ID   VCLAP_EHV2              Reviewed;         311 AA.
AC   Q66677;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   23-FEB-2022, entry version 85.
DE   RecName: Full=CARD domain-containing protein E10;
GN   Name=E10;
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   SEQUENCE REVISION.
RA   Davison A.J.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=10187771; DOI=10.1074/jbc.274.15.9962;
RA   Thome M., Martinon F., Hofmann K., Rubio V., Steiner V., Schneider P.,
RA   Mattmann C., Tschopp J.;
RT   "Equine herpesvirus-2 E10 gene product, but not its cellular homologue,
RT   activates NF-kappaB transcription factor and c-Jun N-terminal kinase.";
RL   J. Biol. Chem. 274:9962-9968(1999).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-310 AND CYS-311.
RX   PubMed=11238466; DOI=10.1083/jcb.152.5.1115;
RA   Thome M., Gaide O., Micheau O., Martinon F., Bonnet D., Gonzalez M.,
RA   Tschopp J.;
RT   "Equine herpesvirus protein E10 induces membrane recruitment and
RT   phosphorylation of its cellular homologue, bcl-10.";
RL   J. Cell Biol. 152:1115-1122(2001).
CC   -!- FUNCTION: Activates host NF-kappa-B and JNK pathways. Induces
CC       hyperphosphorylation and redistribution of host bcl-10 from the
CC       cytoplasm to the plasma membrane. The inhibitory effect of cellular
CC       bcl-10 on NF-kappa-B pathway is then overcome allowing NF-kappa-B
CC       activation. {ECO:0000269|PubMed:10187771, ECO:0000269|PubMed:11238466}.
CC   -!- INTERACTION:
CC       Q66677; O95999: BCL10; Xeno; NbExp=2; IntAct=EBI-11709474, EBI-958922;
CC       Q66677; Q9Z0H7: Bcl10; Xeno; NbExp=3; IntAct=EBI-11709474, EBI-8545413;
CC   -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000269|PubMed:11238466}.
CC       Note=E10 does not contain a putative transmembrane and must therefore
CC       be targeted to the plasma membrane in a different manner. The two
CC       cysteines located on the C-terminal region are essential for the
CC       protein localization and constitute a consensus site for
CC       geranylgeranylation.
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DR   EMBL; U20824; AAC13865.2; -; Genomic_DNA.
DR   PIR; S55671; S55671.
DR   RefSeq; NP_042674.2; NC_001650.2.
DR   SMR; Q66677; -.
DR   IntAct; Q66677; 3.
DR   GeneID; 1461015; -.
DR   KEGG; vg:1461015; -.
DR   Proteomes; UP000007083; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IDA:AgBase.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043621; F:protein self-association; IPI:AgBase.
DR   GO; GO:0085033; P:induction by symbiont of host I-kappaB kinase/NF-kappaB cascade; IDA:AgBase.
DR   GO; GO:0075131; P:induction by symbiont of host protein kinase-mediated signal transduction; IDA:AgBase.
DR   GO; GO:0039652; P:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:AgBase.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; IDA:AgBase.
DR   Gene3D; 1.10.533.10; -; 1.
DR   InterPro; IPR033238; BCL10/E10.
DR   InterPro; IPR001315; CARD.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   PANTHER; PTHR34920; PTHR34920; 1.
DR   Pfam; PF00619; CARD; 1.
DR   SUPFAM; SSF47986; SSF47986; 1.
DR   PROSITE; PS50209; CARD; 1.
PE   1: Evidence at protein level;
KW   Activation of host NF-kappa-B by virus; Host cell membrane; Host membrane;
KW   Host-virus interaction; Membrane; Reference proteome.
FT   CHAIN           1..311
FT                   /note="CARD domain-containing protein E10"
FT                   /id="PRO_0000405984"
FT   DOMAIN          21..110
FT                   /note="CARD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT   REGION          125..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         310
FT                   /note="C->A: Loss of host plasma membrane localization."
FT                   /evidence="ECO:0000269|PubMed:11238466"
FT   MUTAGEN         311
FT                   /note="C->A: Loss of host plasma membrane localization."
FT                   /evidence="ECO:0000269|PubMed:11238466"
SQ   SEQUENCE   311 AA;  32602 MW;  04EC68C7353D723B CRC64;
     MAEKYPLQAG DPCVTLTEED IWDVERLCLE ELRVLLVSHL KSHKHLDHLR AKKILSREDA
     EEVSSRATSR SRAGLLVDMC QDHPRGFQCL KESCKNEVGQ EHLVDLLERA FEKHCGDKLT
     QKWWESGADG RNPRRPPGSE DNSGYTALLP TNPSGGGPSI GSGHSRPRGR DDSGGIGGGV
     YPFSHGGARV VGGGWGGWGE SGGAGRGGSL LSGGHGGHPP HGGPGGGGRD YYGGGGSGYY
     ESIPEPANFP NSGGGGRGGG VRYDAGGDGR LGGLPPDPQE VDDPSLSVQG RGGPAPDPPS
     PPLRTRRFFC C