| IED ID | IndEnz0002018948 |
| Enzyme Type ID | protease018948 |
| Protein Name |
Carboxypeptidase M CPM EC 3.4.17.12 |
| Gene Name | Cpm |
| 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 | MDRARLWLGLLLPVVAALDFRYHHQEGMEAFLKSVAQNYSSITHLHSIGKSVRGRNLWVLVVGQTPKEHRVGIPEFKYVANMHGDETVGRELLLHLIDYLVSSYRKDPEITHLIDSTRIHIMPSMNPDGFEAVQKPDCYYSNGRENYNNYDLNRNFPDAFENNNVTKQPETLAIMEWLKTETFVLSANLHGGALVASYPFDNGVQATGTLLSRSLTPDDDVFQHLAYTYASRNPNMTKGDQCKNKRNFPNGIINGYSWYPLQGGMQDYNYIWAQCFEITLELSCCKYPREEKLPLFWNDNKASLIEYIKQVHLGVKGQVFDQSGAPLPNVIVEVQDRKHICPFRTNKLGEYYLLLLPGSYVINVTVPGHDSYLTKLTIPGKSQPFSALKKDFHLPLRWQPDSISVSNPSCPMIPLYKFMPSHSAATKPSLGVFFMTLLYVFFK |
| Enzyme Length | 443 |
| Uniprot Accession Number | Q80V42 |
| Absorption | |
| Active Site | ACT_SITE 281; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P14384 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of C-terminal arginine or lysine residues from polypeptides.; EC=3.4.17.12; |
| DNA Binding | |
| EC Number | 3.4.17.12 |
| Enzyme Function | FUNCTION: Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (3); Lipidation (1); Metal binding (3); Propeptide (1); Signal peptide (1) |
| Keywords | Alternative splicing;Carboxypeptidase;Cell membrane;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 14610273; 15172686; 18554416; 18844448; 18973680; 19200403; 20510229; 21267068; 21362171; 34155146; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,556 |
| Kinetics | |
| Metal Binding | METAL 83; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 86; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 190; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.12; |