IED ID | IndEnz0002018848 |
Enzyme Type ID | protease018848 |
Protein Name |
Caspase-14 CASP-14 EC 3.4.22.- Mini-ICE MICE Cleaved into: Caspase-14 subunit p17, mature form; Caspase-14 subunit p10, mature form; Caspase-14 subunit p20, intermediate form; Caspase-14 subunit p8, intermediate form |
Gene Name | Casp14 |
Organism | Mus musculus (Mouse) |
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
Enzyme Sequence | MESEMSDPQPLQEERYDMSGARLALTLCVTKAREGSEVDMEALERMFRYLKFESTMKRDPTAQQFLEELDEFQQTIDNWEEPVSCAFVVLMAHGEEGLLKGEDEKMVRLEDLFEVLNNKNCKALRGKPKVYIIQACRGEHRDPGEELRGNEELGGDEELGGDEVAVLKNNPQSIPTYTDTLHIYSTVEGYLSYRHDEKGSGFIQTLTDVFIHKKGSILELTEEITRLMANTEVMQEGKPRKVNPEVQSTLRKKLYLQ |
Enzyme Length | 257 |
Uniprot Accession Number | O89094 |
Absorption | |
Active Site | ACT_SITE 93; /evidence=ECO:0000250|UniProtKB:P29466; ACT_SITE 136; /evidence=ECO:0000250|UniProtKB:P29466 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Non-apoptotic caspase which is involved in epidermal differentiation. Seems to play a role in keratinocyte differentiation and is required for cornification (PubMed:18156206). Regulates maturation of the epidermis by proteolytically processing filaggrin (PubMed:21654840). In vitro is equally active on the synthetic caspase substrates WEHD-ACF and IETD-AFC. Involved in processing of prosaposin in the epidermis (PubMed:24872419). May be involved in retinal pigment epithelium cell barrier function (By similarity). {ECO:0000250|UniProtKB:P31944, ECO:0000269|PubMed:11175259, ECO:0000269|PubMed:17515931, ECO:0000269|PubMed:18156206, ECO:0000269|PubMed:21654840, ECO:0000269|PubMed:24872419}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Alternative sequence (2); Chain (4); Mutagenesis (1); Propeptide (2) |
Keywords | Alternative splicing;Cytoplasm;Differentiation;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11175259}. Nucleus {ECO:0000269|PubMed:11175259}. |
Modified Residue | |
Post Translational Modification | PTM: Maturation by proteolytic processing appears to be a two-step process. The precursor is processed by KLK7 to yield the p20/p8 intermediate form which acts the precursor to yield the p17/p10 mature form (By similarity). Initially it was reported that cleavage by granzyme B, caspase-8 and -10 generates the two active subunits, however the physiological relevance has not been established (PubMed:9823333). {ECO:0000250|UniProtKB:P31944, ECO:0000305|PubMed:9823333}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12200134; 12466851; 12819136; 15316008; 16316411; 18039792; 19092943; 19749746; 20337194; 21267068; 21930782; 22931922; 23014340; 23800061; 26644517; 27709293; 28923684; 29044125; 29317263; |
Motif | |
Gene Encoded By | |
Mass | 29,458 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |