
proteins
function
FUNCTION: Serine protease. Hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1 (By similarity). {ECO:0000250}.
uniprot
proteins
mass_dalton
94483
uniprot
proteins
post_translational_modification
PTM: The 3 protease domains are not proteolytically cleaved. {ECO:0000250}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
15536082
uniprot
proteins
sequence_length
875
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Not attached to membranes. {ECO:0000250}.
uniprot
proteins