| IED ID | IndEnz0002004743 |
| Enzyme Type ID | protease004743 |
| Protein Name |
Caspase-14 CASP-14 EC 3.4.22.- 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 | 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 | MSNPRSLEEEKYDMSGARLALILCVTKAREGSEEDLDALEHMFRQLRFESTMKRDPTAEQFQEELEKFQQAIDSREDPVSCAFVVLMAHGREGFLKGEDGEMVKLENLFEALNNKNCQALRAKPKVYIIQACRGEQRDPGETVGGDEIVMVIKDSPQTIPTYTDALHVYSTVEGYIAYRHDQKGSCFIQTLVDVFTKRKGHILELLTEVTRRMAEAELVQEGKARKTNPEIQSTLRKRLYLQ |
| Enzyme Length | 242 |
| Uniprot Accession Number | P31944 |
| Absorption | |
| Active Site | ACT_SITE 89; /evidence=ECO:0000250|UniProtKB:P29466; ACT_SITE 132; /evidence=ECO:0000250|UniProtKB:P29466 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by caspase-1 inhibitor YVAD-FMK and the pan-caspase inhibitor VAD-FMK. {ECO:0000269|PubMed:19960512}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Non-apoptotic caspase involved in epidermal differentiation. Is the predominant caspase in epidermal stratum corneum (PubMed:15556625). Seems to play a role in keratinocyte differentiation and is required for cornification. Regulates maturation of the epidermis by proteolytically processing filaggrin (By similarity). In vitro has a preference for the substrate [WY]-X-X-D motif and is active on the synthetic caspase substrate WEHD-ACF (PubMed:16854378, PubMed:19960512). Involved in processing of prosaposin in the epidermis (By similarity). May be involved in retinal pigment epithelium cell barrier function (PubMed:25121097). Involved in DNA degradation in differentiated keratinocytes probably by cleaving DFFA/ICAD leading to liberation of DFFB/CAD (PubMed:24743736). {ECO:0000250|UniProtKB:O89094, ECO:0000269|PubMed:15301553, ECO:0000269|PubMed:15556625, ECO:0000269|PubMed:16854378, ECO:0000269|PubMed:19960512, ECO:0000269|PubMed:22825846, ECO:0000269|PubMed:24743736, ECO:0000305|PubMed:25121097}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (4); Propeptide (2) |
| Keywords | Cytoplasm;Differentiation;Direct protein sequencing;Hydrolase;Ichthyosis;Nucleus;Protease;Reference proteome;Thiol protease;Zymogen |
| Interact With | P50222; P07602 |
| Induction | INDUCTION: In undifferentiated keratinocytes under postconfluency growth conditions (in vitro) (PubMed:11175259). By high glucose in retinal pigment epithelia cells (PubMed:25121097). {ECO:0000269|PubMed:11175259, ECO:0000269|PubMed:25121097}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11175259, ECO:0000269|PubMed:12200134, ECO:0000269|PubMed:22825846}. 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 on the precursor to yield the p17/p10 mature form (PubMed:22825846). Initially, cleavage between Ile-152 and Lys-153 has been proposed to yield the large and small subunits of the active enzyme (PubMed:12200134). {ECO:0000269|PubMed:19960512, ECO:0000269|PubMed:22825846, ECO:0000305|PubMed:12200134}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12445205; 15331408; 15619438; 16061209; 16061862; 16168224; 17359582; 17436577; 17515931; 17558860; 18424262; 18762957; 19269008; 19414860; 19573080; 19615732; 19747408; 19773279; 20179351; 20237496; 20402676; 20533828; 20562859; 21539619; 21567094; 21654840; 21930782; 21997417; 22038833; 22548721; 23362869; 23377137; 23408445; 23580611; 23629652; 23645350; 24872419; 25315296; 25416956; 25651379; 26212323; 28570747; 34070382; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,680 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |