| IED ID | IndEnz0002005874 |
| Enzyme Type ID | protease005874 |
| Protein Name |
Carboxypeptidase D EC 3.4.17.22 Metallocarboxypeptidase D gp180 |
| Gene Name | CPD |
| 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 | MASGRDERPPWRLGRLLLLMCLLLLGSSARAAHIKKAEATTTTTSAGAEAAEGQFDRYYHEEELESALREAAAAGLPGLARLFSIGRSVEGRPLWVLRLTAGLGSLIPEGDAGPDAAGPDAAGPLLPGRPQVKLVGNMHGDETVSRQVLIYLARELAAGYRRGDPRLVRLLNTTDVYLLPSLNPDGFERAREGDCGFGDGGPSGASGRDNSRGRDLNRSFPDQFSTGEPPALDEVPEVRALIEWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKATGIYSKTSDDEVFKYLAKAYASNHPIMKTGEPHCPGDEDETFKDGITNGAHWYDVEGGMQDYNYVWANCFEITLELSCCKYPPASQLRQEWENNRESLITLIEKVHIGVKGFVKDSITGSGLENATISVAGINHNITTGRFGDFYRLLVPGTYNLTVVLTGYMPLTVTNVVVKEGPATEVDFSLRPTVTSVIPDTTEAVSTASTVAIPNILSGTSSSYQPIQPKDFHHHHFPDMEIFLRRFANEYPNITRLYSLGKSVESRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVHNTRIHLMPSMNPDGYEKSQEGDSISVIGRNNSNNFDLNRNFPDQFVQITDPTQPETIAVMSWMKSYPFVLSANLHGGSLVVNYPFDDDEQGLATYSKSPDDAVFQQIALSYSKENSQMFQGRPCKNMYPNEYFPHGITNGASWYNVPGGMQDWNYLQTNCFEVTIELGCVKYPLEKELPNFWEQNRRSLIQFMKQVHQGVRGFVLDATDGRGILNATISVAEINHPVTTYKTGDYWRLLVPGTYKITASARGYNPVTKNVTVKSEGAIQVNFTLVRSSTDSNNESKKGKGASSSTNDASDPTTKEFETLIKDLSAENGLESLMLRSSSNLALALYRYHSYKDLSEFLRGLVMNYPHITNLTNLGQSTEYRHIWSLEISNKPNVSEPEEPKIRFVAGIHGNAPVGTELLLALAEFLCLNYKKNPAVTQLVDRTRIVIVPSLNPDGRERAQEKDCTSKIGQTNARGKDLDTDFTNNASQPETKAIIENLIQKQDFSLSVALDGGSMLVTYPYDKPVQTVENKETLKHLASLYANNHPSMHMGQPSCPNKSDENIPGGVMRGAEWHSHLGSMKDYSVTYGHCPEITVYTSCCYFPSAARLPSLWADNKRSLLSMLVEVHKGVHGFVKDKTGKPISKAVIVLNEGIKVQTKEGGYFHVLLAPGVHNIIAIADGYQQQHSQVFVHHDAASSVVIVFDTDNRIFGLPRELVVTVSGATMSALILTACIIWCICSIKSNRHKDGFHRLRQHHDEYEDEIRMMSTGSKKSLLSHEFQDETDTEEETLYSSKH |
| Enzyme Length | 1380 |
| Uniprot Accession Number | O75976 |
| Absorption | |
| Active Site | ACT_SITE 762; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P14384 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Releases C-terminal Arg and Lys from polypeptides.; EC=3.4.17.22; |
| DNA Binding | |
| EC Number | 3.4.17.22 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-6.5.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Beta strand (7); Chain (1); Glycosylation (15); Lipidation (3); Metal binding (6); Modified residue (6); Motif (1); Natural variant (4); Region (6); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Carboxypeptidase;Cell membrane;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Palmitate;Phosphoprotein;Protease;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q90240}; Single-pass type I membrane protein {ECO:0000255}. |
| Modified Residue | MOD_RES 265; /note="Phosphotyrosine"; /evidence="ECO:0000250|UniProtKB:O89001"; MOD_RES 270; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:O89001"; MOD_RES 1358; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"; MOD_RES 1361; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"; MOD_RES 1368; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 1370; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5AQ0; |
| Mapped Pubmed ID | 10394364; 10664463; 11306718; 11604418; 11694590; 11784792; 11940653; 11994746; 12842009; 15738000; 15918796; 16155256; 17116749; 17641957; 18535109; 18996843; 19103606; 20811643; 21628999; 21988832; 23589395; 24433040; 24502978; 24615730; 24690281; 25294878; 26638075; 26969432; 27494742; 28364216; 31871319; 8374173; 8524399; 8670264; |
| Motif | MOTIF 162..164; /note=Cell attachment site; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 152,931 |
| Kinetics | |
| Metal Binding | METAL 139; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 142; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 257; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 564; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 567; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 671; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.22; |