Detail Information for IndEnz0002005971
IED ID IndEnz0002005971
Enzyme Type ID protease005971
Protein Name Carboxypeptidase E
CPE
EC 3.4.17.10
Carboxypeptidase H
CPH
Enkephalin convertase
Prohormone-processing carboxypeptidase
Gene Name cpe
Organism Lophius americanus (American angler) (Anglerfish)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Euteleosteomorpha Neoteleostei Eurypterygia Ctenosquamata Acanthomorphata Euacanthomorphacea Percomorphaceae Eupercaria Lophiiformes (anglerfishes) Lophioidei Lophiidae (goosefishes) Lophius Lophius americanus (American angler) (Anglerfish)
Enzyme Sequence MKQICSIVLLGAAVVSLVSAAGSDSEISFEYHRYEELRKALVSVWLQCPTIARIYTIGESFEGRELLVLEMSDNPGTHEPGEPEFKYIANMHGNEAVGRELLIYLAQYLCNQYQQGNETIIDLIHSTRIHLMPSMNPDGFEKAASQPGEIKDWFVGRSNAQGVDLNRNFPDLDRIIYTNEREGGANNHLLQNMKKAVDENTKLAPETKAVIHWIMEIPFVLSANLHGGDVVANYPYDETRTGSTHEYSASPDDVIFKSLAKAFSIYNPVMSDPQRPPCRKHDDDSSFKDGITNGGAWYSVPGGMQDFNYLSSNCFEITLELSCDKFPNEDTLKTYWEQNRNSLVNYIEQVHRGVKGYVRDLQGNPIFNATISVEGIDHDITTAKDGDYWRLLRQGNYKVAASAPGYLTVIKKVAVPHSPATRVDFELESLMERKEEEREELMDWWKMMSETLNF
Enzyme Length 454
Uniprot Accession Number P37892
Absorption
Active Site ACT_SITE 320; /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: Removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Glycosylation (2); Metal binding (3); Signal peptide (1)
Keywords Carboxypeptidase;Cytoplasmic vesicle;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: 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:P15087}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 51,416
Kinetics
Metal Binding METAL 92; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 95; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 226; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730
Rhea ID
Cross Reference Brenda