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Caspase 14

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Enzyme found in humans
CASP14
Identifiers
AliasesCASP14, caspase 14, ARCI12
External IDsOMIM: 605848; MGI: 1335092; HomoloGene: 36304; GeneCards: CASP14; OMA:CASP14 - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)
Chromosome 19 (human)Genomic location for CASP14Genomic location for CASP14
Band19p13.12Start15,049,480 bp
End15,058,293 bp
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)
Chromosome 10 (mouse)Genomic location for CASP14Genomic location for CASP14
Band10|10 C1Start78,547,825 bp
End78,554,128 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • skin of abdomen

  • skin of leg

  • skin of arm

  • vulva

  • testicle

  • vagina

  • human penis

  • skin of thigh

  • tibialis anterior muscle

  • mucosa of ileum
Top expressed in
  • lip

  • esophagus

  • skin of back

  • umbilical cord

  • skin of abdomen

  • skin of external ear

  • left colon

  • sexually immature organism

  • epidermis

  • cornea
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23581

12365

Ensembl

ENSG00000105141

ENSMUSG00000005355

UniProt

P31944

O89094

RefSeq (mRNA)

NM_012114

NM_009809

RefSeq (protein)

NP_036246

NP_033939

Location (UCSC)Chr 19: 15.05 – 15.06 MbChr 10: 78.55 – 78.55 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Caspase 14 is an enzyme that in humans is encoded by the CASP14 gene. Orthologs of this gene also exist in other mammals, such as sirenians and cetaceans, though they are inactivated in these two clades. Curiously, manatees, which are sirenians, retain some functional CASP14 genes.

The CASP14 gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This caspase has been shown to be processed and activated by caspase 8 and caspase 10 in vitro, and by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this caspase may be involved in keratinocyte terminal differentiation, which is important for the formation of the skin barrier.

According to the Human Protein Atlas, the CASP14 protein is enriched in human skin and mainly expressed in the upper layers of the epidermis. The protein is mainly localised to the cytosol according to the Cell Atlas.

See also

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000105141Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000005355Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Van de Craen M, Van Loo G, Pype S, Van Criekinge W, Van den brande I, Molemans F, Fiers W, Declercq W, Vandenabeele P (May 1999). "Identification of a new caspase homologue: caspase-14". Cell Death Differ. 5 (10): 838–46. doi:10.1038/sj.cdd.4400444. PMID 10203698.
  6. Hu S, Snipas SJ, Vincenz C, Salvesen G, Dixit VM (Dec 1998). "Caspase-14 is a novel developmentally regulated protease". J Biol Chem. 273 (45): 29648–53. doi:10.1074/jbc.273.45.29648. PMID 9792675.
  7. ^ "Entrez Gene: CASP14 caspase 14, apoptosis-related cysteine peptidase".
  8. Steinbinder, Julia; Sachslehner, Attila Placido; Holthaus, Karin Brigit; Eckhart, Leopold (2024-04-23). "Comparative genomics of sirenians reveals evolution of filaggrin and caspase-14 upon adaptation of the epidermis to aquatic life". Scientific Reports. 14 (1): 9278. doi:10.1038/s41598-024-60099-2. ISSN 2045-2322. PMC 11039687. PMID 38653760.
  9. Uhlén, Mathias; Fagerberg, Linn; Hallström, Björn M.; Lindskog, Cecilia; Oksvold, Per; Mardinoglu, Adil; Sivertsson, Åsa; Kampf, Caroline; Sjöstedt, Evelina (2015-01-23). "Tissue-based map of the human proteome". Science. 347 (6220): 1260419. doi:10.1126/science.1260419. ISSN 0036-8075. PMID 25613900. S2CID 802377.
  10. Thul, Peter J.; Åkesson, Lovisa; Wiking, Mikaela; Mahdessian, Diana; Geladaki, Aikaterini; Blal, Hammou Ait; Alm, Tove; Asplund, Anna; Björk, Lars (2017-05-26). "A subcellular map of the human proteome". Science. 356 (6340): eaal3321. doi:10.1126/science.aal3321. ISSN 0036-8075. PMID 28495876. S2CID 10744558.

Further reading

External links

Proteases: cysteine proteases (EC 3.4.22)
Caspase
Fruit-derived
Calpain
Cathepsin
Other


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