Detail Information for IndEnz0002018904
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;