Detail Information for IndEnz0002018938
IED ID IndEnz0002018938
Enzyme Type ID protease018938
Protein Name Carboxypeptidase E
CPE
EC 3.4.17.10
Egg-laying defective protein 21
Gene Name egl-21 F01D4.4
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MLHAMRPVLLVAALLAVTAHAFLGFGSGSTHKDDAEWGHYHNQAQLEAKLGEINEKCPEITTLYEIGQSVEGRPLVVIQFSTTPGEHIPTKPEVKLIGNMHGNEPIGRELLLRFAETLCNGAINNDKEIVQLLNSTSIHILPSMNPDGFELALGTEPAQRQWLTGRSNINGVDLNRDFPDLDSIFYELQKIGVPKFDHLLSLFEDNVDRQPETIAVGQWTLSLPFVLSANFHEGDLVANYPFDAAIDENSQKTAYSASPDDGTFRWLAKSYADNHAHMSKNDHAPCDGTSQDAFARQGGITNGAKWYSVAGGMQDFNYLATNAMEITLELSCEKMPEGSQLPRFWEDNQKSIFEYVWKSHSGVKGMVVDAMTGEPIKRAVVWIRNGTETVPVKHPVTTWSEGDFYRVLPAGKYEIIVAAEGYDIAAKNVTVENKVRDSALVVNFALSPAADEPSENEQEQIAELVNEIARRR
Enzyme Length 472
Uniprot Accession Number O17754
Absorption
Active Site ACT_SITE 329; /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; Evidence={ECO:0000303|PubMed:12657671, ECO:0000303|PubMed:17564681};
DNA Binding
EC Number 3.4.17.10
Enzyme Function FUNCTION: During FMRFamide-like peptide (FaRPs or FLP) and neuropeptide-like protein (NLP) precursor processing, catalyzes the removal of Arg or Lys residues from the C-terminus following the initial endoprotease cleavage (PubMed:17564681, PubMed:12657671). By processing neuropeptides, modulates basal acetylcholine release at the ventral cord neuromuscular junctions (PubMed:12657671, PubMed:22275875). Involved in egg-laying, defecation and locomotion (PubMed:11813735, PubMed:17564681, PubMed:22275875). By processing FLP neuropeptides, regulates the turning step of male mating behavior (PubMed:17611271). Involved in reducing pharyngeal pumping in response to high CO(2) levels (PubMed:25101962). {ECO:0000269|PubMed:11813735, ECO:0000269|PubMed:12657671, ECO:0000269|PubMed:17564681, ECO:0000269|PubMed:17611271, ECO:0000269|PubMed:22275875, ECO:0000269|PubMed:25101962}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Glycosylation (3); Metal binding (3); Signal peptide (1)
Keywords Carboxypeptidase;Cell projection;Cytoplasmic vesicle;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:12657671}. Perikaryon {ECO:0000269|PubMed:12657671}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000303|PubMed:12657671}. Note=Predominantly localizes to axons in the nerve ring. {ECO:0000269|PubMed:12657671}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 14704431; 16049479; 17164286; 17251413; 18316030; 18524955; 18818084; 19343510; 20439776; 21177967; 22286215; 22347378; 22560298; 23658528; 23665919; 23800452; 23852451; 25487147; 30454862;
Motif
Gene Encoded By
Mass 52,279
Kinetics
Metal Binding METAL 101; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 104; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 232; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730
Rhea ID
Cross Reference Brenda