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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]

 CASPE_HUMAN             Reviewed;         242 AA.
P31944; O95823; Q3SYC9;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
30-AUG-2017, entry version 160.
RecName: Full=Caspase-14;
Short=CASP-14;
EC=3.4.22.-;
Contains:
RecName: Full=Caspase-14 subunit p17, mature form;
Contains:
RecName: Full=Caspase-14 subunit p10, mature form;
Contains:
RecName: Full=Caspase-14 subunit p20, intermediate form;
Contains:
RecName: Full=Caspase-14 subunit p8, intermediate form;
Flags: Precursor;
Name=CASP14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11062009; DOI=10.1006/bbrc.2000.3698;
Eckhart L., Ban J., Fischer H., Tschachler E.;
"Caspase-14: analysis of gene structure and mRNA expression during
keratinocyte differentiation.";
Biochem. Biophys. Res. Commun. 277:655-659(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=12181750; DOI=10.1038/sj.cdd.4401061;
Pistritto G., Jost M., Srinivasula S.M., Baffa R., Poyet J.-L.,
Kari C., Lazebnik Y., Rodeck U., Alnemri E.S.;
"Expression and transcriptional regulation of caspase-14 in simple and
complex epithelia.";
Cell Death Differ. 9:995-1006(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 68-74; 137-147 AND 154-162.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[5]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11175259; DOI=10.1038/sj.cdd.4400785;
Lippens S., Kockx M., Knaapen M., Mortier L., Polakowska R.,
Verheyen A., Garmyn M., Zwijsen A., Formstecher P., Huylebroeck D.,
Vandenabeele P., Declercq W.;
"Epidermal differentiation does not involve the pro-apoptotic
executioner caspases, but is associated with caspase-14 induction and
processing.";
Cell Death Differ. 7:1218-1224(2000).
[6]
PROTEIN SEQUENCE OF 153-163, PROTEOLYTIC PROCESSING, SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=12200134; DOI=10.1016/S0006-291X(02)02015-6;
Chien A.J., Presland R.B., Kuechle M.K.;
"Processing of native caspase-14 occurs at an atypical cleavage site
in normal epidermal differentiation.";
Biochem. Biophys. Res. Commun. 296:911-917(2002).
[7]
FUNCTION.
PubMed=15301553; DOI=10.1021/bi0498048;
Mikolajczyk J., Scott F.L., Krajewski S., Sutherlin D.P.,
Salvesen G.S.;
"Activation and substrate specificity of caspase-14.";
Biochemistry 43:10560-10569(2004).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15556625; DOI=10.1016/j.febslet.2004.10.046;
Fischer H., Stichenwirth M., Dockal M., Ghannadan M., Buchberger M.,
Bach J., Kapetanopoulos A., Declercq W., Tschachler E., Eckhart L.;
"Stratum corneum-derived caspase-14 is catalytically active.";
FEBS Lett. 577:446-450(2004).
[9]
FUNCTION.
PubMed=16854378; DOI=10.1016/j.bbrc.2006.06.156;
Park K., Kuechle M.K., Choe Y., Craik C.S., Lawrence O.T.,
Presland R.B.;
"Expression and characterization of constitutively active human
caspase-14.";
Biochem. Biophys. Res. Commun. 347:941-948(2006).
[10]
PROTEOLYTIC PROCESSING, SUBUNIT, ENZYME REGULATION, AND FUNCTION.
PubMed=19960512; DOI=10.1002/jcb.22425;
Hibino T., Fujita E., Tsuji Y., Nakanishi J., Iwaki H., Katagiri C.,
Momoi T.;
"Purification and characterization of active caspase-14 from human
epidermis and development of the cleavage site-directed antibody.";
J. Cell. Biochem. 109:487-497(2010).
[11]
PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
SUBUNIT, AND FUNCTION.
PubMed=22825846; DOI=10.1074/jbc.M112.357467;
Yamamoto M., Miyai M., Matsumoto Y., Tsuboi R., Hibino T.;
"Kallikrein-related peptidase-7 regulates caspase-14 maturation during
keratinocyte terminal differentiation by generating an intermediate
form.";
J. Biol. Chem. 287:32825-32834(2012).
[12]
INDUCTION, AND FUNCTION.
PubMed=25121097; DOI=10.1155/2014/417986;
Beasley S., El-Sherbiny M., Megyerdi S., El-Shafey S., Choksi K.,
Kaddour-Djebbar I., Sheibani N., Hsu S., Al-Shabrawey M.;
"Caspase-14 expression impairs retinal pigment epithelium barrier
function: potential role in diabetic macular edema.";
Biomed. Res. Int. 2014:417986-417986(2014).
[13]
FUNCTION.
PubMed=24743736; DOI=10.1038/cddis.2014.145;
Yamamoto-Tanaka M., Makino T., Motoyama A., Miyai M., Tsuboi R.,
Hibino T.;
"Multiple pathways are involved in DNA degradation during keratinocyte
terminal differentiation.";
Cell Death Dis. 5:E1181-E1181(2014).
[14]
INVOLVEMENT IN ARCI12.
PubMed=27494380; DOI=10.2340/00015555-2510;
Kirchmeier P., Zimmer A., Bouadjar B., Roesler B., Fischer J.;
"Whole-Exome-Sequencing reveals small deletions in CASP14 in patients
with autosomal recessive inherited ichthyosis.";
Acta Derm. Venereol. 96:102-104(2017).
-!- 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}.
-!- ENZYME REGULATION: Inhibited by caspase-1 inhibitor YVAD-FMK and
the pan-caspase inhibitor VAD-FMK. {ECO:0000269|PubMed:19960512}.
-!- SUBUNIT: Heterodimer of a large and a small subunit, both
processed from the precursor; the mature active form is a p17/p10
dimer and the intermediate form a p20/p8 dimer.
{ECO:0000269|PubMed:12200134, ECO:0000269|PubMed:19960512,
ECO:0000269|PubMed:22825846}.
-!- INTERACTION:
P50222:MEOX2; NbExp=3; IntAct=EBI-2510738, EBI-748397;
P07602:PSAP; NbExp=3; IntAct=EBI-2510738, EBI-716699;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11175259,
ECO:0000269|PubMed:12200134, ECO:0000269|PubMed:22825846}. Nucleus
{ECO:0000269|PubMed:11175259}.
-!- TISSUE SPECIFICITY: Expressed in keratinocytes of adult skin
suprabasal layers (from spinous layers to the stratum granulosum
and stratum corneum) (at protein level). Expressed in
keratinocytes of hair shaft and sebaceous glands (at protein
level). In psoriatic skin only expressed at very low levels
(PubMed:11175259). The p17/10 mature form is expressed in
epidermis stratum corneum, the p20/p8 intermediate form in
epidermis upper granular cells of the stratum granulosum
(PubMed:22825846). {ECO:0000269|PubMed:11175259,
ECO:0000269|PubMed:15556625, ECO:0000269|PubMed:22825846}.
-!- 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}.
-!- 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}.
-!- DISEASE: Ichthyosis, congenital, autosomal recessive 12 (ARCI12)
[MIM:617320]: A form of autosomal recessive congenital ichthyosis,
a disorder of keratinization with abnormal differentiation and
desquamation of the epidermis, resulting in abnormal skin scaling
over the whole body. The main skin phenotypes are lamellar
ichthyosis (LI) and non-bullous congenital ichthyosiform
erythroderma (NCIE), although phenotypic overlap within the same
patient or among patients from the same family can occur. Lamellar
ichthyosis is a condition often associated with an embedment in a
collodion-like membrane at birth; skin scales later develop,
covering the entire body surface. Non-bullous congenital
ichthyosiform erythroderma characterized by fine whitish scaling
on an erythrodermal background; larger brownish scales are present
on the buttocks, neck and legs. {ECO:0000269|PubMed:27494380}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Expressed in bacteria requires high concentrations
of kosmotropic salts to be activated (PubMed:15301553). The mature
and the intermediate form differ in activity towards synthetic
caspase substrates: the p17/p10 mature form but not the p20/p8
intermediate form is active on WEHD-MCA; p20/p8 is active on a
number of other caspase substrates without any marked preference
(VEID-AFC, DEVD-AFC, LEVD-AFC and LEHD-AFC) (PubMed:22825846).
{ECO:0000269|PubMed:15301553, ECO:0000269|PubMed:22825846}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF097874; AAD16173.1; -; mRNA.
EMBL; BC069541; AAH69541.1; -; mRNA.
EMBL; BC103868; AAI03869.1; -; mRNA.
EMBL; BC103869; AAI03870.1; -; mRNA.
CCDS; CCDS12323.1; -.
PIR; JC7517; JC7517.
RefSeq; NP_036246.1; NM_012114.2.
UniGene; Hs.466057; -.
ProteinModelPortal; P31944; -.
SMR; P31944; -.
BioGrid; 117116; 26.
IntAct; P31944; 10.
STRING; 9606.ENSP00000221740; -.
BindingDB; P31944; -.
ChEMBL; CHEMBL5991; -.
GuidetoPHARMACOLOGY; 1627; -.
MEROPS; C14.018; -.
iPTMnet; P31944; -.
BioMuta; CASP14; -.
DMDM; 12231007; -.
EPD; P31944; -.
MaxQB; P31944; -.
PaxDb; P31944; -.
PeptideAtlas; P31944; -.
PRIDE; P31944; -.
TopDownProteomics; P31944; -.
DNASU; 23581; -.
Ensembl; ENST00000427043; ENSP00000393417; ENSG00000105141.
GeneID; 23581; -.
KEGG; hsa:23581; -.
UCSC; uc010dzv.3; human.
CTD; 23581; -.
DisGeNET; 23581; -.
GeneCards; CASP14; -.
HGNC; HGNC:1502; CASP14.
HPA; CAB010059; -.
HPA; HPA027062; -.
MIM; 605848; gene.
MIM; 617320; phenotype.
neXtProt; NX_P31944; -.
OpenTargets; ENSG00000105141; -.
PharmGKB; PA26085; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOGENOM; HOG000231878; -.
HOVERGEN; HBG050804; -.
InParanoid; P31944; -.
KO; K04401; -.
OMA; STMKRDP; -.
OrthoDB; EOG091G0KY9; -.
PhylomeDB; P31944; -.
TreeFam; TF102023; -.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
ChiTaRS; CASP14; human.
GeneWiki; Caspase_14; -.
GenomeRNAi; 23581; -.
PMAP-CutDB; P31944; -.
PRO; PR:P31944; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105141; -.
CleanEx; HS_CASP14; -.
ExpressionAtlas; P31944; baseline and differential.
Genevisible; P31944; HS.
GO; GO:0005737; C:cytoplasm; IDA:CACAO.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0045095; C:keratin filament; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:CACAO.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:Reactome.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0004175; F:endopeptidase activity; TAS:Reactome.
GO; GO:0070268; P:cornification; TAS:UniProtKB.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0031424; P:keratinization; TAS:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR033174; Caspase-14.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454:SF184; PTHR10454:SF184; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Differentiation;
Direct protein sequencing; Hydrolase; Hypotrichosis; Ichthyosis;
Nucleus; Protease; Reference proteome; Thiol protease; Zymogen.
CHAIN 1 178 Caspase-14 subunit p20, intermediate
form.
/FTId=PRO_0000432793.
PROPEP 1 5 {ECO:0000269|PubMed:19960512}.
/FTId=PRO_0000004652.
CHAIN 6 146 Caspase-14 subunit p17, mature form.
/FTId=PRO_0000432794.
PROPEP 147 152 {ECO:0000269|PubMed:19960512}.
/FTId=PRO_0000432795.
CHAIN 153 242 Caspase-14 subunit p10, mature form.
/FTId=PRO_0000004654.
CHAIN 179 242 Caspase-14 subunit p8, intermediate form.
/FTId=PRO_0000432796.
ACT_SITE 89 89 {ECO:0000250|UniProtKB:P29466}.
ACT_SITE 132 132 {ECO:0000250|UniProtKB:P29466}.
SEQUENCE 242 AA; 27680 MW; E539FB7E8DD808A2 CRC64;
MSNPRSLEEE KYDMSGARLA LILCVTKARE GSEEDLDALE HMFRQLRFES TMKRDPTAEQ
FQEELEKFQQ AIDSREDPVS CAFVVLMAHG REGFLKGEDG EMVKLENLFE ALNNKNCQAL
RAKPKVYIIQ ACRGEQRDPG ETVGGDEIVM VIKDSPQTIP TYTDALHVYS TVEGYIAYRH
DQKGSCFIQT LVDVFTKRKG HILELLTEVT RRMAEAELVQ EGKARKTNPE IQSTLRKRLY
LQ


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