Q2KHK3
uniprot
Q2KHK3
canonical
activity_regulation
ACTIVITY REGULATION: Inhibited by bestatin. {ECO:0000250|UniProtKB:Q6Q4G3}.
uniprot
proteins
amino_acid_sequence
MSRPFSSGVYVSRGVALLLAALTAVLLLVLVALASLYGSCAHVQPSEQGNSRVKNTSLWPPGGQEWALPTPAQEPTVGTSQDLGPPSGPWDHLRLPPWLVPLHYDLELWPWLQPDKLSPPNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVWGPLAQDTRNATVGRVQVEKVWFAPDMQFVVLDLGQSLEPGSRYELSFHFSGQVLQVGLEGLFLNLYHDEDELRALVATQMEPTFARHVFPCFDEPALKATFNITVIHHPGYAALSNMPQLGQSERIDVNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISRTERGKEIRVWARKDDIANGYLDFAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWFGNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTAVENFTETSEINRLFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQMVIVPFRHFLAEH
uniprot
proteins
ec_number
3.4.11.-
uniprot
proteins
function
FUNCTION: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C. {ECO:0000250|UniProtKB:Q6Q4G3}.
uniprot
proteins
mass_dalton
63338
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6Q4G3}.
uniprot
proteins
protein_family
Peptidase M1 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
559
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6Q4G3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6Q4G3}.
uniprot
proteins
transmembrane_region
TRANSMEM 14..34; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins