Detail Information for IndEnz0002000559
IED ID IndEnz0002000559
Enzyme Type ID protease000559
Protein Name Lysosomal Pro-X carboxypeptidase
EC 3.4.16.2
Angiotensinase C
Lysosomal carboxypeptidase C
Proline carboxypeptidase
Prolylcarboxypeptidase
PRCP
Gene Name PRCP PCP
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MGRRALLLLLLSFLAPWATIALRPALRALGSLHLPTNPTSLPAVAKNYSVLYFQQKVDHFGFNTVKTFNQRYLVADKYWKKNGGSILFYTGNEGDIIWFCNNTGFMWDVAEELKAMLVFAEHRYYGESLPFGDNSFKDSRHLNFLTSEQALADFAELIKHLKRTIPGAENQPVIAIGGSYGGMLAAWFRMKYPHMVVGALAASAPIWQFEDLVPCGVFMKIVTTDFRKSGPHCSESIHRSWDAINRLSNTGSGLQWLTGALHLCSPLTSQDIQHLKDWISETWVNLAMVDYPYASNFLQPLPAWPIKVVCQYLKNPNVSDSLLLQNIFQALNVYYNYSGQVKCLNISETATSSLGTLGWSYQACTEVVMPFCTNGVDDMFEPHSWNLKELSDDCFQQWGVRPRPSWITTMYGGKNISSHTNIVFSNGELDPWSGGGVTKDITDTLVAVTISEGAHHLDLRTKNALDPMSVLLARSLEVRHMKNWIRDFYDSAGKQH
Enzyme Length 496
Uniprot Accession Number P42785
Absorption
Active Site ACT_SITE 179; /note=Charge relay system; /evidence=ECO:0000269|PubMed:20540760; ACT_SITE 430; /note=Charge relay system; /evidence=ECO:0000269|PubMed:20540760; ACT_SITE 455; /note=Charge relay system; /evidence=ECO:0000269|PubMed:20540760
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid.; EC=3.4.16.2;
DNA Binding
EC Number 3.4.16.2
Enzyme Function FUNCTION: Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Beta strand (12); Chain (1); Disulfide bond (4); Glycosylation (6); Helix (18); Natural variant (2); Propeptide (1); Region (1); Sequence conflict (3); Signal peptide (1); Turn (3)
Keywords 3D-structure;Alternative splicing;Carboxypeptidase;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Signal;Zymogen
Interact With O60883
Induction
Subcellular Location SUBCELLULAR LOCATION: Lysosome.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3N2Z;
Mapped Pubmed ID 11830581; 12123826; 12768436; 14996700; 16681991; 18396440; 18656443; 19913121; 20079160; 20516604; 20517885; 20628086; 20711500; 21087932; 21988832; 22079761; 22679278; 23650620; 23744584; 25324000; 25370794; 26496610; 27449720; 28831120; 31837203; 32448049; 33319614; 8692836;
Motif
Gene Encoded By
Mass 55,800
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.16.2;