PRSS36
entrez
146547
canonical
uniprot
Q5K4E3
canonical
ensembl
ENSG00000178226
resolver
ensp
ENSP00000268281
resolver
ensp
ENSP00000407160
resolver
ensp
ENSP00000454768
resolver
genesymbol
PRSS36
resolver
hgnc
HGNC:26906
resolver
uniprot
A8K2P5
resolver
uniprot
B4DNP1
resolver
uniprot
B4DW80
resolver
uniprot
B7ZMK8
resolver
uniprot
E7EX56
resolver
uniprot
Q8NBY4
resolver
uniprot_entry
B4DNP1_HUMAN
resolver
uniprot_entry
POLS2_HUMAN
resolver
uniprot_sec
A8K2P5
resolver
uniprot_sec
B4DW80
resolver
uniprot_sec
B7ZMK8
resolver
uniprot_sec
E7EX56
resolver
uniprot_sec
Q8NBY4
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by serine proteinase inhibitor 4-(2-aminoethyl)-benzenesulfonyl fluoride, but not with EDTA or E-64. {ECO:0000269|PubMed:15536082}.
uniprot
proteins
amino_acid_sequence
MARHLLLPLVMLVISPIPGAFQDSALSPTQEEPEDLDCGRPEPSARIVGGSNAQPGTWPWQVSLHHGGGHICGGSLIAPSWVLSAAHCFMTNGTLEPAAEWSVLLGVHSQDGPLDGAHTRAVAAIVVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPLPLPWVLQEVELRLLGEATCQCLYSQPGPFNLTLQILPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEAWIREQVMGSEPGPAFPTQPQKTQSDPQEPREENCTIALPECGKAPRPGAWPWEAQVMVPGSRPCHGALVSESWVLAPASCFLDPNSSDSPPRDLDAWRVLLPSRPRAERVARLVQHENASWDNASDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGALLEAELLGGWWCHCLYGRQGAAVPLPGDPPHALCPAYQEKEEVGSCWNDSRWSLLCQEEGTWFLAGIRDFPSGCLRPRAFFPLQTHGPWISHVTRGAYLEDQLAWDWGPDGEETETQTCPPHTEHGACGLRLEAAPVGVLWPWLAEVHVAGDRVCTGILLAPGWVLAATHCVLRPGSTTVPYIEVYLGRAGASSLPQGHQVSRLVISIRLPQHLGLRPPLALLELSSRVEPSPSALPICLHPAGIPPGASCWVLGWKEPQDRVPVAAAVSILTQRICDCLYQGILPPGTLCVLYAEGQENRCEMTSAPPLLCQMTEGSWILVGMAVQGSRELFAAIGPEEAWISQTVGEANFLPPSGSPHWPTGGSNLCPPELAKASGSPHAVYFLLLLTLLIQS
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.
uniprot
proteins
mass_dalton
91955
uniprot
proteins
post_translational_modification
PTM: The 3 protease domains are not proteolytically cleaved.; PTM: N-glycosylated. {ECO:0000269|PubMed:15536082}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15536082
uniprot
proteins
pubmed
15616553
uniprot
proteins
sequence_length
855
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:15536082}. Note=Not attached to membranes.
uniprot
proteins