CASP7_HUMAN
ID CASP7_HUMAN Reviewed; 303 AA.
AC P55210; B4DQU7; B5BU45; D3DRB8; Q13364; Q53YD5; Q5SVL0; Q5SVL3; Q96BA0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Caspase-7;
DE Short=CASP-7;
DE EC=3.4.22.60 {ECO:0000269|PubMed:11701129};
DE AltName: Full=Apoptotic protease Mch-3;
DE AltName: Full=CMH-1;
DE AltName: Full=ICE-like apoptotic protease 3;
DE Short=ICE-LAP3;
DE Contains:
DE RecName: Full=Caspase-7 subunit p20;
DE Contains:
DE RecName: Full=Caspase-7 subunit p11;
DE Flags: Precursor;
GN Name=CASP7; Synonyms=MCH3 {ECO:0000303|PubMed:8521391};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND FUNCTION.
RC TISSUE=T-cell;
RX PubMed=8521391;
RA Fernandes-Alnemri T., Takahashi A., Armstrong R.C., Krebs J., Fritz L.C.,
RA Tomaselli K.J., Wang L., Yu Z., Croce C.M., Salveson G., Earnshaw W.C.,
RA Litwack G., Alnemri E.S.;
RT "Mch3, a novel human apoptotic cysteine protease highly related to CPP32.";
RL Cancer Res. 55:6045-6052(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION, AND MUTAGENESIS OF
RP CYS-186.
RX PubMed=8576161; DOI=10.1074/jbc.271.3.1621;
RA Duan H., Chinnaiyan A.M., Hudson P.L., Wing J.P., He W.-W., Dixit V.M.;
RT "ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell
RT death protein Ced-3 is activated during Fas- and tumor necrosis factor-
RT induced apoptosis.";
RL J. Biol. Chem. 271:1621-1625(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND FUNCTION.
RC TISSUE=Spleen;
RX PubMed=8567622; DOI=10.1074/jbc.271.4.1825;
RA Lippke J.A., Gu Y., Sarnecki C., Caron P.R., Su M.S.-S.;
RT "Identification and characterization of CPP32/Mch2 homolog 1, a novel
RT cysteine protease similar to CPP32.";
RL J. Biol. Chem. 271:1825-1828(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND ALPHA'), AND FUNCTION.
RC TISSUE=Fetal lung, and Fetal spleen;
RX PubMed=9070923; DOI=10.1006/geno.1996.4548;
RA Juan T.S.-C., McNiece I.K., Argento J.M., Jenkins N.A., Gilbert D.J.,
RA Copeland N.G., Fletcher F.A.;
RT "Identification and mapping of Casp7, a cysteine protease resembling CPP32
RT beta, interleukin-1 beta converting enzyme, and CED-3.";
RL Genomics 40:86-93(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT GLU-4.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA').
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT GLU-4.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PROTEOLYTIC PROCESSING.
RX PubMed=8755496; DOI=10.1073/pnas.93.15.7464;
RA Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M.,
RA Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J., Litwack G.,
RA Alnemri E.S.;
RT "In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic
RT cysteine protease containing two FADD-like domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996).
RN [12]
RP INTERACTION WITH BIRC6/BRUCE.
RX PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018;
RA Bartke T., Pohl C., Pyrowolakis G., Jentsch S.;
RT "Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin
RT ligase.";
RL Mol. Cell 14:801-811(2004).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP INTERACTION WITH HSPA5.
RX PubMed=26045166; DOI=10.1158/0008-5472.can-14-3751;
RA Kang J.M., Park S., Kim S.J., Kim H., Lee B., Kim J., Park J., Kim S.T.,
RA Yang H.K., Kim W.H., Kim S.J.;
RT "KIAA1324 Suppresses Gastric Cancer Progression by Inhibiting the
RT Oncoprotein GRP78.";
RL Cancer Res. 75:3087-3097(2015).
RN [18]
RP INTERACTION WITH ATXN3.
RX PubMed=30455355; DOI=10.1074/jbc.ra118.005801;
RA Weishaeupl D., Schneider J., Peixoto Pinheiro B., Ruess C., Dold S.M.,
RA von Zweydorf F., Gloeckner C.J., Schmidt J., Riess O., Schmidt T.;
RT "Physiological and pathophysiological characteristics of ataxin-3
RT isoforms.";
RL J. Biol. Chem. 294:644-661(2019).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 51-303, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF CYS-186.
RX PubMed=11701129; DOI=10.1016/s0092-8674(01)00544-x;
RA Chai J., Wu Q., Shiozaki E., Srinivasula S.M., Alnemri E.S., Shi Y.;
RT "Crystal structure of a procaspase-7 zymogen: mechanisms of activation and
RT substrate binding.";
RL Cell 107:399-407(2001).
CC -!- FUNCTION: Involved in the activation cascade of caspases responsible
CC for apoptosis execution (PubMed:8521391, PubMed:8576161,
CC PubMed:8567622, PubMed:9070923, PubMed:11701129). Cleaves and activates
CC sterol regulatory element binding proteins (SREBPs) (PubMed:8521391,
CC PubMed:8576161, PubMed:8567622, PubMed:9070923). Proteolytically
CC cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217'
CC bond. Overexpression promotes programmed cell death (PubMed:8521391,
CC PubMed:8576161, PubMed:8567622, PubMed:9070923). Cleaves phospholipid
CC scramblase proteins XKR4, XKR8 and XKR9 (By similarity).
CC {ECO:0000250|UniProtKB:P97864, ECO:0000269|PubMed:11701129,
CC ECO:0000269|PubMed:8521391, ECO:0000269|PubMed:8567622,
CC ECO:0000269|PubMed:8576161, ECO:0000269|PubMed:9070923}.
CC -!- FUNCTION: [Isoform Beta]: Lacks enzymatic activity.
CC {ECO:0000269|PubMed:8521391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Strict requirement for an Asp residue at position P1 and has a
CC preferred cleavage sequence of Asp-Glu-Val-Asp-|-.; EC=3.4.22.60;
CC Evidence={ECO:0000269|PubMed:11701129};
CC -!- ACTIVITY REGULATION: Inhibited by isatin sulfonamides.
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11)
CC subunit. Interacts with BIRC6/bruce. Interacts with ATXN3 (short
CC isoform 1) (PubMed:30455355). Interacts with HSPA5 (PubMed:26045166).
CC {ECO:0000269|PubMed:11701129, ECO:0000269|PubMed:15200957,
CC ECO:0000269|PubMed:26045166, ECO:0000269|PubMed:30455355}.
CC -!- INTERACTION:
CC P55210; Q13490: BIRC2; NbExp=2; IntAct=EBI-523958, EBI-514538;
CC P55210; P83105: HTRA4; NbExp=6; IntAct=EBI-523958, EBI-21776319;
CC P55210; P42858: HTT; NbExp=12; IntAct=EBI-523958, EBI-466029;
CC P55210; Q8N4N3-2: KLHL36; NbExp=3; IntAct=EBI-523958, EBI-10973851;
CC P55210; P43364: MAGEA11; NbExp=3; IntAct=EBI-523958, EBI-739552;
CC P55210; Q16236: NFE2L2; NbExp=2; IntAct=EBI-523958, EBI-2007911;
CC P55210; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-523958, EBI-740897;
CC P55210; Q13177: PAK2; NbExp=6; IntAct=EBI-523958, EBI-1045887;
CC P55210; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-523958, EBI-9090282;
CC P55210; P21673: SAT1; NbExp=6; IntAct=EBI-523958, EBI-711613;
CC P55210; Q86WV1-2: SKAP1; NbExp=3; IntAct=EBI-523958, EBI-11995314;
CC P55210; P17405: SMPD1; NbExp=6; IntAct=EBI-523958, EBI-7095800;
CC P55210; P98170: XIAP; NbExp=3; IntAct=EBI-523958, EBI-517127;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Alpha;
CC IsoId=P55210-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P55210-2; Sequence=VSP_000807;
CC Name=Alpha'; Synonyms=Beta;
CC IsoId=P55210-3; Sequence=VSP_000806;
CC Name=4;
CC IsoId=P55210-4; Sequence=VSP_045325;
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, skeletal muscle, liver,
CC kidney, spleen and heart, and moderately in testis. No expression in
CC the brain.
CC -!- PTM: Cleavages by granzyme B or caspase-10 generate the two active
CC subunits. Propeptide domains can also be cleaved efficiently by
CC caspase-3. Active heterodimers between the small subunit of caspase-7
CC and the large subunit of caspase-3, and vice versa, also occur.
CC {ECO:0000269|PubMed:8755496}.
CC -!- MISCELLANEOUS: [Isoform Alpha']: What we call isoform Alpha' is also
CC known as Beta. {ECO:0000305|PubMed:9070923}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR EMBL; U37448; AAC50303.1; -; mRNA.
DR EMBL; U37449; AAC50304.1; -; mRNA.
DR EMBL; U39613; AAC50346.1; -; mRNA.
DR EMBL; U40281; AAC50352.1; -; mRNA.
DR EMBL; U67319; AAC51152.1; -; mRNA.
DR EMBL; U67320; AAC51153.1; -; mRNA.
DR EMBL; U67206; AAF21460.1; -; mRNA.
DR EMBL; BT006683; AAP35329.1; -; mRNA.
DR EMBL; AB451281; BAG70095.1; -; mRNA.
DR EMBL; AB451413; BAG70227.1; -; mRNA.
DR EMBL; AK298964; BAG61059.1; -; mRNA.
DR EMBL; AL592546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49494.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49495.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49498.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49496.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49497.1; -; Genomic_DNA.
DR EMBL; BC015799; AAH15799.1; -; mRNA.
DR CCDS; CCDS58096.1; -. [P55210-4]
DR CCDS; CCDS7580.1; -. [P55210-3]
DR CCDS; CCDS7581.1; -. [P55210-1]
DR CCDS; CCDS7582.1; -. [P55210-2]
DR RefSeq; NP_001218.1; NM_001227.4. [P55210-1]
DR RefSeq; NP_001253985.1; NM_001267056.1. [P55210-1]
DR RefSeq; NP_001253986.1; NM_001267057.1.
DR RefSeq; NP_001253987.1; NM_001267058.1. [P55210-4]
DR RefSeq; NP_001307840.1; NM_001320911.1.
DR RefSeq; NP_203124.1; NM_033338.5. [P55210-3]
DR RefSeq; NP_203125.1; NM_033339.4. [P55210-1]
DR RefSeq; NP_203126.1; NM_033340.3. [P55210-2]
DR PDB; 1F1J; X-ray; 2.35 A; A/B=2-303.
DR PDB; 1GQF; X-ray; 2.90 A; A/B=47-303.
DR PDB; 1I4O; X-ray; 2.40 A; A/B=24-303.
DR PDB; 1I51; X-ray; 2.45 A; A/C=51-198, B/D=199-303.
DR PDB; 1K86; X-ray; 2.60 A; A/B=51-303.
DR PDB; 1K88; X-ray; 2.70 A; A/B=51-303.
DR PDB; 1KMC; X-ray; 2.90 A; A/B=1-303.
DR PDB; 1SHJ; X-ray; 2.80 A; A/B=50-303.
DR PDB; 1SHL; X-ray; 3.00 A; A/B=57-303.
DR PDB; 2QL5; X-ray; 2.34 A; A/C=24-196, B/D=207-303.
DR PDB; 2QL7; X-ray; 2.40 A; A/C=24-196, B/D=207-303.
DR PDB; 2QL9; X-ray; 2.14 A; A/C=24-196, B/D=207-303.
DR PDB; 2QLB; X-ray; 2.25 A; A/C=24-196, B/D=207-303.
DR PDB; 2QLF; X-ray; 2.80 A; A/C=24-196, B/D=207-303.
DR PDB; 2QLJ; X-ray; 2.60 A; A/C=24-196, B/D=207-303.
DR PDB; 3EDR; X-ray; 2.45 A; A/C=24-196, B/D=207-303.
DR PDB; 3H1P; X-ray; 2.61 A; A/B=50-303.
DR PDB; 3IBC; X-ray; 2.75 A; A/C=24-196, B/D=207-303.
DR PDB; 3IBF; X-ray; 2.50 A; A/C=24-196, B/D=207-303.
DR PDB; 3R5K; X-ray; 2.86 A; A/B=1-303.
DR PDB; 4FDL; X-ray; 2.80 A; A/B=2-303.
DR PDB; 4FEA; X-ray; 3.79 A; A/B=57-303.
DR PDB; 4HQ0; X-ray; 3.00 A; A/B=47-303.
DR PDB; 4HQR; X-ray; 3.00 A; A/B=47-303.
DR PDB; 4JB8; X-ray; 1.70 A; A=24-198, B=207-303.
DR PDB; 4JJ8; X-ray; 2.94 A; A/B=57-303.
DR PDB; 4JR1; X-ray; 2.15 A; A/B=57-303.
DR PDB; 4JR2; X-ray; 1.65 A; A/B=57-303.
DR PDB; 4LSZ; X-ray; 2.26 A; A/C=24-198, B/D=207-303.
DR PDB; 4ZVO; X-ray; 2.85 A; A/C=1-198, B/D=199-303.
DR PDB; 4ZVP; X-ray; 2.50 A; A/C=1-198, B/D=199-303.
DR PDB; 4ZVQ; X-ray; 2.50 A; A/C=1-198, B/D=199-303.
DR PDB; 4ZVR; X-ray; 2.30 A; A/C=1-198, B/D=199-303.
DR PDB; 4ZVS; X-ray; 2.50 A; A/C=1-198, B/D=199-303.
DR PDB; 4ZVT; X-ray; 2.85 A; A/C=1-198, B/D=199-303.
DR PDB; 4ZVU; X-ray; 2.60 A; A/C=1-198, B/D=199-303.
DR PDB; 5IC6; X-ray; 2.70 A; A/C=1-198, B/D=199-303.
DR PDB; 5K20; X-ray; 2.20 A; A/C=1-198, B/D=199-303.
DR PDB; 5V6U; X-ray; 2.80 A; A/B=1-303.
DR PDB; 5V6Z; X-ray; 2.60 A; A/B=1-303.
DR PDBsum; 1F1J; -.
DR PDBsum; 1GQF; -.
DR PDBsum; 1I4O; -.
DR PDBsum; 1I51; -.
DR PDBsum; 1K86; -.
DR PDBsum; 1K88; -.
DR PDBsum; 1KMC; -.
DR PDBsum; 1SHJ; -.
DR PDBsum; 1SHL; -.
DR PDBsum; 2QL5; -.
DR PDBsum; 2QL7; -.
DR PDBsum; 2QL9; -.
DR PDBsum; 2QLB; -.
DR PDBsum; 2QLF; -.
DR PDBsum; 2QLJ; -.
DR PDBsum; 3EDR; -.
DR PDBsum; 3H1P; -.
DR PDBsum; 3IBC; -.
DR PDBsum; 3IBF; -.
DR PDBsum; 3R5K; -.
DR PDBsum; 4FDL; -.
DR PDBsum; 4FEA; -.
DR PDBsum; 4HQ0; -.
DR PDBsum; 4HQR; -.
DR PDBsum; 4JB8; -.
DR PDBsum; 4JJ8; -.
DR PDBsum; 4JR1; -.
DR PDBsum; 4JR2; -.
DR PDBsum; 4LSZ; -.
DR PDBsum; 4ZVO; -.
DR PDBsum; 4ZVP; -.
DR PDBsum; 4ZVQ; -.
DR PDBsum; 4ZVR; -.
DR PDBsum; 4ZVS; -.
DR PDBsum; 4ZVT; -.
DR PDBsum; 4ZVU; -.
DR PDBsum; 5IC6; -.
DR PDBsum; 5K20; -.
DR PDBsum; 5V6U; -.
DR PDBsum; 5V6Z; -.
DR AlphaFoldDB; P55210; -.
DR SMR; P55210; -.
DR BioGRID; 107290; 60.
DR ComplexPortal; CPX-2862; Caspase-7 complex.
DR DIP; DIP-29973N; -.
DR ELM; P55210; -.
DR IntAct; P55210; 25.
DR MINT; P55210; -.
DR STRING; 9606.ENSP00000358327; -.
DR BindingDB; P55210; -.
DR ChEMBL; CHEMBL3468; -.
DR DrugBank; DB05408; Emricasan.
DR DrugBank; DB03384; Fica.
DR DrugBank; DB06255; Incadronic acid.
DR DrugCentral; P55210; -.
DR GuidetoPHARMACOLOGY; 1623; -.
DR MEROPS; C14.004; -.
DR iPTMnet; P55210; -.
DR PhosphoSitePlus; P55210; -.
DR BioMuta; CASP7; -.
DR DMDM; 1730092; -.
DR EPD; P55210; -.
DR jPOST; P55210; -.
DR MassIVE; P55210; -.
DR MaxQB; P55210; -.
DR PaxDb; P55210; -.
DR PeptideAtlas; P55210; -.
DR PRIDE; P55210; -.
DR ProteomicsDB; 56811; -. [P55210-1]
DR ProteomicsDB; 56812; -. [P55210-2]
DR ProteomicsDB; 56813; -. [P55210-3]
DR Antibodypedia; 18528; 1073 antibodies from 45 providers.
DR DNASU; 840; -.
DR Ensembl; ENST00000345633.8; ENSP00000298701.7; ENSG00000165806.21. [P55210-1]
DR Ensembl; ENST00000369315.5; ENSP00000358321.1; ENSG00000165806.21. [P55210-1]
DR Ensembl; ENST00000369318.8; ENSP00000358324.4; ENSG00000165806.21. [P55210-1]
DR Ensembl; ENST00000369331.8; ENSP00000358337.3; ENSG00000165806.21. [P55210-2]
DR Ensembl; ENST00000452490.3; ENSP00000398107.2; ENSG00000165806.21. [P55210-4]
DR Ensembl; ENST00000614447.4; ENSP00000478285.1; ENSG00000165806.21. [P55210-2]
DR Ensembl; ENST00000621345.4; ENSP00000480584.1; ENSG00000165806.21. [P55210-1]
DR Ensembl; ENST00000621607.4; ENSP00000478999.1; ENSG00000165806.21. [P55210-3]
DR GeneID; 840; -.
DR KEGG; hsa:840; -.
DR MANE-Select; ENST00000369318.8; ENSP00000358324.4; NM_001227.5; NP_001218.1.
DR UCSC; uc001lam.5; human. [P55210-1]
DR CTD; 840; -.
DR DisGeNET; 840; -.
DR GeneCards; CASP7; -.
DR HGNC; HGNC:1508; CASP7.
DR HPA; ENSG00000165806; Low tissue specificity.
DR MIM; 601761; gene.
DR neXtProt; NX_P55210; -.
DR OpenTargets; ENSG00000165806; -.
DR PharmGKB; PA26091; -.
DR VEuPathDB; HostDB:ENSG00000165806; -.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00940000153232; -.
DR HOGENOM; CLU_1098210_0_0_1; -.
DR InParanoid; P55210; -.
DR OMA; MQRSQTE; -.
DR OrthoDB; 984395at2759; -.
DR PhylomeDB; P55210; -.
DR TreeFam; TF102023; -.
DR BRENDA; 3.4.22.60; 2681.
DR PathwayCommons; P55210; -.
DR Reactome; R-HSA-111459; Activation of caspases through apoptosome-mediated cleavage.
DR Reactome; R-HSA-111463; SMAC (DIABLO) binds to IAPs.
DR Reactome; R-HSA-111464; SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes.
DR Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-HSA-111469; SMAC, XIAP-regulated apoptotic response.
DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR SignaLink; P55210; -.
DR SIGNOR; P55210; -.
DR BioGRID-ORCS; 840; 16 hits in 1091 CRISPR screens.
DR ChiTaRS; CASP7; human.
DR EvolutionaryTrace; P55210; -.
DR GeneWiki; Caspase_7; -.
DR GenomeRNAi; 840; -.
DR Pharos; P55210; Tchem.
DR PRO; PR:P55210; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P55210; protein.
DR Bgee; ENSG00000165806; Expressed in rectum and 179 other tissues.
DR ExpressionAtlas; P55210; baseline and differential.
DR Genevisible; P55210; HS.
DR GO; GO:0008303; C:caspase complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:CAFA.
DR GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0008233; F:peptidase activity; IDA:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0072734; P:cellular response to staurosporine; IMP:CAFA.
DR GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IC:ComplexPortal.
DR GO; GO:0044346; P:fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IC:ComplexPortal.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IC:ComplexPortal.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:ComplexPortal.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0009411; P:response to UV; IEA:Ensembl.
DR CDD; cd00032; CASc; 1.
DR InterPro; IPR015471; Casp3/7.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR PANTHER; PTHR10454:SF31; PTHR10454:SF31; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW Hydrolase; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT PROPEP 2..23
FT /note="N-terminally processed"
FT /id="PRO_0000004616"
FT CHAIN 24..198
FT /note="Caspase-7 subunit p20"
FT /id="PRO_0000004617"
FT PROPEP 199..206
FT /id="PRO_0000004618"
FT CHAIN 207..303
FT /note="Caspase-7 subunit p11"
FT /id="PRO_0000004619"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT ACT_SITE 186
FT /evidence="ECO:0000269|PubMed:11701129"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..36
FT /note="MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLF -> MQRGLFSDGDT
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045325"
FT VAR_SEQ 1
FT /note="M -> MDCVGWPPGRKWHLEKNTSCGGSSGICASYVTQM (in isoform
FT Alpha')"
FT /evidence="ECO:0000303|PubMed:19054851,
FT ECO:0000303|PubMed:8521391, ECO:0000303|PubMed:9070923"
FT /id="VSP_000806"
FT VAR_SEQ 149..303
FT /note="VIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSG
FT PINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIM
FT QILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ -> MESCSVTQAGV
FT QRRDLGRLQPPPPRLAEGPSLMMASRPTRGPSMTQMLILDTRSQWKLTSSSPIPRFQAI
FT TRGGAQEEAPGLCKPSAPSWRSTEKTWKSCRSSPG (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:8521391"
FT /id="VSP_000807"
FT VARIANT 4
FT /note="D -> E (in dbSNP:rs11555408)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5"
FT /id="VAR_048617"
FT VARIANT 255
FT /note="D -> E (in dbSNP:rs2227310)"
FT /id="VAR_048618"
FT MUTAGEN 186
FT /note="C->A: No apoptotic activity. Loss of autocatalytic
FT cleavage."
FT /evidence="ECO:0000269|PubMed:11701129,
FT ECO:0000269|PubMed:8576161"
FT CONFLICT 194
FT /note="G -> A (in Ref. 2; AAC50346)"
FT /evidence="ECO:0000305"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4JB8"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4JR2"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4JR2"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:4JR2"
FT HELIX 90..104
FT /evidence="ECO:0007829|PDB:4JR2"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:4JR2"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:4JR2"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1F1J"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:4JR2"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:4JR2"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:4JR2"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:4JR2"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4JR2"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:4JR2"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4JR2"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:4JR2"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4JB8"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:4JR1"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:4JR2"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:4JR2"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4HQ0"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:4JR2"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:4JR2"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:4JR2"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4JR2"
FT HELIX 258..272
FT /evidence="ECO:0007829|PDB:4JR2"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:4ZVO"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:4JR2"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:4JR2"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:4JR2"
SQ 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
