Caspase-7 precursor - Mus musculus (Mouse)

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P97864 (CASP7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Caspase-7
Short name=CASP-7
EC=3.4.22.60

Alternative name(s):
Apoptotic protease Mch-3
Cysteine protease LICE2

Gene names

Name:	Casp7
Synonyms:	Lice2, Mch3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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. Interacts with BIRC6/bruce By similarity.
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.
Sequence caution	The sequence AAC53068.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	heart development Inferred from genetic interaction PubMed 16469926. Source: MGI induction of apoptosis Inferred from genetic interaction PubMed 16469926. Source: MGI positive regulation of neuron apoptotic process Inferred from direct assay PubMed 15231831. Source: MGI protein processing Inferred from direct assay PubMed 15231831. Source: MGI proteolysis Inferred from electronic annotation. Source: UniProtKB-KW release of cytochrome c from mitochondria Inferred from genetic interaction PubMed 16469926. Source: MGI response to UV Inferred from genetic interaction PubMed 16469926. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	aspartic-type endopeptidase activity Inferred from direct assay PubMed 15231831. Source: MGI cysteine-type endopeptidase activity Inferred from direct assay PubMed 19759058. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Parp1	P11103	3	EBI-5307197,EBI-642213
Rps18	P62270	4	EBI-5307197,EBI-352460

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 23

By similarity

PRO_0000004624

Chain

24 – 198

175

Caspase-7 subunit p20 By similarity

PRO_0000004625

Propeptide

199 – 206

By similarity

PRO_0000004626

Chain

207 – 303

Caspase-7 subunit p11 By similarity

PRO_0000004627

Sites

Active site

144

By similarity

Active site

186

By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.5

Experimental info

Sequence conflict

10 – 11

EL → DW in BAA19730. Ref.2

Sequence conflict

A → T in BAA19730. Ref.2

Sequence conflict

48 – 49

VR → RQ in BAA19730. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P97864 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 747787B5BDE5F744
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. NM_007611.2.
UniGene	Mm.35687.
3D structure databases
ProteinModelPortal	P97864.
SMR	P97864. Positions 48-303.
ModBase	Search...
Protein-protein interaction databases
IntAct	P97864. 10 interactions.
STRING	10090.ENSMUSP00000026062.
Protein family/group databases
MEROPS	C14.004.
PTM databases
PhosphoSite	P97864.
Proteomic databases
PaxDb	P97864.
PRIDE	P97864.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026062; ENSMUSP00000026062; ENSMUSG00000025076.
GeneID	12369.
KEGG	mmu:12369.
Organism-specific databases
CTD	840.
MGI	MGI:109383. Casp7.
Phylogenomic databases
eggNOG	NOG279444.
HOGENOM	HOG000231878.
HOVERGEN	HBG050802.
InParanoid	P97864.
KO	K04397.
OMA	DANPRHK.
OrthoDB	EOG4DBTF3.
Enzyme and pathway databases
BRENDA	3.4.22.60. 3474.
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. PTHR10454. 1 hit. PTHR10454:SF31. PTHR10454:SF31. 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
ChiTaRS	CASP7. mouse.
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:	April 3, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents