| IED ID | IndEnz0002004473 |
| Enzyme Type ID | protease004473 |
| Protein Name |
Carboxypeptidase Q EC 3.4.17.- Lysosomal dipeptidase Plasma glutamate carboxypeptidase |
| Gene Name | CPQ LCH1 PGCP |
| 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 | MKFLIFAFFGGVHLLSLCSGKAICKNGISKRTFEEIKEEIASCGDVAKAIINLAVYGKAQNRSYERLALLVDTVGPRLSGSKNLEKAIQIMYQNLQQDGLEKVHLEPVRIPHWERGEESAVMLEPRIHKIAILGLGSSIGTPPEGITAEVLVVTSFDELQRRASEARGKIVVYNQPYINYSRTVQYRTQGAVEAAKVGALASLIRSVASFSIYSPHTGIQEYQDGVPKIPTACITVEDAEMMSRMASHGIKIVIQLKMGAKTYPDTDSFNTVAEITGSKYPEQVVLVSGHLDSWDVGQGAMDDGGGAFISWEALSLIKDLGLRPKRTLRLVLWTAEEQGGVGAFQYYQLHKVNISNYSLVMESDAGTFLPTGLQFTGSEKARAIMEEVMSLLQPLNITQVLSHGEGTDINFWIQAGVPGASLLDDLYKYFFFHHSHGDTMTVMDPKQMNVAAAVWAVVSYVVADMEEMLPRS |
| Enzyme Length | 472 |
| Uniprot Accession Number | Q9Y646 |
| Absorption | |
| Active Site | ACT_SITE 336; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Carboxypeptidase that may play an important role in the hydrolysis of circulating peptides. Catalyzes the hydrolysis of dipeptides with unsubstituted terminals into amino acids. May play a role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Frameshift (1); Glycosylation (5); Metal binding (6); Natural variant (1); Propeptide (1); Sequence conflict (5); Signal peptide (1) |
| Keywords | Carboxypeptidase;Direct protein sequencing;Endoplasmic reticulum;Glycoprotein;Golgi apparatus;Hydrolase;Lysosome;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: Up-regulated in the majority of hepatitis C virus-associated hepatocellular carcinoma. {ECO:0000269|PubMed:12591738}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:10206990}. Golgi apparatus {ECO:0000269|PubMed:10206990}. Lysosome {ECO:0000250}. Secreted {ECO:0000269|PubMed:10206990}. Note=Secretion is stimulated by TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. The secreted form is modified by hybrid or complex type oligosaccharide chains (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20201926; 20379614; 20802479; 27806330; 29196255; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,888 |
| Kinetics | |
| Metal Binding | METAL 290; /note=Zinc 1; /evidence=ECO:0000250; METAL 302; /note=Zinc 1; /evidence=ECO:0000250; METAL 302; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 337; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 364; /note=Zinc 1; /evidence=ECO:0000250; METAL 434; /note=Zinc 2; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |