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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
 
 
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