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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]

 CASPE_MOUSE             Reviewed;         257 AA.
O89094;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
05-JUN-2019, entry version 158.
RecName: Full=Caspase-14;
Short=CASP-14;
EC=3.4.22.-;
AltName: Full=Mini-ICE;
Short=MICE;
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
STRAIN=C57BL/6J;
PubMed=9823333;
Ahmad M., Srinivasula S.M., Hegde R., Mukattash R.,
Fernandes-Alnemri T., Alnemri E.S.;
"Identification and characterization of murine caspase-14, a new
member of the caspase family.";
Cancer Res. 58:5201-5205(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=10203698; DOI=10.1038/sj.cdd.4400444;
Van de Craen M., Van Loo G., Pype S., Van Criekinge W.,
Van den brande I., Molemans F., Fiers W., Declercq W.,
Vandenabeele P.;
"Identification of a new caspase homologue: caspase-14.";
Cell Death Differ. 5:838-846(1998).
[3]
CHARACTERIZATION, AND MUTAGENESIS OF CYS-136.
PubMed=9792675; DOI=10.1074/jbc.273.45.29648;
Hu S., Snipas S.J., Vincenz C., Salvesen G., Dixit V.M.;
"Caspase-14 is a novel developmentally regulated protease.";
J. Biol. Chem. 273:29648-29653(1998).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
[5]
ALTERNATIVE SPLICING (ISOFORM 2), AND DEVELOPMENTAL STAGE.
PubMed=11526440; DOI=10.1038/sj.cdd.4400897;
Kuechle M.K., Predd H.M., Fleckman P., Dale B.A., Presland R.B.;
"Caspase-14, a keratinocyte specific caspase: mRNA splice variants and
expression pattern in embryonic and adult mouse.";
Cell Death Differ. 8:868-870(2001).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17515931; DOI=10.1038/ncb1597;
Denecker G., Hoste E., Gilbert B., Hochepied T., Ovaere P.,
Lippens S., Van den Broecke C., Van Damme P., D'Herde K., Hachem J.P.,
Borgonie G., Presland R.B., Schoonjans L., Libert C.,
Vandekerckhove J., Gevaert K., Vandenabeele P., Declercq W.;
"Caspase-14 protects against epidermal UVB photodamage and water
loss.";
Nat. Cell Biol. 9:666-674(2007).
[7]
FUNCTION.
PubMed=18156206; DOI=10.2353/ajpath.2008.070161;
Demerjian M., Hachem J.P., Tschachler E., Denecker G., Declercq W.,
Vandenabeele P., Mauro T., Hupe M., Crumrine D., Roelandt T.,
Houben E., Elias P.M., Feingold K.R.;
"Acute modulations in permeability barrier function regulate epidermal
cornification: role of caspase-14 and the protease-activated receptor
type 2.";
Am. J. Pathol. 172:86-97(2008).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21654840; DOI=10.1038/jid.2011.153;
Hoste E., Kemperman P., Devos M., Denecker G., Kezic S., Yau N.,
Gilbert B., Lippens S., De Groote P., Roelandt R., Van Damme P.,
Gevaert K., Presland R.B., Takahara H., Puppels G., Caspers P.,
Vandenabeele P., Declercq W.;
"Caspase-14 is required for filaggrin degradation to natural
moisturizing factors in the skin.";
J. Invest. Dermatol. 131:2233-2241(2011).
[9]
FUNCTION.
PubMed=24872419; DOI=10.1074/jbc.M113.543421;
Yamamoto-Tanaka M., Motoyama A., Miyai M., Matsunaga Y., Matsuda J.,
Tsuboi R., Hibino T.;
"Mesotrypsin and caspase-14 participate in prosaposin processing:
potential relevance to epidermal permeability barrier formation.";
J. Biol. Chem. 289:20026-20038(2014).
-!- 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}.
-!- 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:0000250|UniProtKB:P31944}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11175259}.
Nucleus {ECO:0000269|PubMed:11175259}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=C14L;
IsoId=O89094-1; Sequence=Displayed;
Name=2; Synonyms=C14S;
IsoId=O89094-2; Sequence=VSP_028925, VSP_028926;
-!- TISSUE SPECIFICITY: Embryo, adult liver and less in adult brain
and kidney. Expressed in differentiating keratinocytes of
embryonic skin (at protein level). Expressed in keratinocytes of
adult skin suprabasal layers (at protein level).
{ECO:0000269|PubMed:10203698, ECO:0000269|PubMed:11175259}.
-!- DEVELOPMENTAL STAGE: Expressed at embryonic day 18 specifically in
cornified epithelium in the suprabasal layers.
{ECO:0000269|PubMed:11526440}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Mice show a shiny and lichenified skin with
an epidermis containing more alveolar keratohyalin F-granules and
an altered profilaggrin processing. The skin is highly sensitive
to the formation of cyclobutane pyrimidine dimers after UVB
irradiation, leading to increased levels of UVB-induced apoptosis
(PubMed:17515931). Mice accumulate incomplete filaggrin breakdown
products within the epidermal stratum corneum (SC), leading to
reduced levels of natural moisturizing factors (NMFs) and lower SC
hydration (PubMed:21654840). {ECO:0000269|PubMed:17515931,
ECO:0000269|PubMed:21654840}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF092997; AAC63364.1; -; mRNA.
EMBL; AJ007750; CAA07678.1; -; mRNA.
CCDS; CCDS23969.1; -. [O89094-1]
RefSeq; NP_033939.1; NM_009809.5. [O89094-1]
RefSeq; XP_006513223.1; XM_006513160.3. [O89094-2]
SMR; O89094; -.
STRING; 10090.ENSMUSP00000005488; -.
MEROPS; C14.018; -.
CarbonylDB; O89094; -.
PhosphoSitePlus; O89094; -.
PaxDb; O89094; -.
PRIDE; O89094; -.
Ensembl; ENSMUST00000005488; ENSMUSP00000005488; ENSMUSG00000005355. [O89094-1]
Ensembl; ENSMUST00000219237; ENSMUSP00000151657; ENSMUSG00000005355. [O89094-1]
GeneID; 12365; -.
KEGG; mmu:12365; -.
UCSC; uc007fyd.2; mouse. [O89094-1]
CTD; 23581; -.
MGI; MGI:1335092; Casp14.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000162117; -.
HOGENOM; HOG000231878; -.
InParanoid; O89094; -.
KO; K04401; -.
OMA; STMKRDP; -.
OrthoDB; 1092723at2759; -.
PhylomeDB; O89094; -.
TreeFam; TF102023; -.
Reactome; R-MMU-6809371; Formation of the cornified envelope.
PRO; PR:O89094; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000005355; Expressed in 36 organ(s), highest expression level in skin epidermis.
ExpressionAtlas; O89094; baseline and differential.
Genevisible; O89094; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0045095; C:keratin filament; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0008233; F:peptidase activity; TAS:MGI.
GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
GO; GO:0070268; P:cornification; IEA:InterPro.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
CDD; cd00032; CASc; 1.
InterPro; IPR033174; Caspase-14.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
PANTHER; PTHR10454:SF131; PTHR10454:SF131; 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;
Alternative splicing; Complete proteome; Cytoplasm; Differentiation;
Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease;
Zymogen.
CHAIN 1 193 Caspase-14 subunit p20, intermediate
form. {ECO:0000250|UniProtKB:P31944}.
/FTId=PRO_0000432797.
PROPEP 1 ? {ECO:0000305}.
/FTId=PRO_0000004655.
CHAIN ? 155 Caspase-14 subunit p17, mature form.
{ECO:0000250|UniProtKB:P31944}.
/FTId=PRO_0000432798.
PROPEP 156 167 {ECO:0000250|UniProtKB:P31944}.
/FTId=PRO_0000432799.
CHAIN 168 257 Caspase-14 subunit p10, mature form.
{ECO:0000250|UniProtKB:P31944}.
/FTId=PRO_0000004657.
CHAIN 194 257 Caspase-14 subunit p8, intermediate form.
{ECO:0000250|UniProtKB:P31944}.
/FTId=PRO_0000432800.
ACT_SITE 93 93 {ECO:0000250|UniProtKB:P29466}.
ACT_SITE 136 136 {ECO:0000250|UniProtKB:P29466}.
VAR_SEQ 139 159 EHRDPGEELRGNEELGGDEEL -> DHPTYGKHGGDAGRKT
KESEP (in isoform 2). {ECO:0000305}.
/FTId=VSP_028925.
VAR_SEQ 160 257 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_028926.
MUTAGEN 136 136 C->A: Decrease in death-inducing
activity. {ECO:0000269|PubMed:9792675}.
SEQUENCE 257 AA; 29458 MW; A228D88DFBA0EB84 CRC64;
MESEMSDPQP LQEERYDMSG ARLALTLCVT KAREGSEVDM EALERMFRYL KFESTMKRDP
TAQQFLEELD EFQQTIDNWE EPVSCAFVVL MAHGEEGLLK GEDEKMVRLE DLFEVLNNKN
CKALRGKPKV YIIQACRGEH RDPGEELRGN EELGGDEELG GDEVAVLKNN PQSIPTYTDT
LHIYSTVEGY LSYRHDEKGS GFIQTLTDVF IHKKGSILEL TEEITRLMAN TEVMQEGKPR
KVNPEVQSTL RKKLYLQ


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[CASP14] 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]
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[Casp2 Ich1] Caspase-2 (CASP-2) (EC 3.4.22.55) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[CASP10 MCH4] Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12]
[ced-3 C48D1.2] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]
[Casp6] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[CASP6 MCH2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[Casp6 Mch2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[AMC9 MCP2F At5g04200 F21E1.120] Metacaspase-9 (AtMC9) (EC 3.4.22.-) [Cleaved into: Metacaspase-9 subunit p20; Metacaspase-9 subunit p10 (Metacaspase 2f) (AtMCP2f)]
[Cflar Cash] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[CD14] Monocyte differentiation antigen CD14 (Myeloid cell-specific leucine-rich glycoprotein) (CD antigen CD14) [Cleaved into: Monocyte differentiation antigen CD14, urinary form; Monocyte differentiation antigen CD14, membrane-bound form]

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