| IED ID | IndEnz0002018838 |
| Enzyme Type ID | protease018838 |
| Protein Name |
Carboxypeptidase M CPM EC 3.4.17.12 |
| Gene Name | CPM |
| 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 | MDFPCLWLGLLLPLVAALDFNYHRQEGMEAFLKTVAQNYSSVTHLHSIGKSVKGRNLWVLVVGRFPKEHRIGIPEFKYVANMHGDETVGRELLLHLIDYLVTSDGKDPEITNLINSTRIHIMPSMNPDGFEAVKKPDCYYSIGRENYNQYDLNRNFPDAFEYNNVSRQPETVAVMKWLKTETFVLSANLHGGALVASYPFDNGVQATGALYSRSLTPDDDVFQYLAHTYASRNPNMKKGDECKNKMNFPNGVTNGYSWYPLQGGMQDYNYIWAQCFEITLELSCCKYPREEKLPSFWNNNKASLIEYIKQVHLGVKGQVFDQNGNPLPNVIVEVQDRKHICPYRTNKYGEYYLLLLPGSYIINVTVPGHDPHITKVIIPEKSQNFSALKKDILLPFQGQLDSIPVSNPSCPMIPLYRNLPDHSAATKPSLFLFLVSLLHIFFK |
| Enzyme Length | 443 |
| Uniprot Accession Number | P14384 |
| Absorption | |
| Active Site | ACT_SITE 281; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:12457462 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by O-phenanthroline and MGTA and activated by cobalt. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of C-terminal arginine or lysine residues from polypeptides.; EC=3.4.17.12; Evidence={ECO:0000269|PubMed:12457462}; |
| 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. {ECO:0000269|PubMed:12457462}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:12457462}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (18); Chain (1); Disulfide bond (3); Glycosylation (5); Helix (13); Lipidation (1); Metal binding (3); Mutagenesis (5); Natural variant (2); Propeptide (1); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Carboxypeptidase;Cell membrane;Direct protein sequencing;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:0000269|PubMed:12457462}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12457462}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence="ECO:0000269|PubMed:12457462, ECO:0000269|PubMed:2753907" |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1UWY; |
| Mapped Pubmed ID | 11072085; 11891060; 18187413; 18292211; 18617639; 19820690; 20360068; 20673876; 20711500; 21278420; 21454694; 22106087; 22157720; 23172796; 24108126; 2443973; 26496610; 28186967; 2914904; 30674606; 31218444; 3422494; 8635221; 8796265; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,514 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=59 uM for synthetic dansyl-Ala-Arg {ECO:0000269|PubMed:12457462}; KM=57 uM for placental peptide hormones {ECO:0000269|PubMed:12457462}; |
| Metal Binding | METAL 83; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:15066430, ECO:0007744|PDB:1UWY"; METAL 86; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:15066430, ECO:0007744|PDB:1UWY"; METAL 190; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:15066430, ECO:0007744|PDB:1UWY" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.12; |