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UniProtKB/Swiss-Prot entry P55210


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CASP7_HUMAN
Primary accession number P55210
Secondary accession numbers Q13364 Q5SVL0 Q96BA0
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    September 23, 2008 (Entry version 94)
Name and origin of the protein
Protein name Caspase-7 [Precursor]
Synonyms CASP-7
EC 3.4.22.60
ICE-like apoptotic protease 3
ICE-LAP3
Apoptotic protease Mch-3
CMH-1
Contains Caspase-7 subunit p20
Caspase-7 subunit p11
Gene name
Name: CASP7
Synonyms: MCH3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
TISSUE=T-cell;
PubMed=8521391 [NCBI, ExPASy, EBI, Israel, Japan]
Fernandes-Alnemri T., Takahashi A., Armstrong R.C., Krebs J., Fritz L.C., Tomaselli K.J., Wang L., Yu Z., Croce C.M., Salveson G., Earnshaw W.C., Litwack G., Alnemri E.S.;
"Mch3, a novel human apoptotic cysteine protease highly related to CPP32.";
Cancer Res. 55:6045-6052(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
DOI=10.1074/jbc.271.3.1621; PubMed=8576161 [NCBI, ExPASy, EBI, Israel, Japan]
Duan H., Chinnaiyan A.M., Hudson P.L., Wing J.P., He W.-W., Dixit V.M.;
"ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis.";
J. Biol. Chem. 271:1621-1625(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Spleen;
DOI=10.1074/jbc.271.4.1825; PubMed=8567622 [NCBI, ExPASy, EBI, Israel, Japan]
Lippke J.A., Gu Y., Sarnecki C., Caron P.R., Su M.S.-S.;
"Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32.";
J. Biol. Chem. 271:1825-1828(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND ALPHA').
TISSUE=Fetal lung, and Fetal spleen;
DOI=10.1006/geno.1996.4548; PubMed=9070923 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
PROTEOLYTIC PROCESSING.
DOI=10.1073/pnas.93.15.7464; PubMed=8755496 [NCBI, ExPASy, EBI, Israel, Japan]
Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M., Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J., Litwack G., Alnemri E.S.;
"In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains.";
Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996).
[9]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 51-303, AND SUBUNIT.
DOI=10.1016/S0092-8674(01)00544-X; PubMed=11701129 [NCBI, ExPASy, EBI, Israel, Japan]
Chai J., Wu Q., Shiozaki E., Srinivasula S.M., Alnemri E.S., Shi Y.;
"Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding.";
Cell 107:399-407(2001).
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.
  • CATALYTIC ACTIVITY: Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.
  • ENZYME REGULATION: Inhibited by isatin sulfonamides.
  • SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit.
  • INTERACTION:
    Q13490:BIRC2; NbExp=2; IntAct=EBI-523958, EBI-514538;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    NameAlpha
    Isoform IDP55210-1
    This is the isoform sequence displayed in this entry.
    NameBeta
    Isoform IDP55210-2
    Note: Not proteolytically active.
    Features which should be applied to build the isoform sequence: VSP_000807.
    NameAlpha'
    SynonymsBeta
    Isoform IDP55210-3
    Note: What we call isoform Alpha' is known in Ref.4 as Beta.
    Features which should be applied to build the isoform sequence: VSP_000806.
  • TISSUE SPECIFICITY: Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in 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.
  • SIMILARITY: Belongs to the peptidase C14 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U37448; AAC50303.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U37449; AAC50304.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U39613; AAC50346.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U40281; AAC50352.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U67319; AAC51152.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U67320; AAC51153.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U67206; AAF21460.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592546; CAI12638.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627395; CAI12638.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627395; CAI16004.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592546; CAI16004.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471066; EAW49495.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015799; AAH15799.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001218.1; -.
NP_203124.1; -.
NP_203125.1; -.
NP_203126.1; -.
UniGene Hs.9216
3D structure databases
PDB
1F1J; X-ray; 2.35 A; A/B=2-303.[ExPASy / RCSB / EBI]
1GQF; X-ray; 2.90 A; A/B=47-303.[ExPASy / RCSB / EBI]
1I4O; X-ray; 2.40 A; A/B=24-303.[ExPASy / RCSB / EBI]
1I51; X-ray; 2.45 A; A/C=51-198, B/D=199-303.[ExPASy / RCSB / EBI]
1K86; X-ray; 2.60 A; A/B=51-303.[ExPASy / RCSB / EBI]
1K88; X-ray; 2.70 A; A/B=51-303.[ExPASy / RCSB / EBI]
1KMC; X-ray; 2.90 A; A/B=1-303.[ExPASy / RCSB / EBI]
1MIA; Model; -; A=57-193, B=211-303.[ExPASy / RCSB / EBI]
1SHJ; X-ray; 2.80 A; A/B=50-303.[ExPASy / RCSB / EBI]
1SHL; X-ray; 3.00 A; A/B=57-303.[ExPASy / RCSB / EBI]
2QL5; X-ray; 2.34 A; A/C=24-196, B/D=207-303.[ExPASy / RCSB / EBI]
2QL7; X-ray; 2.40 A; A/C=24-196, B/D=207-303.[ExPASy / RCSB / EBI]
2QL9; X-ray; 2.14 A; A/C=24-196, B/D=207-303.[ExPASy / RCSB / EBI]
2QLB; X-ray; 2.25 A; A/C=24-196, B/D=207-303.[ExPASy / RCSB / EBI]
2QLF; X-ray; 2.80 A; A/C=24-196, B/D=207-303.[ExPASy / RCSB / EBI]
2QLJ; X-ray; 2.60 A; A/C=24-196, B/D=207-303.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1F1J; -.
1GQF; -.
1I4O; -.
1I51; -.
1K86; -.
1K88; -.
1KMC; -.
1MIA; -.
1SHJ; -.
1SHL; -.
2QL5; -.
2QL7; -.
2QL9; -.
2QLB; -.
2QLF; -.
2QLJ; -.
ModBase P55210.
Protein-protein interaction databases
IntAct P55210; -.
Protein family/group databases
MEROPS C14.004; -.
PTM databases
PhosphoSite P55210; -.
Enzyme and pathway databases
Reactome REACT_578; Apoptosis.
Organism-specific databases
H-InvDB HIX0009219; -.
HGNC HGNC:1508; CASP7.
GenAtlas CASP7.
MIM 601761; gene. [NCBI / EBI]
PharmGKB PA26091; -.
GeneCards P55210.
Gene expression databases
ArrayExpress P55210; -.
CleanEx HS_CASP7; -.
GermOnline ENSG00000165806; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005789; Cellular component: endoplasmic reticulum membrane (traceable author statement from UniProtKB).
GO:0031966; Cellular component: mitochondrial membrane (traceable author statement from UniProtKB).
GO:0030693; Molecular function: caspase activity (inferred from experiment from Reactome).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0008632; Biological process: apoptotic program (traceable author statement from ProtInc).
GO:0006508; Biological process: proteolysis (inferred from direct assay from UniProtKB).
QuickGo view.
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 of domain structure.
PANTHER PTHR10454:SF31; Casp7; 1.
PTHR10454; Pept_C14_p45; 1.
Pfam PF00656; Peptidase_C14; 1.
Pfam graphical view of domain structure.
PRINTS PR00376; IL1BCENZYME.
SMART SM00115; CASc; 1.
SMART graphical view of domain structure.
PROSITE PS01122; CASPASE_CYS; 1.
PS01121; CASPASE_HIS; 1.
PS50207; CASPASE_P10; 1.
PS50208; CASPASE_P20; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P55210.
Genome annotation databases
Ensembl ENSG00000165806; Homo sapiens. [Contig view]
GeneID 840; -.
KEGG hsa:840; -.
Phylogenomic databases
HOGENOM P55210; -.
HOVERGEN P55210; -.
Other
BindingDB P55210; -.
SOURCE CASP7; Homo sapiens.
ProtoNet P55210.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Hydrolase; Protease; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   1    23  23      PRO_0000004616
CHAIN   24   198  175     Caspase-7 subunit p20. PRO_0000004617
PROPEP   199   206  8      PRO_0000004618
CHAIN   207   303  97     Caspase-7 subunit p11. PRO_0000004619
ACT_SITE   144   144        By similarity. 
ACT_SITE   186   186         
VAR_SEQ   1     1        M -> MDCVGWPPGRKWHLEKNTSCGGSSGICASYVTQM (in isoform Alpha'). VSP_000806
VAR_SEQ   149   303        VIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRG TELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPG YYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDR VARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ -> MESCSVTQAGVQRRDLGRLQPPPPRLAEGPSLMMASRPTR GPSMTQMLILDTRSQWKLTSSSPIPRFQAITRGGAQEEAP GLCKPSAPSWRSTEKTWKSCRSSPG (in isoform Beta). VSP_000807
MUTAGEN   186   186        C->A: No apoptotic activity. 
CONFLICT   4     4        D -> E (in Ref. 7; AAH15799). 
CONFLICT   194   194        G -> A (in Ref. 2; AAC50346). 
STRAND   64    74  11      
TURN   80    82  3      
HELIX   90   104  15      
STRAND   106   113  8      
HELIX   116   128  13      
HELIX   131   133  3      
STRAND   134   143  10      
STRAND   149   151  3      
STRAND   153   158  6      
HELIX   159   164  6      
TURN   168   170  3      
HELIX   172   174  3      
STRAND   179   185  7      
STRAND   188   190  3      
TURN   215   218  4      
STRAND   219   225  7      
STRAND   232   234  3      
TURN   235   237  3      
HELIX   240   252  13      
TURN   253   255  3      
HELIX   258   272  15      
HELIX   280   282  3      
STRAND   290   293  4      
STRAND   296   298  3      
Sequence information
Length: 303 AA [This is the length of the unprocessed precursor] Molecular weight: 34277 Da [This is the MW of the unprocessed precursor] CRC64: CD373EE54A232CA4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADDQGCIEE QGVEDSANED SVDAKPDRSS FVPSLFSKKK KNVTMRSIKT TRDRVPTYQY 

        70         80         90        100        110        120 
NMNFEKLGKC IIINNKNFDK VTGMGVRNGT DKDAEALFKC FRSLGFDVIV YNDCSCAKMQ 

       130        140        150        160        170        180 
DLLKKASEED HTNAACFACI LLSHGEENVI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL 

       190        200        210        220        230        240 
FFIQACRGTE LDDGIQADSG PINDTDANPR YKIPVEADFL FAYSTVPGYY SWRSPGRGSW 

       250        260        270        280        290        300 
FVQALCSILE EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP HFHEKKQIPC VVSMLTKELY 


FSQ 

P55210 in FASTA format

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View entry in raw text format (no links)
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