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Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (CMH-1) (ICE-like apoptotic protease 3) (ICE-LAP3) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]

 CASP7_HUMAN             Reviewed;         303 AA.
P55210; B4DQU7; B5BU45; D3DRB8; Q13364; Q53YD5; Q5SVL0; Q5SVL3;
Q96BA0;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 190.
RecName: Full=Caspase-7;
Short=CASP-7;
EC=3.4.22.60;
AltName: Full=Apoptotic protease Mch-3;
AltName: Full=CMH-1;
AltName: Full=ICE-like apoptotic protease 3;
Short=ICE-LAP3;
Contains:
RecName: Full=Caspase-7 subunit p20;
Contains:
RecName: Full=Caspase-7 subunit p11;
Flags: Precursor;
Name=CASP7; Synonyms=MCH3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
TISSUE=T-cell;
PubMed=8521391;
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).
PubMed=8576161; DOI=10.1074/jbc.271.3.1621;
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;
PubMed=8567622; DOI=10.1074/jbc.271.4.1825;
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;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
GLU-4.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA').
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
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).
[9]
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
GLU-4.
TISSUE=Skin;
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).
[11]
PROTEOLYTIC PROCESSING.
PubMed=8755496; DOI=10.1073/pnas.93.15.7464;
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).
[12]
INTERACTION WITH BIRC6/BRUCE.
PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018;
Bartke T., Pohl C., Pyrowolakis G., Jentsch S.;
"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3
ubiquitin ligase.";
Mol. Cell 14:801-811(2004).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 51-303, AND SUBUNIT.
PubMed=11701129; DOI=10.1016/S0092-8674(01)00544-X;
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).
-!- 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. Interacts with BIRC6/bruce.
{ECO:0000269|PubMed:11701129, ECO:0000269|PubMed:15200957}.
-!- INTERACTION:
Q13490:BIRC2; NbExp=2; IntAct=EBI-523958, EBI-514538;
Q9GZT8:NIF3L1; NbExp=6; IntAct=EBI-523958, EBI-740897;
Q13177:PAK2; NbExp=6; IntAct=EBI-523958, EBI-1045887;
P21673:SAT1; NbExp=5; IntAct=EBI-523958, EBI-711613;
P17405:SMPD1; NbExp=6; IntAct=EBI-523958, EBI-7095800;
P98170:XIAP; NbExp=2; IntAct=EBI-523958, EBI-517127;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=Alpha;
IsoId=P55210-1; Sequence=Displayed;
Name=Beta;
IsoId=P55210-2; Sequence=VSP_000807;
Note=Lacks enzymatic activity.;
Name=Alpha'; Synonyms=Beta;
IsoId=P55210-3; Sequence=VSP_000806;
Note=What we call isoform Alpha' is also known as Beta.
{ECO:0000305|PubMed:9070923};
Name=4;
IsoId=P55210-4; Sequence=VSP_045325;
-!- 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. {ECO:0000269|PubMed:8755496}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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EMBL; U37448; AAC50303.1; -; mRNA.
EMBL; U37449; AAC50304.1; -; mRNA.
EMBL; U39613; AAC50346.1; -; mRNA.
EMBL; U40281; AAC50352.1; -; mRNA.
EMBL; U67319; AAC51152.1; -; mRNA.
EMBL; U67320; AAC51153.1; -; mRNA.
EMBL; U67206; AAF21460.1; -; mRNA.
EMBL; BT006683; AAP35329.1; -; mRNA.
EMBL; AB451281; BAG70095.1; -; mRNA.
EMBL; AB451413; BAG70227.1; -; mRNA.
EMBL; AK298964; BAG61059.1; -; mRNA.
EMBL; AL592546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL627395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49494.1; -; Genomic_DNA.
EMBL; CH471066; EAW49495.1; -; Genomic_DNA.
EMBL; CH471066; EAW49498.1; -; Genomic_DNA.
EMBL; CH471066; EAW49496.1; -; Genomic_DNA.
EMBL; CH471066; EAW49497.1; -; Genomic_DNA.
EMBL; BC015799; AAH15799.1; -; mRNA.
CCDS; CCDS58096.1; -. [P55210-4]
CCDS; CCDS7580.1; -. [P55210-3]
CCDS; CCDS7581.1; -. [P55210-1]
CCDS; CCDS7582.1; -. [P55210-2]
RefSeq; NP_001218.1; NM_001227.4. [P55210-1]
RefSeq; NP_001253985.1; NM_001267056.1. [P55210-1]
RefSeq; NP_001253986.1; NM_001267057.1.
RefSeq; NP_001253987.1; NM_001267058.1. [P55210-4]
RefSeq; NP_001307840.1; NM_001320911.1.
RefSeq; NP_203124.1; NM_033338.5. [P55210-3]
RefSeq; NP_203125.1; NM_033339.4. [P55210-1]
RefSeq; NP_203126.1; NM_033340.3. [P55210-2]
UniGene; Hs.9216; -.
PDB; 1F1J; X-ray; 2.35 A; A/B=2-303.
PDB; 1GQF; X-ray; 2.90 A; A/B=47-303.
PDB; 1I4O; X-ray; 2.40 A; A/B=24-303.
PDB; 1I51; X-ray; 2.45 A; A/C=51-198, B/D=199-303.
PDB; 1K86; X-ray; 2.60 A; A/B=51-303.
PDB; 1K88; X-ray; 2.70 A; A/B=51-303.
PDB; 1KMC; X-ray; 2.90 A; A/B=1-303.
PDB; 1MIA; Model; -; A=57-193, B=211-303.
PDB; 1SHJ; X-ray; 2.80 A; A/B=50-303.
PDB; 1SHL; X-ray; 3.00 A; A/B=57-303.
PDB; 2QL5; X-ray; 2.34 A; A/C=24-196, B/D=207-303.
PDB; 2QL7; X-ray; 2.40 A; A/C=24-196, B/D=207-303.
PDB; 2QL9; X-ray; 2.14 A; A/C=24-196, B/D=207-303.
PDB; 2QLB; X-ray; 2.25 A; A/C=24-196, B/D=207-303.
PDB; 2QLF; X-ray; 2.80 A; A/C=24-196, B/D=207-303.
PDB; 2QLJ; X-ray; 2.60 A; A/C=24-196, B/D=207-303.
PDB; 3EDR; X-ray; 2.45 A; A/C=24-196, B/D=207-303.
PDB; 3H1P; X-ray; 2.61 A; A/B=50-303.
PDB; 3IBC; X-ray; 2.75 A; A/C=24-196, B/D=207-303.
PDB; 3IBF; X-ray; 2.50 A; A/C=24-196, B/D=207-303.
PDB; 3R5K; X-ray; 2.86 A; A/B=1-303.
PDB; 4FDL; X-ray; 2.80 A; A/B=2-303.
PDB; 4FEA; X-ray; 3.79 A; A/B=57-303.
PDB; 4HQ0; X-ray; 3.00 A; A/B=47-303.
PDB; 4HQR; X-ray; 3.00 A; A/B=47-303.
PDB; 4JB8; X-ray; 1.70 A; A=24-198, B=207-303.
PDB; 4JJ8; X-ray; 2.94 A; A/B=57-303.
PDB; 4JR1; X-ray; 2.15 A; A/B=57-303.
PDB; 4JR2; X-ray; 1.65 A; A/B=57-303.
PDB; 4LSZ; X-ray; 2.26 A; A/C=24-198, B/D=207-303.
PDB; 4ZVO; X-ray; 2.85 A; A/C=1-198, B/D=199-303.
PDB; 4ZVP; X-ray; 2.50 A; A/C=1-198, B/D=199-303.
PDB; 4ZVQ; X-ray; 2.50 A; A/C=1-198, B/D=199-303.
PDB; 4ZVR; X-ray; 2.30 A; A/C=1-198, B/D=199-303.
PDB; 4ZVS; X-ray; 2.50 A; A/C=1-198, B/D=199-303.
PDB; 4ZVT; X-ray; 2.85 A; A/C=1-198, B/D=199-303.
PDB; 4ZVU; X-ray; 2.60 A; A/C=1-198, B/D=199-303.
PDB; 5IC6; X-ray; 2.70 A; A/C=1-198, B/D=199-303.
PDB; 5K20; X-ray; 2.20 A; A/C=1-198, B/D=199-303.
PDBsum; 1F1J; -.
PDBsum; 1GQF; -.
PDBsum; 1I4O; -.
PDBsum; 1I51; -.
PDBsum; 1K86; -.
PDBsum; 1K88; -.
PDBsum; 1KMC; -.
PDBsum; 1MIA; -.
PDBsum; 1SHJ; -.
PDBsum; 1SHL; -.
PDBsum; 2QL5; -.
PDBsum; 2QL7; -.
PDBsum; 2QL9; -.
PDBsum; 2QLB; -.
PDBsum; 2QLF; -.
PDBsum; 2QLJ; -.
PDBsum; 3EDR; -.
PDBsum; 3H1P; -.
PDBsum; 3IBC; -.
PDBsum; 3IBF; -.
PDBsum; 3R5K; -.
PDBsum; 4FDL; -.
PDBsum; 4FEA; -.
PDBsum; 4HQ0; -.
PDBsum; 4HQR; -.
PDBsum; 4JB8; -.
PDBsum; 4JJ8; -.
PDBsum; 4JR1; -.
PDBsum; 4JR2; -.
PDBsum; 4LSZ; -.
PDBsum; 4ZVO; -.
PDBsum; 4ZVP; -.
PDBsum; 4ZVQ; -.
PDBsum; 4ZVR; -.
PDBsum; 4ZVS; -.
PDBsum; 4ZVT; -.
PDBsum; 4ZVU; -.
PDBsum; 5IC6; -.
PDBsum; 5K20; -.
ProteinModelPortal; P55210; -.
SMR; P55210; -.
BioGrid; 107290; 47.
DIP; DIP-29973N; -.
ELM; P55210; -.
IntAct; P55210; 18.
MINT; MINT-147084; -.
STRING; 9606.ENSP00000358327; -.
BindingDB; P55210; -.
ChEMBL; CHEMBL3468; -.
DrugBank; DB03384; Fica.
DrugBank; DB05408; IDN-6556.
GuidetoPHARMACOLOGY; 1623; -.
MEROPS; C14.004; -.
iPTMnet; P55210; -.
PhosphoSitePlus; P55210; -.
BioMuta; CASP7; -.
DMDM; 1730092; -.
EPD; P55210; -.
MaxQB; P55210; -.
PaxDb; P55210; -.
PeptideAtlas; P55210; -.
PRIDE; P55210; -.
DNASU; 840; -.
Ensembl; ENST00000345633; ENSP00000298701; ENSG00000165806. [P55210-1]
Ensembl; ENST00000369315; ENSP00000358321; ENSG00000165806. [P55210-1]
Ensembl; ENST00000369318; ENSP00000358324; ENSG00000165806. [P55210-1]
Ensembl; ENST00000369331; ENSP00000358337; ENSG00000165806. [P55210-2]
Ensembl; ENST00000452490; ENSP00000398107; ENSG00000165806. [P55210-4]
Ensembl; ENST00000614447; ENSP00000478285; ENSG00000165806. [P55210-2]
Ensembl; ENST00000621345; ENSP00000480584; ENSG00000165806. [P55210-1]
Ensembl; ENST00000621607; ENSP00000478999; ENSG00000165806. [P55210-3]
GeneID; 840; -.
KEGG; hsa:840; -.
UCSC; uc001lam.5; human. [P55210-1]
CTD; 840; -.
DisGeNET; 840; -.
EuPathDB; HostDB:ENSG00000165806.19; -.
GeneCards; CASP7; -.
HGNC; HGNC:1508; CASP7.
HPA; CAB025563; -.
MIM; 601761; gene.
neXtProt; NX_P55210; -.
OpenTargets; ENSG00000165806; -.
PharmGKB; PA26091; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOVERGEN; HBG050802; -.
InParanoid; P55210; -.
KO; K04397; -.
PhylomeDB; P55210; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.60; 2681.
Reactome; R-HSA-111459; Activation of caspases through apoptosome-mediated cleavage.
Reactome; R-HSA-111463; SMAC binds to IAPs.
Reactome; R-HSA-111464; SMAC-mediated dissociation of IAP:caspase complexes.
Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
SIGNOR; P55210; -.
ChiTaRS; CASP7; human.
EvolutionaryTrace; P55210; -.
GeneWiki; Caspase_7; -.
GenomeRNAi; 840; -.
PMAP-CutDB; P55210; -.
PRO; PR:P55210; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000165806; -.
CleanEx; HS_CASP7; -.
ExpressionAtlas; P55210; baseline and differential.
Genevisible; P55210; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:Reactome.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:CAFA.
GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
GO; GO:0008233; F:peptidase activity; IDA:BHF-UCL.
GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0072734; P:cellular response to staurosporine; IMP:CAFA.
GO; GO:0097194; P:execution phase of apoptosis; TAS:Reactome.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
CDD; cd00032; CASc; 1.
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.
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;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein; Polymorphism;
Protease; Reference proteome; Thiol protease; Zymogen.
PROPEP 1 23
/FTId=PRO_0000441163.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
PROPEP 2 23 N-terminally processed.
/FTId=PRO_0000004616.
CHAIN 24 198 Caspase-7 subunit p20.
/FTId=PRO_0000004617.
PROPEP 199 206
/FTId=PRO_0000004618.
CHAIN 207 303 Caspase-7 subunit p11.
/FTId=PRO_0000004619.
ACT_SITE 144 144 {ECO:0000250}.
ACT_SITE 186 186
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P97864}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 36 MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLF -> M
QRGLFSDGDT (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045325.
VAR_SEQ 1 1 M -> MDCVGWPPGRKWHLEKNTSCGGSSGICASYVTQM
(in isoform Alpha').
{ECO:0000303|PubMed:19054851,
ECO:0000303|PubMed:8521391,
ECO:0000303|PubMed:9070923}.
/FTId=VSP_000806.
VAR_SEQ 149 303 VIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGT
ELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYY
SWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVAR
HFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ -> MESCS
VTQAGVQRRDLGRLQPPPPRLAEGPSLMMASRPTRGPSMTQ
MLILDTRSQWKLTSSSPIPRFQAITRGGAQEEAPGLCKPSA
PSWRSTEKTWKSCRSSPG (in isoform Beta).
{ECO:0000303|PubMed:8521391}.
/FTId=VSP_000807.
VARIANT 4 4 D -> E (in dbSNP:rs11593766).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5}.
/FTId=VAR_048617.
VARIANT 255 255 D -> E (in dbSNP:rs2227310).
/FTId=VAR_048618.
MUTAGEN 186 186 C->A: No apoptotic activity.
CONFLICT 194 194 G -> A (in Ref. 2; AAC50346).
{ECO:0000305}.
HELIX 56 58 {ECO:0000244|PDB:4JB8}.
STRAND 64 66 {ECO:0000244|PDB:4JR2}.
STRAND 68 74 {ECO:0000244|PDB:4JR2}.
HELIX 80 82 {ECO:0000244|PDB:4JR2}.
HELIX 90 104 {ECO:0000244|PDB:4JR2}.
STRAND 106 113 {ECO:0000244|PDB:4JR2}.
HELIX 116 127 {ECO:0000244|PDB:4JR2}.
HELIX 131 133 {ECO:0000244|PDB:1F1J}.
STRAND 137 143 {ECO:0000244|PDB:4JR2}.
STRAND 149 152 {ECO:0000244|PDB:4JR2}.
STRAND 155 158 {ECO:0000244|PDB:4JR2}.
HELIX 159 163 {ECO:0000244|PDB:4JR2}.
HELIX 164 166 {ECO:0000244|PDB:4JR2}.
TURN 168 170 {ECO:0000244|PDB:4JR2}.
HELIX 172 174 {ECO:0000244|PDB:4JR2}.
STRAND 179 185 {ECO:0000244|PDB:4JR2}.
STRAND 188 190 {ECO:0000244|PDB:4JB8}.
TURN 209 211 {ECO:0000244|PDB:4JR1}.
TURN 215 218 {ECO:0000244|PDB:4JR2}.
STRAND 219 225 {ECO:0000244|PDB:4JR2}.
STRAND 227 229 {ECO:0000244|PDB:4HQ0}.
STRAND 232 234 {ECO:0000244|PDB:4JR2}.
TURN 235 237 {ECO:0000244|PDB:4JR2}.
HELIX 240 252 {ECO:0000244|PDB:4JR2}.
TURN 253 255 {ECO:0000244|PDB:4JR2}.
HELIX 258 272 {ECO:0000244|PDB:4JR2}.
TURN 276 278 {ECO:0000244|PDB:4ZVO}.
HELIX 280 282 {ECO:0000244|PDB:4JR2}.
STRAND 290 293 {ECO:0000244|PDB:4JR2}.
STRAND 296 298 {ECO:0000244|PDB:4JR2}.
SEQUENCE 303 AA; 34277 MW; CD373EE54A232CA4 CRC64;
MADDQGCIEE QGVEDSANED SVDAKPDRSS FVPSLFSKKK KNVTMRSIKT TRDRVPTYQY
NMNFEKLGKC IIINNKNFDK VTGMGVRNGT DKDAEALFKC FRSLGFDVIV YNDCSCAKMQ
DLLKKASEED HTNAACFACI LLSHGEENVI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL
FFIQACRGTE LDDGIQADSG PINDTDANPR YKIPVEADFL FAYSTVPGYY SWRSPGRGSW
FVQALCSILE EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP HFHEKKQIPC VVSMLTKELY
FSQ


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