VFLIP_HHV8P
ID VFLIP_HHV8P Reviewed; 188 AA.
AC F5HEZ4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Viral FLICE protein;
DE Short=vFLIP;
GN Name=ORF71;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP FUNCTION, AND INTERACTION WITH HOST TRAF2; MAP3K14; IKBKB AND RIPK1.
RX PubMed=10523854; DOI=10.1038/sj.onc.1202976;
RA Chaudhary P.M., Jasmin A., Eby M.T., Hood L.;
RT "Modulation of the NF-kappa B pathway by virally encoded death effector
RT domains-containing proteins.";
RL Oncogene 18:5738-5746(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH HOST TRAF2 AND IKBKG.
RX PubMed=16311516; DOI=10.1038/sj.embor.7400580;
RA Guasparri I., Wu H., Cesarman E.;
RT "The KSHV oncoprotein vFLIP contains a TRAF-interacting motif and requires
RT TRAF2 and TRAF3 for signalling.";
RL EMBO Rep. 7:114-119(2006).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST CADM1.
RX PubMed=29698475; DOI=10.1371/journal.ppat.1006968;
RA Hunte R., Alonso P., Thomas R., Bazile C.A., Ramos J.C., van der Weyden L.,
RA Dominguez-Bendala J., Khan W.N., Shembade N.;
RT "CADM1 is essential for KSHV-encoded vGPCR-and vFLIP-mediated chronic NF-
RT kappaB activation.";
RL PLoS Pathog. 14:E1006968-E1006968(2018).
CC -!- FUNCTION: Plays a role in the modulation of host signaling pathways by
CC acting as an activator of both the classic and the alternative NF-
CC kappa-B pathways. Thereby, initiates an important range of cellular
CC processes to promote cell survival, proliferation and protection from
CC apoptosis. {ECO:0000269|PubMed:10523854, ECO:0000269|PubMed:16311516,
CC ECO:0000269|PubMed:29698475}.
CC -!- SUBUNIT: Interacts with host RIPK1, TRAF2, MAP3K14, IKBKB, and IKBKG.
CC Interacts with host CADM1; this interaction is essential for chronic
CC NF-kappa-B activation. {ECO:0000269|PubMed:10523854,
CC ECO:0000269|PubMed:16311516, ECO:0000269|PubMed:29698475}.
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DR EMBL; AF148805; AAD46498.1; -; Genomic_DNA.
DR RefSeq; YP_001129429.1; NC_009333.1.
DR PDB; 5LDE; X-ray; 3.38 A; A/B=1-188.
DR PDBsum; 5LDE; -.
DR SMR; F5HEZ4; -.
DR BioGRID; 1776997; 11.
DR PRIDE; F5HEZ4; -.
DR GeneID; 4961494; -.
DR KEGG; vg:4961494; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0039652; P:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Activation of host NF-kappa-B by virus; Apoptosis;
KW 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..188
FT /note="Viral FLICE protein"
FT /id="PRO_0000423909"
FT DOMAIN 2..74
FT /note="DED 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
FT DOMAIN 93..169
FT /note="DED 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:5LDE"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:5LDE"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:5LDE"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:5LDE"
SQ SEQUENCE 188 AA; 21474 MW; 37CFE147EAE45371 CRC64;
MATYEVLCEV ARKLGTDDRE VVLFLLNVFI PQPTLAQLIG ALRALKEEGR LTFPLLAECL
FRAGRRDLLR DLLHLDPRFL ERHLAGTMSY FSPYQLTVLH VDGELCARDI RSLIFLSKDT
IGSRSTPQTF LHWVYCMENL DLLGPTDVDA LMSMLRSLSR VDLQRQVQTL MGLHLSGPSH
SQHYRHTP
