CASP5_HUMAN
ID CASP5_HUMAN Reviewed; 434 AA.
AC P51878; B4DKP5; Q0QVY7; Q0QVY8; Q0QVZ0; Q0QVZ1; Q0QVZ2; Q14DD6; Q1HBJ3;
AC Q6DJV7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Caspase-5 {ECO:0000303|PubMed:16893518};
DE Short=CASP-5 {ECO:0000303|PubMed:16893518};
DE EC=3.4.22.58 {ECO:0000269|PubMed:28314590};
DE AltName: Full=ICE(rel)-III {ECO:0000303|PubMed:7797592};
DE AltName: Full=Protease ICH-3 {ECO:0000303|PubMed:7797592};
DE AltName: Full=Protease TY {ECO:0000303|PubMed:8617266};
DE Contains:
DE RecName: Full=Caspase-5 subunit p20;
DE Contains:
DE RecName: Full=Caspase-5 subunit p10;
DE Flags: Precursor;
GN Name=CASP5 {ECO:0000303|PubMed:16893518, ECO:0000312|HGNC:HGNC:1506};
GN Synonyms=ICH3 {ECO:0000303|PubMed:7797592};
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 1; 2; 3; 4 AND 5), ALTERNATIVE
RP SPLICING (ISOFORM 6), VARIANTS ALA-106 AND VAL-334, AND INDUCTION BY LPS.
RX PubMed=16893518; DOI=10.1016/j.bbrc.2006.07.104;
RA Eckhart L., Kittel C., Gawlas S., Gruber F., Mildner M., Jilma B.,
RA Tschachler E.;
RT "Identification of a novel exon encoding the amino-terminus of the
RT predominant caspase-5 variants.";
RL Biochem. Biophys. Res. Commun. 348:682-688(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-106.
RC TISSUE=Colon;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-434 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP VARIANTS ALA-106 AND VAL-334.
RX PubMed=7797592; DOI=10.1074/jbc.270.26.15870;
RA Munday N.A., Vaillancourt J.P., Ali A., Casano F.J., Miller D.K.,
RA Molineaux S.M., Yamin T.-T., Yu V.L., Nicholson D.W.;
RT "Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII,
RT members of the ICE/CED-3 family of cysteine proteases.";
RL J. Biol. Chem. 270:15870-15876(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-434 (ISOFORM 1), AND VARIANTS
RP LEU-29; ALA-106; HIS-168; LEU-217 AND VAL-334.
RC TISSUE=Colon;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-434, AND VARIANT ALA-106.
RC TISSUE=Placenta, and Spleen;
RX PubMed=8617266; DOI=10.1111/j.1432-1033.1996.t01-1-00207.x;
RA Faucheu C., Blanchet A.-M., Collard-Dutilleul V., Lalanne J.-L.,
RA Diu-Hercend A.;
RT "Identification of a cysteine protease closely related to interleukin-1
RT beta-converting enzyme.";
RL Eur. J. Biochem. 236:207-213(1996).
RN [7]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-19; LEU-29;
RP ARG-75; ALA-106; HIS-168; LEU-217; HIS-298; VAL-334; LYS-353 AND GLN-382.
RG NIEHS SNPs program;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-106.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INTERACTION WITH MEFV.
RX PubMed=17431422; DOI=10.1038/sj.cdd.4402142;
RA Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D.,
RA Grutter C., Grutter M., Tschopp J.;
RT "The SPRY domain of Pyrin, mutated in familial Mediterranean fever
RT patients, interacts with inflammasome components and inhibits proIL-1beta
RT processing.";
RL Cell Death Differ. 14:1457-1466(2007).
RN [10]
RP FUNCTION.
RX PubMed=29898893; DOI=10.15252/embj.201798321;
RA Mulvihill E., Sborgi L., Mari S.A., Pfreundschuh M., Hiller S.,
RA Mueller D.J.;
RT "Mechanism of membrane pore formation by human gasdermin-D.";
RL EMBO J. 37:0-0(2018).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-315.
RX PubMed=28314590; DOI=10.1016/j.immuni.2017.02.011;
RA Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J., Fang R.,
RA Meng G., Su X., Jiang Z.;
RT "Inflammasome activation triggers caspase-1-mediated cleavage of cGAS to
RT regulate responses to DNA virus infection.";
RL Immunity 46:393-404(2017).
RN [12]
RP INTERACTION WITH SERPINB1.
RX PubMed=30692621; DOI=10.1038/s41590-018-0303-z;
RA Choi Y.J., Kim S., Choi Y., Nielsen T.B., Yan J., Lu A., Ruan J., Lee H.R.,
RA Wu H., Spellberg B., Jung J.U.;
RT "SERPINB1-mediated checkpoint of inflammatory caspase activation.";
RL Nat. Immunol. 20:276-287(2019).
CC -!- FUNCTION: Thiol protease that acts as a mediator of programmed cell
CC death (PubMed:29898893, PubMed:28314590). Initiates pyroptosis, a
CC programmed lytic cell death pathway through cleavage of Gasdermin-D
CC (GSDMD): cleavage releases the N-terminal gasdermin moiety (Gasdermin-
CC D, N-terminal) that binds to membranes and forms pores, triggering
CC pyroptosis (PubMed:29898893). During non-canonical inflammasome
CC activation, cuts CGAS and may play a role in the regulation of
CC antiviral innate immune activation (PubMed:28314590).
CC {ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:29898893}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Strict requirement for Asp at the P1 position. It has a
CC preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at
CC Asp-Glu-Val-Asp-|-.; EC=3.4.22.58;
CC Evidence={ECO:0000269|PubMed:28314590};
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 20 kDa (p20) and a 10 kDa (p10)
CC subunits (By similarity). Interacts with MEFV (PubMed:17431422).
CC Interacts with SERPINB1; this interaction regulates CASP5 activity
CC (PubMed:30692621). {ECO:0000250|UniProtKB:P29466,
CC ECO:0000269|PubMed:17431422, ECO:0000269|PubMed:30692621}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=6;
CC Name=1; Synonyms=caspase-5/a {ECO:0000303|PubMed:16893518};
CC IsoId=P51878-1; Sequence=Displayed;
CC Name=2; Synonyms=Caspase-5/b {ECO:0000303|PubMed:16893518};
CC IsoId=P51878-2; Sequence=VSP_038993;
CC Name=3; Synonyms=Caspase-5/c {ECO:0000303|PubMed:16893518};
CC IsoId=P51878-3; Sequence=VSP_038990;
CC Name=4; Synonyms=Caspase-5/e {ECO:0000303|PubMed:16893518};
CC IsoId=P51878-4; Sequence=VSP_038993, VSP_038994, VSP_038995;
CC Name=5; Synonyms=Caspase-5/f {ECO:0000303|PubMed:16893518};
CC IsoId=P51878-5; Sequence=VSP_038992;
CC Name=6; Synonyms=Caspase-5-S {ECO:0000303|PubMed:16893518};
CC IsoId=P51878-6; Sequence=VSP_038991;
CC -!- TISSUE SPECIFICITY: Expressed in barely detectable amounts in most
CC tissues except brain, highest levels being found in lung, liver and
CC skeletal muscle. {ECO:0000269|PubMed:7797592}.
CC -!- INDUCTION: Up-regulated by bacterial lipopolysaccharides (LPS).
CC {ECO:0000269|PubMed:16893518}.
CC -!- PTM: The two subunits are derived from the precursor sequence by an
CC autocatalytic mechanism. {ECO:0000250|UniProtKB:P29466}.
CC -!- MISCELLANEOUS: [Isoform 1]: Most abundant isoform.
CC -!- MISCELLANEOUS: [Isoform 2]: Most abundant isoform. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative initiation at Met-
CC 71 of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA75172.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH74994.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI13407.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABF47103.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG59257.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA64450.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/casp5/";
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DR EMBL; DQ228672; ABB58698.1; -; mRNA.
DR EMBL; DQ228673; ABB58699.1; -; mRNA.
DR EMBL; DQ228674; ABB58700.1; -; mRNA.
DR EMBL; DQ228676; ABB58702.1; -; mRNA.
DR EMBL; DQ228677; ABB58703.1; -; mRNA.
DR EMBL; AK296660; BAG59257.1; ALT_FRAME; mRNA.
DR EMBL; AP001153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U28015; AAA75172.1; ALT_INIT; mRNA.
DR EMBL; BC074994; AAH74994.1; ALT_INIT; mRNA.
DR EMBL; BC113406; AAI13407.1; ALT_INIT; mRNA.
DR EMBL; X94993; CAA64450.1; ALT_INIT; mRNA.
DR EMBL; DQ508420; ABF47103.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471065; EAW67054.1; -; Genomic_DNA.
DR CCDS; CCDS44718.1; -. [P51878-3]
DR CCDS; CCDS44719.1; -. [P51878-2]
DR CCDS; CCDS44720.1; -. [P51878-5]
DR CCDS; CCDS8328.2; -. [P51878-1]
DR PIR; B57511; B57511.
DR RefSeq; NP_001129581.1; NM_001136109.1. [P51878-2]
DR RefSeq; NP_001129582.1; NM_001136110.1. [P51878-3]
DR RefSeq; NP_001129584.1; NM_001136112.1. [P51878-5]
DR RefSeq; NP_004338.3; NM_004347.3. [P51878-1]
DR AlphaFoldDB; P51878; -.
DR SMR; P51878; -.
DR BioGRID; 107288; 5.
DR CORUM; P51878; -.
DR DIP; DIP-40038N; -.
DR IntAct; P51878; 5.
DR STRING; 9606.ENSP00000376849; -.
DR BindingDB; P51878; -.
DR ChEMBL; CHEMBL3131; -.
DR GuidetoPHARMACOLOGY; 1621; -.
DR MEROPS; C14.008; -.
DR GlyGen; P51878; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51878; -.
DR PhosphoSitePlus; P51878; -.
DR BioMuta; CASP5; -.
DR DMDM; 294862523; -.
DR EPD; P51878; -.
DR jPOST; P51878; -.
DR MassIVE; P51878; -.
DR MaxQB; P51878; -.
DR PaxDb; P51878; -.
DR PeptideAtlas; P51878; -.
DR PRIDE; P51878; -.
DR ProteomicsDB; 56442; -. [P51878-1]
DR ProteomicsDB; 56443; -. [P51878-2]
DR ProteomicsDB; 56444; -. [P51878-3]
DR ProteomicsDB; 56445; -. [P51878-4]
DR ProteomicsDB; 56446; -. [P51878-5]
DR ProteomicsDB; 56447; -. [P51878-6]
DR Antibodypedia; 18098; 549 antibodies from 40 providers.
DR DNASU; 838; -.
DR Ensembl; ENST00000260315.8; ENSP00000260315.3; ENSG00000137757.11. [P51878-1]
DR Ensembl; ENST00000393141.6; ENSP00000376849.2; ENSG00000137757.11. [P51878-5]
DR Ensembl; ENST00000418434.5; ENSP00000398130.1; ENSG00000137757.11. [P51878-3]
DR Ensembl; ENST00000444749.6; ENSP00000388365.2; ENSG00000137757.11. [P51878-2]
DR Ensembl; ENST00000456200.5; ENSP00000408455.1; ENSG00000137757.11. [P51878-4]
DR Ensembl; ENST00000526056.5; ENSP00000436877.1; ENSG00000137757.11. [P51878-5]
DR Ensembl; ENST00000531367.5; ENSP00000434471.1; ENSG00000137757.11. [P51878-3]
DR GeneID; 838; -.
DR KEGG; hsa:838; -.
DR MANE-Select; ENST00000260315.8; ENSP00000260315.3; NM_004347.5; NP_004338.3.
DR UCSC; uc010ruz.1; human. [P51878-1]
DR CTD; 838; -.
DR DisGeNET; 838; -.
DR GeneCards; CASP5; -.
DR HGNC; HGNC:1506; CASP5.
DR HPA; ENSG00000137757; Group enriched (brain, intestine, lymphoid tissue).
DR MIM; 602665; gene.
DR neXtProt; NX_P51878; -.
DR OpenTargets; ENSG00000137757; -.
DR PharmGKB; PA26089; -.
DR VEuPathDB; HostDB:ENSG00000137757; -.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00940000161497; -.
DR HOGENOM; CLU_036904_0_0_1; -.
DR InParanoid; P51878; -.
DR OMA; FNSRNCV; -.
DR OrthoDB; 1327703at2759; -.
DR PhylomeDB; P51878; -.
DR TreeFam; TF102023; -.
DR BRENDA; 3.4.22.58; 2681.
DR PathwayCommons; P51878; -.
DR Reactome; R-HSA-5620971; Pyroptosis.
DR SABIO-RK; P51878; -.
DR SignaLink; P51878; -.
DR SIGNOR; P51878; -.
DR BioGRID-ORCS; 838; 7 hits in 1064 CRISPR screens.
DR ChiTaRS; CASP5; human.
DR GenomeRNAi; 838; -.
DR Pharos; P51878; Tchem.
DR PRO; PR:P51878; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P51878; protein.
DR Bgee; ENSG00000137757; Expressed in rectum and 112 other tissues.
DR ExpressionAtlas; P51878; baseline and differential.
DR Genevisible; P51878; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0072558; C:NLRP1 inflammasome complex; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR CDD; cd00032; CASc; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR011029; DEATH-like_dom_sf.
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 Pfam; PF00619; CARD; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS50209; CARD; 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 Alternative initiation; Alternative splicing; Apoptosis; Hydrolase;
KW Protease; Reference proteome; Thiol protease; Zymogen.
FT PROPEP 1..136
FT /evidence="ECO:0000255"
FT /id="PRO_0000004604"
FT CHAIN 137..327
FT /note="Caspase-5 subunit p20"
FT /evidence="ECO:0000250|UniProtKB:P29466"
FT /id="PRO_0000004605"
FT PROPEP 328..346
FT /evidence="ECO:0000255"
FT /id="PRO_0000004606"
FT CHAIN 347..434
FT /note="Caspase-5 subunit p10"
FT /evidence="ECO:0000250|UniProtKB:P29466"
FT /id="PRO_0000004607"
FT DOMAIN 56..148
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT ACT_SITE 267
FT /evidence="ECO:0000250|UniProtKB:P29466"
FT ACT_SITE 315
FT /evidence="ECO:0000269|PubMed:28314590"
FT VAR_SEQ 1..145
FT /note="MAEDSGKKKRRKNFEAMFKGILQSGLDNFVINHMLKNNVAGQTSIQTLVPNT
FT DQKSTSVKKDNHKKKTVKMLEYLGKDVLHGVFNYLAKHDVLTLKEEEKKKYYDTKIEDK
FT ALILVDSLRKNRVAHQMFTQTLLNMDQKITSVKP -> MAA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16893518"
FT /id="VSP_038990"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_038991"
FT VAR_SEQ 1..2
FT /note="MA -> MAAVPRVEGVFIFLI (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16893518"
FT /id="VSP_038992"
FT VAR_SEQ 5..62
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16893518"
FT /id="VSP_038993"
FT VAR_SEQ 145..166
FT /note="PLLQIEAGPPESAESTNILKLC -> HLSNKKERGPQTPGSHHMQYKV (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16893518"
FT /id="VSP_038994"
FT VAR_SEQ 167..434
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16893518"
FT /id="VSP_038995"
FT VARIANT 19
FT /note="K -> N (in dbSNP:rs45483102)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_047216"
FT VARIANT 26
FT /note="L -> W (in dbSNP:rs1792778)"
FT /id="VAR_047217"
FT VARIANT 29
FT /note="F -> L (in dbSNP:rs3181320)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.7"
FT /id="VAR_024403"
FT VARIANT 75
FT /note="L -> R (in dbSNP:rs45585331)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_054480"
FT VARIANT 106
FT /note="T -> A (in dbSNP:rs507879)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16893518,
FT ECO:0000269|PubMed:7797592, ECO:0000269|PubMed:8617266,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8"
FT /id="VAR_047218"
FT VARIANT 168
FT /note="R -> H (in dbSNP:rs3181179)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.7"
FT /id="VAR_024404"
FT VARIANT 217
FT /note="V -> L (in dbSNP:rs3181326)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.7"
FT /id="VAR_024405"
FT VARIANT 298
FT /note="R -> H (in dbSNP:rs45464699)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_054481"
FT VARIANT 334
FT /note="L -> V (in dbSNP:rs523104)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16893518, ECO:0000269|PubMed:7797592,
FT ECO:0000269|Ref.7"
FT /id="VAR_047219"
FT VARIANT 353
FT /note="E -> K (in dbSNP:rs45619739)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_047220"
FT VARIANT 382
FT /note="E -> Q (in dbSNP:rs45458695)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_054482"
FT MUTAGEN 315
FT /note="C->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:28314590"
SQ SEQUENCE 434 AA; 49736 MW; C5257C2BF15EB6D5 CRC64;
MAEDSGKKKR RKNFEAMFKG ILQSGLDNFV INHMLKNNVA GQTSIQTLVP NTDQKSTSVK
KDNHKKKTVK MLEYLGKDVL HGVFNYLAKH DVLTLKEEEK KKYYDTKIED KALILVDSLR
KNRVAHQMFT QTLLNMDQKI TSVKPLLQIE AGPPESAEST NILKLCPREE FLRLCKKNHD
EIYPIKKRED RRRLALIICN TKFDHLPARN GAHYDIVGMK RLLQGLGYTV VDEKNLTARD
MESVLRAFAA RPEHKSSDST FLVLMSHGIL EGICGTAHKK KKPDVLLYDT IFQIFNNRNC
LSLKDKPKVI IVQACRGEKH GELWVRDSPA SLALISSQSS ENLEADSVCK IHEEKDFIAF
CSSTPHNVSW RDRTRGSIFI TELITCFQKY SCCCHLMEIF RKVQKSFEVP QAKAQMPTIE
RATLTRDFYL FPGN
