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Database: UniProt
Entry: B2CMK5_CRIGR
LinkDB: B2CMK5_CRIGR
Original site: B2CMK5_CRIGR 
ID   B2CMK5_CRIGR            Unreviewed;       481 AA.
AC   B2CMK5;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Caspase-8 {ECO:0000313|EMBL:ACB41092.1, ECO:0000313|Ensembl:ENSCGRP00001022456.1};
DE            EC=3.4.22.61 {ECO:0000313|RefSeq:NP_001233725.1};
GN   Name=Casp8 {ECO:0000313|Ensembl:ENSCGRP00001022456.1,
GN   ECO:0000313|RefSeq:NP_001233725.1};
GN   ORFNames=I79_014611 {ECO:0000313|EMBL:EGV99437.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:ACB41092.1};
RN   [1] {ECO:0000313|EMBL:ACB41092.1, ECO:0000313|RefSeq:NP_001233725.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17658284; DOI=10.1016/j.ymben.2007.06.001;
RA   Yun C.Y., Liu S., Lim S.F., Wang T., Chung B.Y., Jiat Teo J., Chuan K.H.,
RA   Soon A.S., Goh K.S., Song Z.;
RT   "Specific inhibition of caspase-8 and -9 in CHO cells enhances cell
RT   viability in batch and fed-batch cultures.";
RL   Metab. Eng. 9:406-418(2007).
RN   [2] {ECO:0000313|EMBL:ACB41092.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yun C.Y., Liu S., Lim S.F., Wang T., Chung B.Y., Teo J.J., Chuan K.H.,
RA   Soon A.S., Goh K.S., Song Z.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001233725.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21945585;
RA   Becker J., Hackl M., Rupp O., Jakobi T., Schneider J., Szczepanowski R.,
RA   Bekel T., Borth N., Goesmann A., Grillari J., Kaltschmidt C., Noll T.,
RA   Puhler A., Tauch A., Brinkrolf K.;
RT   "Unraveling the Chinese hamster ovary cell line transcriptome by next-
RT   generation sequencing.";
RL   J. Biotechnol. 156:227-235(2011).
RN   [4] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
RN   [5] {ECO:0000313|EMBL:EGV99437.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|Ensembl:ENSCGRP00001022456.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [7] {ECO:0000313|RefSeq:NP_001233725.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C14A family.
CC       {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR   EMBL; EU527788; ACB41092.1; -; mRNA.
DR   EMBL; JH000741; EGV99437.1; -; Genomic_DNA.
DR   RefSeq; NP_001233725.1; NM_001246796.1.
DR   STRING; 10029.B2CMK5; -.
DR   MEROPS; C14.009; -.
DR   PaxDb; 10029-NP_001233725-1; -.
DR   Ensembl; ENSCGRT00001026701.1; ENSCGRP00001022456.1; ENSCGRG00001020998.1.
DR   GeneID; 100689369; -.
DR   KEGG; cge:100689369; -.
DR   CTD; 841; -.
DR   eggNOG; KOG3573; Eukaryota.
DR   GeneTree; ENSGT00940000160319; -.
DR   OMA; WNRIEDG; -.
DR   OrthoDB; 2873736at2759; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
DR   Proteomes; UP000694386; Unplaced.
DR   Proteomes; UP001108280; Chromosome 2.
DR   GO; GO:0031265; C:CD95 death-inducing signaling complex; IEA:Ensembl.
DR   GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0097342; C:ripoptosome; ISS:UniProtKB.
DR   GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0035877; F:death effector domain binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
DR   GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
DR   GO; GO:0045862; P:positive regulation of proteolysis; IEA:Ensembl.
DR   GO; GO:0051604; P:protein maturation; IEA:Ensembl.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IEA:Ensembl.
DR   CDD; cd00032; CASc; 1.
DR   CDD; cd08333; DED_Caspase_8_r1; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 2.
DR   InterPro; IPR033170; Caspase-8_DED1.
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; IPR001875; DED_dom.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR001309; Pept_C14_p20.
DR   InterPro; IPR015917; Pept_C14A.
DR   PANTHER; PTHR48169:SF5; CASPASE 10; 1.
DR   PANTHER; PTHR48169; DED DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01335; DED; 2.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 1.
DR   SMART; SM00031; DED; 2.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   SUPFAM; SSF47986; DEATH domain; 2.
DR   PROSITE; PS01122; CASPASE_CYS; 1.
DR   PROSITE; PS01121; CASPASE_HIS; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
DR   PROSITE; PS50168; DED; 2.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          2..80
FT                   /note="DED"
FT                   /evidence="ECO:0000259|PROSITE:PS50168"
FT   DOMAIN          100..178
FT                   /note="DED"
FT                   /evidence="ECO:0000259|PROSITE:PS50168"
FT   DOMAIN          235..367
FT                   /note="Caspase family p20"
FT                   /evidence="ECO:0000259|PROSITE:PS50208"
FT   DOMAIN          391..480
FT                   /note="Caspase family p10"
FT                   /evidence="ECO:0000259|PROSITE:PS50207"
SQ   SEQUENCE   481 AA;  55708 MW;  B5076FF0C1D1216A CRC64;
     MDFRNCLYKI AENLDSSELA ALKFLCLDYI PQKKQEPIKD ALMLFQVLQE KGLLEEDNLS
     FLKELIFLIN RLDLLSNTLN SSKEEMVREL QVPDKAQVSA YRVMLFKLSE EVTKSELKSF
     KFFLNEEIPK CKLYDDNSSL LDIFVEMEKR VILREENLDA LKSICAQVNK SLLEKIEAYE
     KSSRGRMSLE GGAESPVSVL DGESYFRMQE TWDSQREQDS DSQVSHRIYQ MKSKPRGYCL
     IINNNDFSEA RKNIPRFHKM KDRKGTNYDE EALTETFKEL HFEVKPYRDC TANKIHEVLR
     FYQSMDHKDK DCFICCILSH GDTGIIYGTD GKEAPIYELT SYFTGSECPS LAGKPKIFFI
     QACQGDNYQK AVLVETDWEE MVSFLDVDSS QKSYIPDEAD FLLGMATVKN CVSYRDPTQG
     TWYIQSLCQS LRKRCPQGDD ILSILTGVNY DVSNKDDRKN MGKQMPQPIF TLRKKLFFPP
     K
//
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