| IED ID | IndEnz0002007722 |
| Enzyme Type ID | protease007722 |
| Protein Name |
Carboxypeptidase N catalytic chain CPN EC 3.4.17.3 Anaphylatoxin inactivator Arginine carboxypeptidase Carboxypeptidase N polypeptide 1 Carboxypeptidase N small subunit Kininase-1 Lysine carboxypeptidase Plasma carboxypeptidase B Serum carboxypeptidase N SCPN |
| Gene Name | CPN1 ACBP |
| 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 | MSDLLSVFLHLLLLFKLVAPVTFRHHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLPLPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTASTPTPDDKLFQKLAKVYSYAHGWMFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQVHQGIKGMVLDENYNNLANAVISVSGINHDVTSGDHGDYFRLLLPGIYTVSATAPGYDPETVTVTVGPAEPTLVNFHLKRSIPQVSPVRRAPSRRHGVRAKVQPQARKKEMEMRQLQRGPA |
| Enzyme Length | 458 |
| Uniprot Accession Number | P15169 |
| Absorption | |
| Active Site | ACT_SITE 308; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P14384 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal basic amino acid, preferentially lysine.; EC=3.4.17.3; |
| DNA Binding | |
| EC Number | 3.4.17.3 |
| Enzyme Function | FUNCTION: Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (16); Chain (1); Disulfide bond (2); Glycosylation (3); Helix (16); Metal binding (3); Natural variant (1); Region (2); Sequence conflict (2); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Carboxypeptidase;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc |
| Interact With | Q5SUL5; Q92993; Q8TAP4-4; Q96CV9; P17252; Q15047-2; P61981 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000269|PubMed:3408501 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2NSM; |
| Mapped Pubmed ID | 11939578; 15718415; 16385451; 18039526; 18624398; 18940312; 19010784; 20200978; 20648472; 21052031; 23000409; 4098172; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,286 |
| Kinetics | |
| Metal Binding | METAL 86; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 89; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 216; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.3; |