Reviewed, UniProtKB/Swiss-Prot P97864 (CASP7_MOUSE)

Names and origin

Protein names

Recommended name:
    Caspase-7
      Short name=CASP-7
    EC=3.4.22.60
Alternative name(s):
    LICE2 cysteine protease
    Apoptotic protease Mch-3
Cleaved into the following 2 chains:
    1- Recommended name:
            Caspase-7 subunit p20
    2- Recommended name:
            Caspase-7 subunit p11

Gene names

Name:	Casp7
Synonyms:	Lice2, Mch3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Catalytic activity	Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.
Subunit structure	Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit.
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.
Post-translational modification	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.
Sequence similarities	Belongs to the peptidase C14A family.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein Zymogen
Gene Ontology (GO)
Biological process	heart development Inferred from genetic interaction. Source: MGI induction of apoptosis Inferred from genetic interaction. Source: MGI release of cytochrome c from mitochondria Inferred from genetic interaction. Source: MGI response to UV Inferred from genetic interaction. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 23	23	By similarity		PRO_0000004624
	Chain	24 – 198	175	Caspase-7 subunit p20 By similarity		PRO_0000004625
	Propeptide	199 – 206	8	By similarity		PRO_0000004626
	Chain	207 – 303	97	Caspase-7 subunit p11 By similarity		PRO_0000004627
Sites
	Active site	144	1	By similarity
	Active site	186	1	By similarity
Amino acid modifications
	Modified residue	16	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	10 – 11	2	EL → DW in BAA19730. Ref.2
	Sequence conflict	45	1	A → T in BAA19730. Ref.2
	Sequence conflict	48 – 49	2	VR → RQ in BAA19730. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P97864-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 747787B5BDE5F744	FASTA	303	34,061
	10 20 30 40 50 60 MTDDQDCAAE LEKVDSSSED GVDAKPDRSS IISSILLKKK RNASAGPVRT GRDRVPTYLY 70 80 90 100 110 120 RMDFQKMGKC IIINNKNFDK ATGMDVRNGT DKDAGALFKC FQNLGFEVTV HNDCSCAKMQ 130 140 150 160 170 180 DLLRKASEED HSNSACFACV LLSHGEEDLI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL 190 200 210 220 230 240 FFIQACRGTE LDDGIQADSG PINDIDANPR NKIPVEADFL FAYSTVPGYY SWRNPGKGSW 250 260 270 280 290 300 FVQALCSILN EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP RFNEKKQIPC MVSMLTKELY FSR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and mapping of Casp7, a cysteine protease resembling CPP32 beta, interleukin-1 beta converting enzyme, and CED-3." Juan T.S.-C., McNiece I.K., Argento J.M., Jenkins N.A., Gilbert D.J., Copeland N.G., Fletcher F.A. Genomics 40:86-93(1997) [PubMed: 9070923] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[2]	"Wortmannin enhances CPP32-like activity during neuronal differentiation of P19 embryonal carcinoma cells induced by retinoic acid." Mukasa T., Khoroku Y., Tsukahara T., Momoi M.Y., Kimura I., Momoi T. Biochem. Biophys. Res. Commun. 232:192-197(1997) [PubMed: 9125129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Characterization of seven murine caspase family members." 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. FEBS Lett. 403:61-69(1997) [PubMed: 9038361] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C3H/An.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U67321 mRNA. Translation: AAC53068.1. Different initiation. D86353 mRNA. Translation: BAA19730.1. Y13088 mRNA. Translation: CAA73530.1. BC005428 mRNA. Translation: AAH05428.1.
IPI	IPI00130131.
RefSeq	NP_031637.1.
UniGene	Mm.35687
3D structure databases
HSSP	HSSP built from PDB template 1F1J based on UniProtKB P55210.
SMR	P97864. Positions 48-303.
ModBase	Search...
Protein-protein interaction databases
STRING	P97864.
Protein family/group databases
MEROPS	C14.004.
PTM databases
PhosphoSite	P97864.
Proteomic databases
PRIDE	P97864.
Genome annotation databases
Ensembl	ENSMUST00000026062; ENSMUSP00000026062; ENSMUSG00000025076; Mus musculus. [Genome view]
GeneID	12369.
KEGG	mmu:12369.
UCSC	uc008hyw.1. mouse.
Organism-specific databases
CTD	12369.
MGI	MGI:109383. Casp7.
Phylogenomic databases
HOGENOM	P97864.
HOVERGEN	P97864.
OMA	NDCSCAK.
Enzyme and pathway databases
BRENDA	3.4.22.60. 244.
Gene expression databases
ArrayExpress	P97864.
Bgee	P97864.
CleanEx	MM_CASP7.
Genevestigator	P97864.
GermOnline	ENSMUSG00000025076. Mus musculus.
Family and domain databases
InterPro	IPR015471. Casp7. IPR011600. Pept_C14_cat. IPR001309. Pept_C14_ICE_p20. IPR016129. Pept_C14_ICE_p20_AS. IPR002138. Pept_C14_p10. IPR002398. Pept_C14_p45. IPR015917. Pept_C14_p45_core. [Graphical view]
PANTHER	PTHR10454:SF31. Casp7. 1 hit. PTHR10454. Pept_C14_p45. 1 hit.
Pfam	PF00656. Peptidase_C14. 1 hit. [Graphical view]
PRINTS	PR00376. IL1BCENZYME.
SMART	SM00115. CASc. 1 hit. [Graphical view]
PROSITE	PS01122. CASPASE_CYS. 1 hit. PS01121. CASPASE_HIS. 1 hit. PS50207. CASPASE_P10. 1 hit. PS50208. CASPASE_P20. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	281060.
PMAP-CutDB	P97864.
SOURCE	Search...

Entry information

Entry name

CASP7_MOUSE

Accession

Primary (citable) accession number: P97864
Secondary accession number(s): O08669

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 3, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)