Detail Information for IndEnz0002019298
IED ID IndEnz0002019298
Enzyme Type ID protease019298
Protein Name EEF1AKMT4-ECE2 readthrough transcript protein
EC 3.4.24.71

Includes: Methyltransferase-like region
EC 2.1.1.-
; Endothelin-converting enzyme 2 region
EC 3.4.24.71
Gene Name Eef1akmt4-Ece2
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MASPRTPVSPPELPEKNFQYRQVQYWDQRYKDAADSGPYEWFGDFASFRALLEPELCPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSPVVVAAMQVRYAHVPSLRWETMDVRALDFPSGSFDVVLEKGTLDAMLAGEPDPWNVSSEGVHTVDQVLSEVGFQKRTRQLFGSHTQLELVLAGLILVLAALLLGCLVALWVHRDPAHSTCVTEACIRVAGKILESLDRGVSPCQDFYQFSCGGWIRRNPLPNGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTRSFYLSCLQSERIEKLGAKPLRDLIDKIGGWNITGPWDEDSFMDVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMVELGVLLGGQPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPAVDWLEFLSFLLSPLELGDSEPVVVYGTEYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDQRFETAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMINEIRSAFEETLGDLVWMDEKTRLAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYAHNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLTAFQNHTACMEEQYSQYQVNGERLNGLQTLGENIADNGGLKAAYNAYKAWLRKHGEEQPLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW
Enzyme Length 881
Uniprot Accession Number P0DPD9
Absorption
Active Site ACT_SITE 719; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 782; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
Activity Regulation ACTIVITY REGULATION: Inhibited by phosphoramidon. {ECO:0000250|UniProtKB:P0DPE2}.
Binding Site BINDING 26; /note=S-adenosyl-L-methionine; /evidence=ECO:0000250|UniProtKB:P0DPD7; BINDING 30; /note=S-adenosyl-L-methionine; /evidence=ECO:0000250|UniProtKB:P0DPD7; BINDING 41; /note=S-adenosyl-L-methionine; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P0DPD7; BINDING 66; /note=S-adenosyl-L-methionine; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P0DPD7; BINDING 130; /note=S-adenosyl-L-methionine; /evidence=ECO:0000250|UniProtKB:P0DPD7
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.; EC=3.4.24.71; Evidence={ECO:0000250|UniProtKB:P0DPE2};
DNA Binding
EC Number 3.4.24.71; 2.1.1.-; 3.4.24.71
Enzyme Function FUNCTION: Converts big endothelin-1 to endothelin-1. May also have methyltransferase activity (By similarity). May play a role in amyloid-beta processing (PubMed:12464614). {ECO:0000250|UniProtKB:P0DPE2, ECO:0000269|PubMed:12464614}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (1); Binding site (5); Chain (1); Disulfide bond (5); Domain (1); Erroneous initiation (2); Glycosylation (9); Metal binding (3); Modified residue (2); Region (3); Sequence conflict (10); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Golgi apparatus;Hydrolase;Membrane;Metal-binding;Metalloprotease;Methyltransferase;Multifunctional enzyme;Phosphoprotein;Protease;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P0DPE2}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P0DPE2}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P0DPE2}.
Modified Residue MOD_RES 39; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:P0DPD8; MOD_RES P0DPD9-2:174; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 20807771; 21450041; 21972895; 24847082; 24990314; 27644077;
Motif
Gene Encoded By
Mass 99,480
Kinetics
Metal Binding METAL 718; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 722; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 778; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
Rhea ID
Cross Reference Brenda