| IED ID | IndEnz0002019206 |
| Enzyme Type ID | protease019206 |
| Protein Name |
Calpain-8 EC 3.4.22.53 New calpain 2 nCL-2 Stomach-specific M-type calpain |
| Gene Name | CAPN8 NCL2 |
| 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 | MAAQAAGVSRQRAATQGLGSNQNALKYLGQDFKTLRQQCLDSGVLFKDPEFPACPSALGYKDLGPGSPQTQGIIWKRPTELCPSPQFIVGGATRTDICQGGLGDCWLLAAIASLTLNEELLYRVVPRDQDFQENYAGIFHFQFWQYGEWVEVVIDDRLPTKNGQLLFLHSEQGNEFWSALLEKAYAKLNGCYEALAGGSTVEGFEDFTGGISEFYDLKKPPANLYQIIRKALCAGSLLGCSIDVSSAAEAEAITSQKLVKSHAYSVTGVEEVNFQGHPEKLIRLRNPWGEVEWSGAWSDDAPEWNHIDPRRKEELDKKVEDGEFWMSLSDFVRQFSRLEICNLSPDSLSSEEVHKWNLVLFNGHWTRGSTAGGCQNYPATYWTNPQFKIRLDEVDEDQEESIGEPCCTVLLGLMQKNRRWRKRIGQGMLSIGYAVYQVPKELESHTDAHLGRDFFLAYQPSARTSTYVNLREVSGRARLPPGEYLVVPSTFEPFKDGEFCLRVFSEKKAQALEIGDVVAGNPYEPHPSEVDQEDDQFRRLFEKLAGKDSEITANALKILLNEAFSKRTDIKFDGFNINTCREMISLLDSNGTGTLGAVEFKTLWLKIQKYLEIYWETDYNHSGTIDAHEMRTALRKAGFTLNSQVQQTIALRYACSKLGINFDSFVACMIRLETLFKLFSLLDEDKDGMVQLSLAEWLCCVLV |
| Enzyme Length | 703 |
| Uniprot Accession Number | A6NHC0 |
| Absorption | |
| Active Site | ACT_SITE 105; /evidence=ECO:0000250; ACT_SITE 262; /evidence=ECO:0000250; ACT_SITE 286; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.53; |
| DNA Binding | |
| EC Number | 3.4.22.53 |
| Enzyme Function | FUNCTION: Calcium-regulated non-lysosomal thiol-protease. Involved in membrane trafficking in the gastric surface mucus cells (pit cells) and may involve the membrane trafficking of mucus cells via interactions with coat protein. Proteolytically cleaves the beta-subunit of coatomer complex (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (13); Chain (1); Domain (4); Helix (15); Metal binding (10); Region (1); Sequence conflict (2); Turn (1) |
| Keywords | 3D-structure;Autocatalytic cleavage;Calcium;Cytoplasm;Golgi apparatus;Hydrolase;Metal-binding;Protease;Reference proteome;Repeat;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Undergoes autolytic cleavage between Ala-5 and Ala-6 which gives rise to fragments extending from Ala-6 to the C-terminus, Ala-6 to the EF-hand 2 domain and from Ala-6 to the beginning of domain III. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2NQA; |
| Mapped Pubmed ID | 12843408; 17608959; 17646163; 21030783; 21670566; 21864727; 23035980; 28002826; |
| Motif | |
| Gene Encoded By | |
| Mass | 79,144 |
| Kinetics | |
| Metal Binding | METAL 588; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 590; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 592; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 594; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 599; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 618; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 620; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 622; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 624; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 629; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B28; |