P55214 (CASP7_MESAU) Reviewed, UniProtKB/Swiss-Prot

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
ICE-like apoptotic protease 3
Short name=ICE-LAP3
SREBP cleavage activity 2
Short name=SCA-2

Cleaved into the following 2 chains:

1. Caspase-7 subunit p20
2. Caspase-7 subunit p11

Gene names

Name:	CASP7
Synonyms:	MCH3

Organism

Mesocricetus auratus (Golden hamster)

Taxonomic identifier

10036 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

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). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. 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 By similarity.
Subcellular location	Cytoplasm.
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	Acetylation Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
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
	Initiator methionine	1	1	Removed By similarity
	Propeptide	2 – 23	22			PRO_0000004620
	Chain	24 – 198	175	Caspase-7 subunit p20		PRO_0000004621
	Propeptide	199 – 206	8	By similarity		PRO_0000004622
	Chain	207 – 303	97	Caspase-7 subunit p11		PRO_0000004623
Sites
	Active site	144	1	By similarity
	Active site	186	1	By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P55214 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EA29356D90984648	FASTA	303	34,038
	10 20 30 40 50 60 MADDQNCAPE LEKADPSGED GVDAKPDRSS IISSILGKKK KNASACPVKT ARDRVPTYLY 70 80 90 100 110 120 RMDFEKMGKC IIINNKNFDK VTGMDVRNGT DKDAEALFKC FRSLGFDVVV YNDCSCAKMQ 130 140 150 160 170 180 DLLRKASEED HSNSACFACV LLSHGEENLI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL 190 200 210 220 230 240 FFIQACRGTE LDDGVQADSG PINETDANPR YKIPVEADFL FAYSTVPGYY SWRNPGKGSW 250 260 270 280 290 300 FVQALCSILD EHGKDLEIMQ ILTRVNDRVA RHFESQCDDP CFNEKKQIPC MVSMLTKELY FGR

References

[1]	"Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins." Pai J.-T., Brown M.S., Goldstein J.L. Proc. Natl. Acad. Sci. U.S.A. 93:5437-5442(1996) [PubMed: 8643593] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: Syrian. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U47332 mRNA. Translation: AAC52595.1.
3D structure databases
ProteinModelPortal	P55214.
SMR	P55214. Positions 48-303.
ModBase	Search...
Protein family/group databases
MEROPS	C14.004.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG050802.
Enzyme and pathway databases
BRENDA	3.4.22.60. 3239.
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...

Entry information

Entry name

CASP7_MESAU

Accession

Primary (citable) accession number: P55214

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 16, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program