| IED ID | IndEnz0002005969 |
| Enzyme Type ID | protease005969 |
| Protein Name |
Carboxypeptidase E CPE EC 3.4.17.10 Carboxypeptidase H CPH Enkephalin convertase Prohormone-processing carboxypeptidase |
| Gene Name | CPE |
| 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 | MAGRGGSALLALCGALAACGWLLGAEAQEPGAPAAGMRRRRRLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQKGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNMKKIVDQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGSAHEYSSSPDDAIFQSLARAYSSFNPAMSDPNRPPCRKNDDDSSFVDGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKFPPEETLKTYWEDNKNSLISYLEQIHRGVKGFVRDLQGNPIANATISVEGIDHDVTSAKDGDYWRLLIPGNYKLTASAPGYLAITKKVAVPYSPAAGVDFELESFSERKEEEKEELMEWWKMMSETLNF |
| Enzyme Length | 476 |
| Uniprot Accession Number | P16870 |
| Absorption | |
| Active Site | ACT_SITE 342; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P14384 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of C-terminal arginine or lysine residues from polypeptides.; EC=3.4.17.10; |
| DNA Binding | |
| EC Number | 3.4.17.10 |
| Enzyme Function | FUNCTION: Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. {ECO:0000250|UniProtKB:Q00493}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Frameshift (1); Glycosylation (2); Metal binding (3); Natural variant (2); Propeptide (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Alternative splicing;Carboxypeptidase;Cleavage on pair of basic residues;Cytoplasmic vesicle;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | P49768-2 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q00493}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P15087}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15087}. Secreted {ECO:0000250|UniProtKB:P15087}. Note=Associated with the secretory granule membrane through direct binding to lipid rafts in intragranular conditions. {ECO:0000250|UniProtKB:Q00493}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10966857; 11462236; 12136131; 12479974; 12530526; 14690244; 15492986; 16158220; 16169070; 16984975; 17957445; 18080843; 18501121; 18550819; 19077438; 19120309; 19166515; 19491387; 19593212; 19913121; 20201924; 20368287; 20379614; 20468064; 20628086; 21628999; 22824791; 22998035; 23852859; 24006921; 24835590; 24843127; 25157818; 25374060; 26228366; 26695643; 26803519; 27375026; 27922637; 28114332; 2822027; 28656234; 32675394; 34383079; 34966948; 3896518; 9019408; 9369230; 9631292; 9667917; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,151 |
| Kinetics | |
| Metal Binding | METAL 114; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 117; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 248; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.10; |