Q9ESD1
uniprot
Q9ESD1
canonical
amino_acid_sequence
MAPRVGLGLGQLEAVTILLLLGLLQSGIRADGTEASCGAVIQPRITGGGSAKPGQWPWQVSITYDGNHVCGGSLVSNKWVVSAAHCFPREHSREAYEVKLGAHQLDSYSNDTVVHTVAQIITHSSYREEGSQGDIAFIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLQTPRPLQQLEVPLISRETCSCLYNINAVPEEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTSTYASWIHHHVAELQPRVVPQTQESQPDGHLCNHHPVFSSAAAPKLLRPVLFLPLGLTLGLLSLWLEH
uniprot
proteins
ec_number
3.4.21.-
uniprot
proteins
function
FUNCTION: Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates (By similarity). Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G). {ECO:0000250, ECO:0000269|PubMed:10770960}.
uniprot
proteins
mass_dalton
36729
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10770960
uniprot
proteins
sequence_length
342
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Prostasin]: Secreted, extracellular space {ECO:0000250}.; SUBCELLULAR LOCATION: [Prostasin light chain]: Secreted, extracellular space {ECO:0000250}. Note=Found in the seminal fluid. Secreted after cleavage of its C-terminus. {ECO:0000250}.; SUBCELLULAR LOCATION: [Prostasin heavy chain]: Secreted, extracellular space {ECO:0000250}. Note=Found in the seminal fluid. Secreted after cleavage of its C-terminus. {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 320..340; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins