| IED ID | IndEnz0002000788 |
| Enzyme Type ID | protease000788 |
| Protein Name |
Proprotein convertase subtilisin/kexin type 7 EC 3.4.21.- Lymphoma proprotein convertase Prohormone convertase 7 Proprotein convertase 7 PC7 Proprotein convertase 8 PC8 hPC8 Subtilisin/kexin-like protease PC7 |
| Gene Name | PCSK7 LPC PC7 PC8 SPC7 |
| 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 | MPKGRQKVPHLDAPLGLPTCLWLELAGLFLLVPWVMGLAGTGGPDGQGTGGPSWAVHLESLEGDGEEETLEQQADALAQAAGLVNAGRIGELQGHYLFVQPAGHRPALEVEAIRQQVEAVLAGHEAVRWHSEQRLLRRAKRSVHFNDPKYPQQWHLNNRRSPGRDINVTGVWERNVTGRGVTVVVVDDGVEHTIQDIAPNYSPEGSYDLNSNDPDPMPHPDVENGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGPLTDSMEAVAFNKHYQINDIYSCSWGPDDDGKTVDGPHQLGKAALQHGVIAGRQGFGSIFVVASGNGGQHNDNCNYDGYANSIYTVTIGAVDEEGRMPFYAEECASMLAVTFSGGDKMLRSIVTTDWDLQKGTGCTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTATRYEDRRAEWVTNEAGFSHSHQHGFGLLNAWRLVNAAKIWTSVPYLASYVSPVLKENKAIPQSPRSLEVLWNVSRMDLEMSGLKTLEHVAVTVSITHPRRGSLELKLFCPSGMMSLIGAPRSMDSDPNGFNDWTFSTVRCWGERARGTYRLVIRDVGDESFQVGILRQWQLTLYGSVWSAVDIRDRQRLLESAMSGKYLHDDFALPCPPGLKIPEEDGYTITPNTLKTLVLVGCFTVFWTVYYMLEVYLSQRNVASNQVCRSGPCHWPHRSRKAKEEGTELESVPLCSSKDPDEVETESRGPPTTSDLLAPDLLEQGDWSLSQNKSALDCPHQHLDVPHGKEEQIC |
| Enzyme Length | 785 |
| Uniprot Accession Number | Q16549 |
| Absorption | |
| Active Site | ACT_SITE 187; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 228; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 406; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by zinc and copper. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (2); Glycosylation (4); Natural variant (5); Propeptide (1); Region (2); Sequence conflict (6); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Cleavage on pair of basic residues;Glycoprotein;Golgi apparatus;Hydrolase;Lipoprotein;Membrane;Palmitate;Protease;Reference proteome;Serine protease;Signal;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | P14136; Q8WXH2; Q92876; P19404; P29474; P16284; P17612; P50454; P37173 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Seems to be localized intracellularly to the trans Golgi network. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cysteine residues in the cytoplasmic tail are probably palmitoylated. {ECO:0000269|PubMed:9341152}.; PTM: N-glycosylated. {ECO:0000269|PubMed:9341152}. |
| Signal Peptide | SIGNAL 1..37; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11723118; 17242158; 20164418; 20608975; 21075846; 21149283; 21209099; 22294700; 23390091; 23686857; 24436242; 24556216; 25504030; 26763881; 26868056; 30918065; 31915245; 31945259; 33118184; 33565643; 34207761; 34876018; |
| Motif | |
| Gene Encoded By | |
| Mass | 86,247 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.B27; |