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query proteins and first shell of interactors
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a 3D structure is known or predicted
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PRCPLysosomal Pro-X carboxypeptidase; 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. (517 aa)    
Predicted Functional Partners:
DPP4
Dipeptidyl peptidase 4 membrane form; Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the mi [...]
     
 0.964
MME
Neprilysin; Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers. Belongs to the peptidase M13 family.
     
 0.964
ACE2
Processed angiotensin-converting enzyme 2; Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. By cleavage of angiotensin II, may be an important regulator of heart function. By cleavage of angiotensin II, may also have a protective role in acute lung injury (By similarity). Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SL6A19 in intestine, regulating traffickin [...]
     
 0.949
ACE
Angiotensin-converting enzyme, soluble form; Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI- anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety; Belongs to the peptidase M2 family.
     
 0.947
MEP1A
Meprin A subunit alpha.
     
 0.945
MEP1B
Meprin A subunit beta; Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components.
     
 0.938
KLK2
Kallikrein-2; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin; Belongs to the peptidase S1 family. Kallikrein subfamily.
     
 0.934
CMA1
Chymase; Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.
   
 
 0.933
XPNPEP2
Xaa-Pro aminopeptidase 2; Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin; Belongs to the peptidase M24B family.
   
 
 0.933
KLK1
Kallikrein-1; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin; Belongs to the peptidase S1 family. Kallikrein subfamily.
     
 0.932
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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