ID CASP5_HUMAN Reviewed; 418 AA. AC P51878; Q1HBJ3; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 2. DT 07-JUL-2009, entry version 83. DE RecName: Full=Caspase-5; DE Short=CASP-5; DE EC=3.4.22.58; DE AltName: Full=ICH-3 protease; DE AltName: Full=TY protease; DE AltName: Full=ICE(rel)-III; DE Contains: DE RecName: Full=Caspase-5 subunit p20; DE Contains: DE RecName: Full=Caspase-5 subunit p10; DE Flags: Precursor; GN Name=CASP5; Synonyms=ICH3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-90 AND VAL-318. RX MEDLINE=95318183; 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 RT ICErelIII, members of the ICE/CED-3 family of cysteine proteases."; RL J. Biol. Chem. 270:15870-15876(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-3; LEU-13; ARG-59; RP ALA-90; HIS-152; LEU-201; HIS-282; VAL-318; LYS-337 AND GLN-366. RG NIEHS SNPs program; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. 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., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA 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 21-418, AND VARIANT ALA-90. RC TISSUE=Placenta, and Spleen; RX MEDLINE=96184899; PubMed=8617266; RX 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- RT 1 beta-converting enzyme."; RL Eur. J. Biochem. 236:207-213(1996). CC -!- FUNCTION: Mediator of programmed cell death (apoptosis). CC -!- CATALYTIC ACTIVITY: Strict requirement for Asp at the P1 position. CC It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but CC also cleaves at Asp-Glu-Val-Asp-|-. CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel CC arranged heterodimers, each one formed by a 20 kDa (p20) and a 10 CC kDa (p10) subunits. CC -!- INTERACTION: CC Q9C000:NLRP1; NbExp=1; IntAct=EBI-1246700, EBI-1220518; CC -!- TISSUE SPECIFICITY: Expressed in barely detectable amounts in most CC tissues except brain, highest levels being found in lung, liver CC and skeletal muscle. CC -!- PTM: The two subunits are derived from the precursor sequence by CC an autocatalytic mechanism. CC -!- SIMILARITY: Belongs to the peptidase C14A family. CC -!- SIMILARITY: Contains 1 CARD domain. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/casp5/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U28015; AAA75172.1; -; mRNA. DR EMBL; DQ508420; ABF47103.1; -; Genomic_DNA. DR EMBL; AP001153; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X94993; CAA64450.1; ALT_INIT; mRNA. DR IPI; IPI00873979; -. DR PIR; B57511; B57511. DR UniGene; Hs.213327; -. DR HSSP; P29466; 1ICE. DR IntAct; P51878; 1. DR MEROPS; C14.008; -. DR Ensembl; ENSG00000137757; Homo sapiens. DR GeneCards; GC11M104370; -. DR HGNC; HGNC:1506; CASP5. DR MIM; 602665; gene. DR PharmGKB; PA26089; -. DR HOVERGEN; P51878; -. DR BRENDA; 3.4.22.58; 247. DR BindingDB; P51878; -. DR ArrayExpress; P51878; -. DR Bgee; P51878; -. DR CleanEx; HS_CASP5; -. DR GermOnline; ENSG00000137757; Homo sapiens. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006915; P:apoptosis; TAS:ProtInc. DR GO; GO:0006508; P:proteolysis; TAS:ProtInc. DR GO; GO:0042981; P:regulation of apoptosis; IEA:InterPro. DR InterPro; IPR001315; CARD. DR InterPro; IPR017350; Caspase_IL-1_beta. DR InterPro; IPR011029; DEATH-like. DR InterPro; IPR011600; Pept_C14_cat. DR InterPro; IPR001309; Pept_C14_ICE_p20. DR InterPro; IPR016129; Pept_C14_ICE_p20_AS. DR InterPro; IPR002138; Pept_C14_p10. DR InterPro; IPR002398; Pept_C14_p45. DR InterPro; IPR015917; Pept_C14_p45_core. DR Gene3D; G3DSA:1.10.533.10; DEATH_like; 1. DR PANTHER; PTHR10454; Pept_C14_p45; 1. DR Pfam; PF00619; CARD; 1. DR Pfam; PF00656; Peptidase_C14; 1. DR PIRSF; PIRSF038001; Caspase_ICE; 1. DR PRINTS; PR00376; IL1BCENZYME. DR SMART; SM00114; CARD; 1. DR SMART; SM00115; CASc; 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 Apoptosis; Complete proteome; Hydrolase; Polymorphism; Protease; KW Thiol protease; Zymogen. FT PROPEP 1 120 Potential. FT /FTId=PRO_0000004604. FT CHAIN 121 311 Caspase-5 subunit p20. FT /FTId=PRO_0000004605. FT PROPEP 312 330 Potential. FT /FTId=PRO_0000004606. FT CHAIN 331 418 Caspase-5 subunit p10. FT /FTId=PRO_0000004607. FT DOMAIN 40 132 CARD. FT ACT_SITE 251 251 By similarity. FT ACT_SITE 299 299 FT VARIANT 3 3 K -> N (in dbSNP:rs45483102). FT /FTId=VAR_047216. FT VARIANT 10 10 L -> W (in dbSNP:rs1792778). FT /FTId=VAR_047217. FT VARIANT 13 13 F -> L (in dbSNP:rs3181320). FT /FTId=VAR_024403. FT VARIANT 59 59 L -> R. FT /FTId=VAR_054480. FT VARIANT 90 90 T -> A (in dbSNP:rs507879). FT /FTId=VAR_047218. FT VARIANT 152 152 R -> H (in dbSNP:rs3181179). FT /FTId=VAR_024404. FT VARIANT 201 201 V -> L (in dbSNP:rs3181326). FT /FTId=VAR_024405. FT VARIANT 282 282 R -> H. FT /FTId=VAR_054481. FT VARIANT 318 318 L -> V (in dbSNP:rs523104). FT /FTId=VAR_047219. FT VARIANT 337 337 E -> K (in dbSNP:rs45619739). FT /FTId=VAR_047220. FT VARIANT 366 366 E -> Q. FT /FTId=VAR_054482. SQ SEQUENCE 418 AA; 47858 MW; 018E53BCA9801368 CRC64; MFKGILQSGL DNFVINHMLK NNVAGQTSIQ TLVPNTDQKS TSVKKDNHKK KTVKMLEYLG KDVLHGVFNY LAKHDVLTLK EEEKKKYYDT KIEDKALILV DSLRKNRVAH QMFTQTLLNM DQKITSVKPL LQIEAGPPES AESTNILKLC PREEFLRLCK KNHDEIYPIK KREDRRRLAL IICNTKFDHL PARNGAHYDI VGMKRLLQGL GYTVVDEKNL TARDMESVLR AFAARPEHKS SDSTFLVLMS HGILEGICGT AHKKKKPDVL LYDTIFQIFN NRNCLSLKDK PKVIIVQACR GEKHGELWVR DSPASLALIS SQSSENLEAD SVCKIHEEKD FIAFCSSTPH NVSWRDRTRG SIFITELITC FQKYSCCCHL MEIFRKVQKS FEVPQAKAQM PTIERATLTR DFYLFPGN //