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Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (Cysteine protease LICE2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]

 CASP7_MOUSE             Reviewed;         303 AA.
P97864; O08669;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
12-SEP-2018, entry version 166.
RecName: Full=Caspase-7;
Short=CASP-7;
EC=3.4.22.60;
AltName: Full=Apoptotic protease Mch-3;
AltName: Full=Cysteine protease LICE2;
Contains:
RecName: Full=Caspase-7 subunit p20;
Contains:
RecName: Full=Caspase-7 subunit p11;
Flags: Precursor;
Name=Casp7; Synonyms=Lice2, Mch3;
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].
TISSUE=Skeletal muscle;
PubMed=9070923; DOI=10.1006/geno.1996.4548;
Juan T.S.-C., McNiece I.K., Argento J.M., Jenkins N.A., Gilbert D.J.,
Copeland N.G., Fletcher F.A.;
"Identification and mapping of Casp7, a cysteine protease resembling
CPP32 beta, interleukin-1 beta converting enzyme, and CED-3.";
Genomics 40:86-93(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9125129; DOI=10.1006/bbrc.1997.6234;
Mukasa T., Khoroku Y., Tsukahara T., Momoi M.Y., Kimura I., Momoi T.;
"Wortmannin enhances CPP32-like activity during neuronal
differentiation of P19 embryonal carcinoma cells induced by retinoic
acid.";
Biochem. Biophys. Res. Commun. 232:192-197(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/An;
PubMed=9038361; DOI=10.1016/S0014-5793(97)00026-4;
van de Craen M., Vandenabeele P., Declercq W., van den Brande I.,
van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R.,
Fiers W.;
"Characterization of seven murine caspase family members.";
FEBS Lett. 403:61-69(1997).
[4]
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).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. Cleaves and activates sterol
regulatory element binding proteins (SREBPs). Overexpression
promotes programmed cell death (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at
position P1 and has a preferred cleavage sequence of Asp-Glu-Val-
Asp-|-.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 20 kDa (p20) and a 11
kDa (p11) subunit. Interacts with BIRC6/bruce (By similarity).
{ECO:0000250}.
-!- INTERACTION:
P11103:Parp1; NbExp=3; IntAct=EBI-5307197, EBI-642213;
P62270:Rps18; NbExp=4; IntAct=EBI-5307197, EBI-352460;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Highly expressed in heart, lung, liver and
kidney. Low levels in spleen, skeletal muscle and testis. No
expression in the brain.
-!- PTM: Cleavages by granzyme B or caspase-10 generate the two active
subunits. Propeptide domains can also be cleaved efficiently by
caspase-3. Active heterodimers between the small subunit of
caspase-7 and the large subunit of caspase-3, and vice versa, also
occur (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC53068.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U67321; AAC53068.1; ALT_INIT; mRNA.
EMBL; D86353; BAA19730.1; -; mRNA.
EMBL; Y13088; CAA73530.1; -; mRNA.
EMBL; BC005428; AAH05428.1; -; mRNA.
CCDS; CCDS29915.1; -.
RefSeq; NP_031637.1; NM_007611.2.
UniGene; Mm.35687; -.
ProteinModelPortal; P97864; -.
SMR; P97864; -.
BioGrid; 198499; 7.
IntAct; P97864; 10.
STRING; 10090.ENSMUSP00000026062; -.
MEROPS; C14.004; -.
iPTMnet; P97864; -.
PhosphoSitePlus; P97864; -.
EPD; P97864; -.
PaxDb; P97864; -.
PeptideAtlas; P97864; -.
PRIDE; P97864; -.
Ensembl; ENSMUST00000026062; ENSMUSP00000026062; ENSMUSG00000025076.
GeneID; 12369; -.
KEGG; mmu:12369; -.
UCSC; uc008hyw.1; mouse.
CTD; 840; -.
MGI; MGI:109383; Casp7.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOGENOM; HOG000231878; -.
HOVERGEN; HBG050802; -.
InParanoid; P97864; -.
KO; K04397; -.
OMA; SGSWFVQ; -.
OrthoDB; EOG091G05YD; -.
PhylomeDB; P97864; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.60; 3474.
Reactome; R-MMU-111463; SMAC binds to IAPs.
Reactome; R-MMU-111464; SMAC-mediated dissociation of IAP:caspase complexes.
Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
ChiTaRS; Casp7; mouse.
PMAP-CutDB; P97864; -.
PRO; PR:P97864; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000025076; Expressed in 244 organ(s), highest expression level in pineal body.
CleanEx; MM_CASP7; -.
ExpressionAtlas; P97864; baseline and differential.
Genevisible; P97864; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:MGI.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; ISO:MGI.
GO; GO:0008234; F:cysteine-type peptidase activity; ISO:MGI.
GO; GO:0008233; F:peptidase activity; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IGI:MGI.
GO; GO:0072734; P:cellular response to staurosporine; ISO:MGI.
GO; GO:0097194; P:execution phase of apoptosis; IGI:MGI.
GO; GO:0007507; P:heart development; IGI:MGI.
GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
GO; GO:0016485; P:protein processing; IDA:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0009411; P:response to UV; IGI:MGI.
CDD; cd00032; CASc; 1.
InterPro; IPR015471; Casp3/7.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454:SF31; PTHR10454:SF31; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Complete proteome; Cytoplasm; Hydrolase;
Protease; Reference proteome; Thiol protease; Zymogen.
PROPEP 1 23 {ECO:0000250}.
/FTId=PRO_0000004624.
CHAIN 24 198 Caspase-7 subunit p20. {ECO:0000250}.
/FTId=PRO_0000004625.
PROPEP 199 206 {ECO:0000250}.
/FTId=PRO_0000004626.
CHAIN 207 303 Caspase-7 subunit p11. {ECO:0000250}.
/FTId=PRO_0000004627.
ACT_SITE 144 144 {ECO:0000250}.
ACT_SITE 186 186 {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:17242355}.
CONFLICT 10 11 EL -> DW (in Ref. 2; BAA19730).
{ECO:0000305}.
CONFLICT 45 45 A -> T (in Ref. 2; BAA19730).
{ECO:0000305}.
CONFLICT 48 49 VR -> RQ (in Ref. 2; BAA19730).
{ECO:0000305}.
SEQUENCE 303 AA; 34061 MW; 747787B5BDE5F744 CRC64;
MTDDQDCAAE LEKVDSSSED GVDAKPDRSS IISSILLKKK RNASAGPVRT GRDRVPTYLY
RMDFQKMGKC IIINNKNFDK ATGMDVRNGT DKDAGALFKC FQNLGFEVTV HNDCSCAKMQ
DLLRKASEED HSNSACFACV LLSHGEEDLI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL
FFIQACRGTE LDDGIQADSG PINDIDANPR NKIPVEADFL FAYSTVPGYY SWRNPGKGSW
FVQALCSILN EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP RFNEKKQIPC MVSMLTKELY
FSR


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