| IED ID | IndEnz0002018904 |
| Enzyme Type ID | protease018904 |
| Protein Name |
Carboxypeptidase A4 EC 3.4.17.- Carboxypeptidase A3 |
| Gene Name | CPA4 CPA3 UNQ694/PRO1339 |
| 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 | MRWILFIGALIGSSICGQEKFFGDQVLRINVRNGDEISKLSQLVNSNNLKLNFWKSPSSFNRPVDVLVPSVSLQAFKSFLRSQGLEYAVTIEDLQALLDNEDDEMQHNEGQERSSNNFNYGAYHSLEAIYHEMDNIAADFPDLARRVKIGHSFENRPMYVLKFSTGKGVRRPAVWLNAGIHSREWISQATAIWTARKIVSDYQRDPAITSILEKMDIFLLPVANPDGYVYTQTQNRLWRKTRSRNPGSSCIGADPNRNWNASFAGKGASDNPCSEVYHGPHANSEVEVKSVVDFIQKHGNFKGFIDLHSYSQLLMYPYGYSVKKAPDAEELDKVARLAAKALASVSGTEYQVGPTCTTVYPASGSSIDWAYDNGIKFAFTFELRDTGTYGFLLPANQIIPTAEETWLGLKTIMEHVRDNLY |
| Enzyme Length | 421 |
| Uniprot Accession Number | Q9UI42 |
| Absorption | |
| Active Site | ACT_SITE 382; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00732 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by interaction with the metallocarboxypeptidase inhibitor (MCPI) from N.versicolor that binds to the catalytic zinc ion. {ECO:0000269|PubMed:22294694}. |
| Binding Site | BINDING 239; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730; BINDING 360; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Metalloprotease that could be involved in the histone hyperacetylation pathway (PubMed:10383164). Releases a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val (PubMed:20385563). {ECO:0000269|PubMed:10383164, ECO:0000269|PubMed:20385563}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9. {ECO:0000269|PubMed:20385563}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Beta strand (18); Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (1); Helix (17); Metal binding (3); Natural variant (4); Propeptide (1); Region (4); Sequence conflict (1); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Alternative splicing;Carboxypeptidase;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | P84875 |
| Induction | INDUCTION: Up-regulated by inhibitors of histone dacetylation. {ECO:0000269|PubMed:10383164}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 2BO9; 2BOA; 2PCU; 4A94; 4BD9; |
| Mapped Pubmed ID | 17506531; 19245716; 23746805; 27780921; 28209092; 31279884; 31397502; 31466718; 32347291; 33746592; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,351 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=55.6 uM for 3-(2-furyl)acryloyl-Phe-Phe {ECO:0000269|PubMed:20385563}; KM=19.4 uM for 3-(2-furyl)acryloyl-Phe-Leu {ECO:0000269|PubMed:20385563}; KM=23.3 uM for 3-(2-furyl)acryloyl-Phe-Ile {ECO:0000269|PubMed:20385563}; KM=40.4 uM for 3-(2-furyl)acryloyl-Phe-Met {ECO:0000269|PubMed:20385563}; KM=57.3 uM for 3-(2-furyl)acryloyl-Phe-Val {ECO:0000269|PubMed:20385563}; KM=0.329 uM for neurotensin {ECO:0000269|PubMed:20385563}; KM=9.23 uM for Met-enkephalin-Arg-Phe {ECO:0000269|PubMed:20385563}; |
| Metal Binding | METAL 181; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:22294694; METAL 184; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:22294694; METAL 308; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:22294694 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.1; |