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CASPE_MOUSE
ID   CASPE_MOUSE             Reviewed;         257 AA.
AC   O89094;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=Caspase-14;
DE            Short=CASP-14;
DE            EC=3.4.22.-;
DE   AltName: Full=Mini-ICE;
DE            Short=MICE;
DE   Contains:
DE     RecName: Full=Caspase-14 subunit p17, mature form;
DE   Contains:
DE     RecName: Full=Caspase-14 subunit p10, mature form;
DE   Contains:
DE     RecName: Full=Caspase-14 subunit p20, intermediate form;
DE   Contains:
DE     RecName: Full=Caspase-14 subunit p8, intermediate form;
DE   Flags: Precursor;
GN   Name=Casp14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC   STRAIN=C57BL/6J;
RX   PubMed=9823333;
RA   Ahmad M., Srinivasula S.M., Hegde R., Mukattash R., Fernandes-Alnemri T.,
RA   Alnemri E.S.;
RT   "Identification and characterization of murine caspase-14, a new member of
RT   the caspase family.";
RL   Cancer Res. 58:5201-5205(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=10203698; DOI=10.1038/sj.cdd.4400444;
RA   Van de Craen M., Van Loo G., Pype S., Van Criekinge W., Van den brande I.,
RA   Molemans F., Fiers W., Declercq W., Vandenabeele P.;
RT   "Identification of a new caspase homologue: caspase-14.";
RL   Cell Death Differ. 5:838-846(1998).
RN   [3]
RP   CHARACTERIZATION, AND MUTAGENESIS OF CYS-136.
RX   PubMed=9792675; DOI=10.1074/jbc.273.45.29648;
RA   Hu S., Snipas S.J., Vincenz C., Salvesen G., Dixit V.M.;
RT   "Caspase-14 is a novel developmentally regulated protease.";
RL   J. Biol. Chem. 273:29648-29653(1998).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11175259; DOI=10.1038/sj.cdd.4400785;
RA   Lippens S., Kockx M., Knaapen M., Mortier L., Polakowska R., Verheyen A.,
RA   Garmyn M., Zwijsen A., Formstecher P., Huylebroeck D., Vandenabeele P.,
RA   Declercq W.;
RT   "Epidermal differentiation does not involve the pro-apoptotic executioner
RT   caspases, but is associated with caspase-14 induction and processing.";
RL   Cell Death Differ. 7:1218-1224(2000).
RN   [5]
RP   ALTERNATIVE SPLICING (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RX   PubMed=11526440; DOI=10.1038/sj.cdd.4400897;
RA   Kuechle M.K., Predd H.M., Fleckman P., Dale B.A., Presland R.B.;
RT   "Caspase-14, a keratinocyte specific caspase: mRNA splice variants and
RT   expression pattern in embryonic and adult mouse.";
RL   Cell Death Differ. 8:868-870(2001).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17515931; DOI=10.1038/ncb1597;
RA   Denecker G., Hoste E., Gilbert B., Hochepied T., Ovaere P., Lippens S.,
RA   Van den Broecke C., Van Damme P., D'Herde K., Hachem J.P., Borgonie G.,
RA   Presland R.B., Schoonjans L., Libert C., Vandekerckhove J., Gevaert K.,
RA   Vandenabeele P., Declercq W.;
RT   "Caspase-14 protects against epidermal UVB photodamage and water loss.";
RL   Nat. Cell Biol. 9:666-674(2007).
RN   [7]
RP   FUNCTION.
RX   PubMed=18156206; DOI=10.2353/ajpath.2008.070161;
RA   Demerjian M., Hachem J.P., Tschachler E., Denecker G., Declercq W.,
RA   Vandenabeele P., Mauro T., Hupe M., Crumrine D., Roelandt T., Houben E.,
RA   Elias P.M., Feingold K.R.;
RT   "Acute modulations in permeability barrier function regulate epidermal
RT   cornification: role of caspase-14 and the protease-activated receptor type
RT   2.";
RL   Am. J. Pathol. 172:86-97(2008).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21654840; DOI=10.1038/jid.2011.153;
RA   Hoste E., Kemperman P., Devos M., Denecker G., Kezic S., Yau N.,
RA   Gilbert B., Lippens S., De Groote P., Roelandt R., Van Damme P.,
RA   Gevaert K., Presland R.B., Takahara H., Puppels G., Caspers P.,
RA   Vandenabeele P., Declercq W.;
RT   "Caspase-14 is required for filaggrin degradation to natural moisturizing
RT   factors in the skin.";
RL   J. Invest. Dermatol. 131:2233-2241(2011).
RN   [9]
RP   FUNCTION.
RX   PubMed=24872419; DOI=10.1074/jbc.m113.543421;
RA   Yamamoto-Tanaka M., Motoyama A., Miyai M., Matsunaga Y., Matsuda J.,
RA   Tsuboi R., Hibino T.;
RT   "Mesotrypsin and caspase-14 participate in prosaposin processing: potential
RT   relevance to epidermal permeability barrier formation.";
RL   J. Biol. Chem. 289:20026-20038(2014).
CC   -!- FUNCTION: Non-apoptotic caspase which is involved in epidermal
CC       differentiation. Seems to play a role in keratinocyte differentiation
CC       and is required for cornification (PubMed:18156206). Regulates
CC       maturation of the epidermis by proteolytically processing filaggrin
CC       (PubMed:21654840). In vitro is equally active on the synthetic caspase
CC       substrates WEHD-ACF and IETD-AFC. Involved in processing of prosaposin
CC       in the epidermis (PubMed:24872419). May be involved in retinal pigment
CC       epithelium cell barrier function (By similarity).
CC       {ECO:0000250|UniProtKB:P31944, ECO:0000269|PubMed:11175259,
CC       ECO:0000269|PubMed:17515931, ECO:0000269|PubMed:18156206,
CC       ECO:0000269|PubMed:21654840, ECO:0000269|PubMed:24872419}.
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit, both processed
CC       from the precursor; the mature active form is a p17/p10 dimer and the
CC       intermediate form a p20/p8 dimer. {ECO:0000250|UniProtKB:P31944}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11175259}. Nucleus
CC       {ECO:0000269|PubMed:11175259}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=C14L;
CC         IsoId=O89094-1; Sequence=Displayed;
CC       Name=2; Synonyms=C14S;
CC         IsoId=O89094-2; Sequence=VSP_028925, VSP_028926;
CC   -!- TISSUE SPECIFICITY: Embryo, adult liver and less in adult brain and
CC       kidney. Expressed in differentiating keratinocytes of embryonic skin
CC       (at protein level). Expressed in keratinocytes of adult skin suprabasal
CC       layers (at protein level). {ECO:0000269|PubMed:10203698,
CC       ECO:0000269|PubMed:11175259}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at embryonic day 18 specifically in
CC       cornified epithelium in the suprabasal layers.
CC       {ECO:0000269|PubMed:11526440}.
CC   -!- PTM: Maturation by proteolytic processing appears to be a two-step
CC       process. The precursor is processed by KLK7 to yield the p20/p8
CC       intermediate form which acts the precursor to yield the p17/p10 mature
CC       form (By similarity). Initially it was reported that cleavage by
CC       granzyme B, caspase-8 and -10 generates the two active subunits,
CC       however the physiological relevance has not been established
CC       (PubMed:9823333). {ECO:0000250|UniProtKB:P31944,
CC       ECO:0000305|PubMed:9823333}.
CC   -!- DISRUPTION PHENOTYPE: Mice show a shiny and lichenified skin with an
CC       epidermis containing more alveolar keratohyalin F-granules and an
CC       altered profilaggrin processing. The skin is highly sensitive to the
CC       formation of cyclobutane pyrimidine dimers after UVB irradiation,
CC       leading to increased levels of UVB-induced apoptosis (PubMed:17515931).
CC       Mice accumulate incomplete filaggrin breakdown products within the
CC       epidermal stratum corneum (SC), leading to reduced levels of natural
CC       moisturizing factors (NMFs) and lower SC hydration (PubMed:21654840).
CC       {ECO:0000269|PubMed:17515931, ECO:0000269|PubMed:21654840}.
CC   -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR   EMBL; AF092997; AAC63364.1; -; mRNA.
DR   EMBL; AJ007750; CAA07678.1; -; mRNA.
DR   CCDS; CCDS23969.1; -. [O89094-1]
DR   RefSeq; NP_033939.1; NM_009809.5. [O89094-1]
DR   RefSeq; XP_006513223.1; XM_006513160.3. [O89094-2]
DR   AlphaFoldDB; O89094; -.
DR   SMR; O89094; -.
DR   STRING; 10090.ENSMUSP00000005488; -.
DR   MEROPS; C14.018; -.
DR   CarbonylDB; O89094; -.
DR   PhosphoSitePlus; O89094; -.
DR   MaxQB; O89094; -.
DR   PaxDb; O89094; -.
DR   PRIDE; O89094; -.
DR   ProteomicsDB; 265537; -. [O89094-1]
DR   ProteomicsDB; 265538; -. [O89094-2]
DR   Antibodypedia; 4107; 496 antibodies from 45 providers.
DR   DNASU; 12365; -.
DR   Ensembl; ENSMUST00000005488; ENSMUSP00000005488; ENSMUSG00000005355. [O89094-1]
DR   Ensembl; ENSMUST00000219237; ENSMUSP00000151657; ENSMUSG00000005355. [O89094-1]
DR   GeneID; 12365; -.
DR   KEGG; mmu:12365; -.
DR   UCSC; uc007fyd.2; mouse. [O89094-1]
DR   CTD; 23581; -.
DR   MGI; MGI:1335092; Casp14.
DR   VEuPathDB; HostDB:ENSMUSG00000005355; -.
DR   eggNOG; KOG3573; Eukaryota.
DR   GeneTree; ENSGT00940000162117; -.
DR   HOGENOM; CLU_036904_2_2_1; -.
DR   InParanoid; O89094; -.
DR   OMA; YRHDKDG; -.
DR   PhylomeDB; O89094; -.
DR   TreeFam; TF102023; -.
DR   Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR   BioGRID-ORCS; 12365; 1 hit in 74 CRISPR screens.
DR   PRO; PR:O89094; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; O89094; protein.
DR   Bgee; ENSMUSG00000005355; Expressed in lip and 23 other tissues.
DR   ExpressionAtlas; O89094; baseline and differential.
DR   Genevisible; O89094; MM.
DR   GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0045095; C:keratin filament; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; TAS:MGI.
DR   GO; GO:0070268; P:cornification; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00032; CASc; 1.
DR   InterPro; IPR033174; Caspase-14.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR033139; Caspase_cys_AS.
DR   InterPro; IPR002398; Pept_C14.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR001309; Pept_C14_p20.
DR   InterPro; IPR015917; Pept_C14A.
DR   PANTHER; PTHR10454; PTHR10454; 1.
DR   PANTHER; PTHR10454:SF131; PTHR10454:SF131; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 1.
DR   SUPFAM; SSF52129; SSF52129; 1.
DR   PROSITE; PS01122; CASPASE_CYS; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Differentiation; Hydrolase; Nucleus;
KW   Protease; Reference proteome; Thiol protease; Zymogen.
FT   CHAIN           1..193
FT                   /note="Caspase-14 subunit p20, intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P31944"
FT                   /id="PRO_0000432797"
FT   PROPEP          1..?
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000004655"
FT   CHAIN           ?..155
FT                   /note="Caspase-14 subunit p17, mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P31944"
FT                   /id="PRO_0000432798"
FT   PROPEP          156..167
FT                   /evidence="ECO:0000250|UniProtKB:P31944"
FT                   /id="PRO_0000432799"
FT   CHAIN           168..257
FT                   /note="Caspase-14 subunit p10, mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P31944"
FT                   /id="PRO_0000004657"
FT   CHAIN           194..257
FT                   /note="Caspase-14 subunit p8, intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P31944"
FT                   /id="PRO_0000432800"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000250|UniProtKB:P29466"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000250|UniProtKB:P29466"
FT   VAR_SEQ         139..159
FT                   /note="EHRDPGEELRGNEELGGDEEL -> DHPTYGKHGGDAGRKTKESEP (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_028925"
FT   VAR_SEQ         160..257
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_028926"
FT   MUTAGEN         136
FT                   /note="C->A: Decrease in death-inducing activity."
FT                   /evidence="ECO:0000269|PubMed:9792675"
SQ   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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