Q6IE14
uniprot
Q6IE14
canonical
activity_regulation
ACTIVITY REGULATION: Inhibited by aprotinin, leupeptin, benzamidine, SERPINA1, SPINT1 and SPINT2. {ECO:0000250|UniProtKB:Q86T26}.
uniprot
proteins
amino_acid_sequence
MTVSKLRPVIASRKSFPPWMIILGVLGVLAILGLIIGLLVHFLAVENKIYYYQGSFKVLNIPYDRNYERETSLESNYLSKILEIKMVDAFESSNIYKQYINSQIITLVPENNSVTAHIWLVFKDPWSNKENLRRRIESILHQMLENNSGSLTTDPGSLKLTEITKVDAEKIINNRCGRRPRMSATYDRITGGSTAQKGEWPWQASLRVNGKHHCGASLIGERFLLTAAHCFLRTNNPKNLTVSFGTRVTPAYMQHYVEEVIIHEDYVKGQHHDDVAIIKLTEKVSFRNDVHRVCLPEATQVFPPGEGVVVTGWGSLSYNGKSPLLLQKASIKIIDTNACNSEEAYGGRIMDTMLCAGYMEGYVDACQGDSGGPLVHPNSRDIWYLVGIVSWGHECGRVNKPGVYMRVTSYRDWIASKTGI
uniprot
proteins
ec_number
3.4.21.-
uniprot
proteins
function
FUNCTION: Serine protease. {ECO:0000250|UniProtKB:Q86T26}.
uniprot
proteins
mass_dalton
47242
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15060002
uniprot
proteins
sequence_length
420
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q86T26}.
uniprot
proteins
transmembrane_region
TRANSMEM 20..40; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins