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Caspase-8 (CASP-8) (EC 3.4.22.61) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]

 CASP8_RAT               Reviewed;         482 AA.
Q9JHX4;
01-APR-2015, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 132.
RecName: Full=Caspase-8 {ECO:0000303|Ref.2, ECO:0000305};
Short=CASP-8;
EC=3.4.22.61;
Contains:
RecName: Full=Caspase-8 subunit p18;
Contains:
RecName: Full=Caspase-8 subunit p10;
Flags: Precursor;
Name=Casp8 {ECO:0000312|RGD:620945};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Itoh T., Itoh A., Pleasure D.;
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
Cao G., Graham S.H., Chen D., Chen J.;
"Molecular cloning and characterization of rat caspase-8: Its
implication in delayed neuronal cell death after ischemia.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH NOL3.
PubMed=15383280; DOI=10.1016/j.molcel.2004.08.020;
Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B.,
Hayakawa Y., Lee P., Korsmeyer S.J., Kitsis R.N.;
"Inhibition of both the extrinsic and intrinsic death pathways through
nonhomotypic death-fold interactions.";
Mol. Cell 15:901-912(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Most upstream protease of the activation cascade of
caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A
induced cell death. Binding to the adapter molecule FADD recruits
it to either receptor. The resulting aggregate called death-
inducing signaling complex (DISC) performs CASP8 proteolytic
activation. The active dimeric enzyme is then liberated from the
DISC and free to activate downstream apoptotic proteases.
Proteolytic fragments of the N-terminal propeptide (termed CAP3,
CAP5 and CAP6) are likely retained in the DISC. Cleaves and
activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May
participate in the GZMB apoptotic pathways. Cleaves ADPRT.
Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC.
Likely target for the cowpox virus CRMA death inhibitory protein.
{ECO:0000250|UniProtKB:O89110}.
-!- CATALYTIC ACTIVITY: Strict requirement for Asp at position P1 and
has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-
(Gly/Ser/Ala). {ECO:0000250|UniProtKB:O89110}.
-!- ENZYME REGULATION: Inhibited by CRMA and P35.
{ECO:0000250|UniProtKB:O89110}.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 18 kDa (p18) and a 10
kDa (p10) subunit. Interacts with FADD, CFLAR and PEA15. Interacts
with RFFL and RNF34; negatively regulate CASP8 through proteasomal
degradation (By similarity). Interacts with TNFAIP8L2. Interacts
with CASP8AP2. Interacts with NOL3; decreases CASP8 activity in a
mitochondria localization- and phosphorylation-dependent manner
and this interaction is dissociated by calcium.
{ECO:0000250|UniProtKB:O89110, ECO:0000250|UniProtKB:Q14790,
ECO:0000269|PubMed:15383280}.
-!- INTERACTION:
Q8R2E7:Fadd; NbExp=2; IntAct=EBI-4326675, EBI-4326723;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- PTM: Generation of the subunits requires association with the
death-inducing signaling complex (DISC), whereas additional
processing is likely due to the autocatalytic activity of the
activated protease. GZMB and CASP10 can be involved in these
processing events (By similarity). {ECO:0000250|UniProtKB:Q14790}.
-!- PTM: Phosphorylation on Ser-389 during mitosis by CDK1 inhibits
activation by proteolysis and prevents apoptosis. This
phosphorylation occurs in cancer cell lines, as well as in primary
breast tissues and lymphocytes (By similarity).
{ECO:0000250|UniProtKB:Q14790}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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EMBL; AF279308; AAF87778.1; -; mRNA.
EMBL; AF288372; AAK83055.1; -; mRNA.
EMBL; AABR06060567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06060568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473965; EDL98978.1; -; Genomic_DNA.
EMBL; CH473965; EDL98979.1; -; Genomic_DNA.
RefSeq; NP_071613.1; NM_022277.1.
RefSeq; XP_006245077.1; XM_006245015.3.
UniGene; Rn.54474; -.
ProteinModelPortal; Q9JHX4; -.
SMR; Q9JHX4; -.
IntAct; Q9JHX4; 2.
STRING; 10116.ENSRNOP00000016613; -.
MEROPS; C14.009; -.
iPTMnet; Q9JHX4; -.
PhosphoSitePlus; Q9JHX4; -.
PaxDb; Q9JHX4; -.
PRIDE; Q9JHX4; -.
Ensembl; ENSRNOT00000016613; ENSRNOP00000016613; ENSRNOG00000012331.
Ensembl; ENSRNOT00000084498; ENSRNOP00000069982; ENSRNOG00000012331.
GeneID; 64044; -.
KEGG; rno:64044; -.
UCSC; RGD:620945; rat.
CTD; 841; -.
RGD; 620945; Casp8.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOGENOM; HOG000276884; -.
HOVERGEN; HBG050803; -.
KO; K04398; -.
OMA; IFIEMEK; -.
PhylomeDB; Q9JHX4; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.61; 5301.
Reactome; R-RNO-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-RNO-168638; NOD1/2 Signaling Pathway.
Reactome; R-RNO-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-RNO-3371378; Regulation by c-FLIP.
Reactome; R-RNO-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-RNO-5218900; CASP8 activity is inhibited.
Reactome; R-RNO-5357905; Regulation of TNFR1 signaling.
Reactome; R-RNO-5660668; CLEC7A/inflammasome pathway.
Reactome; R-RNO-69416; Dimerization of procaspase-8.
Reactome; R-RNO-75108; Activation, myristolyation of BID and translocation to mitochondria.
Reactome; R-RNO-75153; Apoptotic execution phase.
Reactome; R-RNO-75157; FasL/ CD95L signaling.
Reactome; R-RNO-75158; TRAIL signaling.
PRO; PR:Q9JHX4; -.
Proteomes; UP000002494; Chromosome 9.
Bgee; ENSRNOG00000012331; -.
Genevisible; Q9JHX4; RN.
GO; GO:0031265; C:CD95 death-inducing signaling complex; IDA:RGD.
GO; GO:0044297; C:cell body; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0031264; C:death-inducing signaling complex; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0097342; C:ripoptosome; ISS:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:RGD.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0035877; F:death effector domain binding; IEA:Ensembl.
GO; GO:0005123; F:death receptor binding; IPI:RGD.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IPI:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IMP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IBA:GO_Central.
GO; GO:0030225; P:macrophage differentiation; IBA:GO_Central.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; IDA:RGD.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEP:RGD.
GO; GO:0032025; P:response to cobalt ion; IEP:RGD.
GO; GO:0009409; P:response to cold; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IDA:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IEA:Ensembl.
CDD; cd00032; CASc; 1.
InterPro; IPR033170; Caspase-8.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR001875; DED_dom.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454:SF162; PTHR10454:SF162; 1.
Pfam; PF01335; DED; 2.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SMART; SM00031; DED; 2.
SUPFAM; SSF47986; SSF47986; 2.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
PROSITE; PS50168; DED; 2.
1: Evidence at protein level;
Apoptosis; Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein;
Protease; Reference proteome; Repeat; Thiol protease; Zymogen.
PROPEP 1 218 {ECO:0000250|UniProtKB:Q14790}.
/FTId=PRO_0000432425.
CHAIN 219 378 Caspase-8 subunit p18.
/FTId=PRO_0000432426.
PROPEP 379 388 {ECO:0000250|UniProtKB:Q14790}.
/FTId=PRO_0000432427.
CHAIN 389 482 Caspase-8 subunit p10.
/FTId=PRO_0000432428.
DOMAIN 2 80 DED 1. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
DOMAIN 100 177 DED 2. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
ACT_SITE 319 319 {ECO:0000250|UniProtKB:Q14790}.
ACT_SITE 362 362 {ECO:0000250|UniProtKB:Q14790}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000250|UniProtKB:O89110}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000250|UniProtKB:O89110}.
MOD_RES 336 336 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q14790}.
MOD_RES 390 390 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q14790}.
SEQUENCE 482 AA; 55339 MW; 82B4A29330C53264 CRC64;
MDFHSCLYDI AERLGNEELA ALKFLCLDHI PQKKQESIND VLVLFQRLQE EGMLEEDNLS
FLKELLFHIS RRDLLSRVLK SSPEEMVREL QVLGKAQVSA YRVMLFKLSE DMDKEDLKSF
KFLLITEIPK CKLQDNSSLL DIFVEMEKRT ILAENNLVTL KSICFRVNRS LLGRIDDYER
SSTERRMSTE GGEELPVSVL DEVTIKMQDM WDSPGEQESE SLNSDNVYQM KSKPRGYCLI
FNNNNFSKAR EDIPKLSNMR DRKGTNYDEE ALSKTFKELH FEIVSFSDCT ASQIHEVLVS
YQSKDHKGKD CFICCILSHG DKGIVYGTDG KEASIYELTS YFTGSKCPSL AGKPKIFFIQ
ACQGNNFQKA VPVPDETGLE QEHVLEEDSS SYKNYIPDEA DFLLGMATVK NCVSYRDPTR
GTWYIQSLCQ SLRERCPRGE DILSILTGVN YDVSNKDNPR NMGKQMPQPI FTLRKKLFFP
PN


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