ID   CFLA_EHV2               Reviewed;         171 AA.
AC   Q66674;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Viral CASP8 and FADD-like apoptosis regulator;
DE            Short=v-CFLAR;
DE   AltName: Full=Viral FLICE-inhibitory protein;
DE            Short=v-FLIP;
GN   ORFNames=E8;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(1995).
RN   [2]
RP   FUNCTION.
RX   PubMed=9087414; DOI=10.1038/386517a0;
RA   Thome M., Schneider P., Hofmann K., Fickenscher H., Meinl E., Neipel F.,
RA   Mattmann C., Burns K., Bodmer J.-L., Schroeter M., Scaffidi C.,
RA   Krammer P.H., Peter M.E., Tschopp J.;
RT   "Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death
RT   receptors.";
RL   Nature 386:517-521(1997).
RN   [3]
RP   FUNCTION.
RX   PubMed=9037025; DOI=10.1073/pnas.94.4.1172;
RA   Bertin J., Armstrong R.C., Ottilie S., Martin D.A., Wang Y., Banks S.,
RA   Wang G.-H., Senkevich T.G., Alnemri E.S., Moss B., Lenardo M.J.,
RA   Tomaselli K.J., Cohen J.I.;
RT   "Death effector domain-containing herpesvirus and poxvirus proteins inhibit
RT   both Fas- and TNFR1-induced apoptosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:1172-1176(1997).
CC   -!- FUNCTION: Inhibits TNFRSF1A, TNFRSF6, TNFRSF10 and TNFRSF12 induced
CC       apoptosis. May interfere with caspase-8 recruitment and activation at
CC       the death-inducing signaling complex (DISC). May lead to higher virus
CC       production and contribute to virus persistence and oncogenicity.
CC       {ECO:0000269|PubMed:9037025, ECO:0000269|PubMed:9087414}.
CC   -!- SUBUNIT: Associates with the death-inducing signaling complex (DISC)
CC       formed by TNFRSF6, FADD and caspase-8. Interacts with FADD.
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DR   EMBL; U20824; AAC13862.1; -; Genomic_DNA.
DR   PIR; S55668; S55668.
DR   RefSeq; NP_042671.1; NC_001650.2.
DR   SMR; Q66674; -.
DR   GeneID; 1461077; -.
DR   KEGG; vg:1461077; -.
DR   Proteomes; UP000007083; Genome.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0019050; P:suppression by virus of host apoptotic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.533.10; -; 2.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR001875; DED_dom.
DR   InterPro; IPR002398; Pept_C14.
DR   PANTHER; PTHR10454; PTHR10454; 1.
DR   Pfam; PF01335; DED; 1.
DR   SMART; SM00031; DED; 2.
DR   SUPFAM; SSF47986; SSF47986; 1.
DR   PROSITE; PS50168; DED; 2.
PE   4: Predicted;
KW   Apoptosis; Host-virus interaction;
KW   Inhibition of host apoptosis by viral FLIP-like protein;
KW   Modulation of host cell apoptosis by virus; Reference proteome; Repeat.
FT   CHAIN           1..171
FT                   /note="Viral CASP8 and FADD-like apoptosis regulator"
FT                   /id="PRO_0000072820"
FT   DOMAIN          1..74
FT                   /note="DED 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
FT   DOMAIN          92..171
FT                   /note="DED 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
SQ   SEQUENCE   171 AA;  19925 MW;  4CEAF9D0EE04D9AE CRC64;
     MSHYSMIDTY FSLDEDETET YLYLCRDLLK NKGEFQCTRD AFKFLSDYAC LSAANQMELL
     FRVGRLDLIR RIFGQTWTPD SCPRYYMPIC SPFRCLMALV NDFLSDKEVE EMYFLCAPRL
     ESHLEPGSKK SFLRLASLLE DLELLGGDKL TFLRHLLTTI GRADLVKNLQ V