| IED ID | IndEnz0002019365 |
| Enzyme Type ID | protease019365 |
| Protein Name |
Calpain-7 EC 3.4.22.- PalB homolog PalBH |
| Gene Name | CAPN7 PALBH |
| 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 | MDATALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAGSSLENIQEKITEYLERVQALHSAVQSKSADPLKSKHQLDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSEPLTKPVGKISSTSVKPKPPPVRAHFPLGANPFLERPQSFISPQSCDAQGQRYTAEEIEVLRTTSKINGIEYVPFMNVDLRERFAYPMPFCDRWGKLPLSPKQKTTFSKWVRPEDLTNNPTMIYTVSSFSIKQTIVSDCSFVASLAISAAYERRFNKKLITGIIYPQNKDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHKGELLCSYSNNKSELWVSLIEKAYMKVMGGYDFPGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYQRFHKGDVLITASTGMMTEAEGEKWGLVPTHAYAVLDIREFKGLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQKYLNFDPRTAQKIDNGIFWISWDDLCQYYDVIYLSWNPGLFKESTCIHSTWDAKQGPVKDAYSLANNPQYKLEVQCPQGGAAVWVLLSRHITDKDDFANNREFITMVVYKTDGKKVYYPADPPPYIDGIRINSPHYLTKIKLTTPGTHTFTLVVSQYEKQNTIHYTVRVYSACSFTFSKIPSPYTLSKRINGKWSGQSAGGCGNFQETHKNNPIYQFHIEKTGPLLIELRGPRQYSVGFEVVTVSTLGDPGPHGFLRKSSGDYRCGFCYLELENIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKITQLQ |
| Enzyme Length | 813 |
| Uniprot Accession Number | Q9Y6W3 |
| Absorption | |
| Active Site | ACT_SITE 290; /evidence=ECO:0000255|PROSITE-ProRule:PRU00239; ACT_SITE 458; /evidence=ECO:0000255|PROSITE-ProRule:PRU00239; ACT_SITE 478; /evidence=ECO:0000255|PROSITE-ProRule:PRU00239 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (9); Chain (1); Domain (1); Helix (2); Modified residue (2); Region (2); Turn (1) |
| Keywords | 3D-structure;Acetylation;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Repeat;Thiol protease |
| Interact With | A0A087WVE9; Q9Y2T1; Q96MT8-3; P56545-3; Q08379; Q13099; P53990; Q9Y6D9; Q9Y5V3; Q96KQ4; Q14558; Q13829; P14373; Q8N720 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0007744|PubMed:22814378; MOD_RES 95; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:19690332 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2QFE; |
| Mapped Pubmed ID | 12843408; 17608959; 17986458; 20711500; 20849418; 21030783; 21616915; 21670566; 21864727; 23035980; 23497113; 23855590; 24953135; 26496610; |
| Motif | |
| Gene Encoded By | |
| Mass | 92,652 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B27; |