EAR_EBVA8
ID EAR_EBVA8 Reviewed; 191 AA.
AC P0C6Z1; Q777H0;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Apoptosis regulator BHRF1;
DE AltName: Full=Early antigen protein R;
DE Short=EA-R;
DE AltName: Full=Nuclear antigen;
GN ORFNames=BHRF1;
OS Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=82830;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT "The genome of Epstein-Barr virus type 2 strain AG876.";
RL Virology 350:164-170(2006).
CC -!- FUNCTION: Prevents premature death of the host cell during virus
CC production, which would otherwise reduce the amount of progeny virus.
CC Acts as a host B-cell leukemia/lymphoma 2 (Bcl-2) homolog, and
CC interacts with pro-apoptotic proteins to prevent mitochondria
CC permeabilization, release of cytochrome c and subsequent apoptosis of
CC the host cell (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with isoform 1 of host VRK2; this interaction is
CC involved in protecting cells from apoptosis. Interacts with host PRA1;
CC this interaction seems to modulate BHRF1 anti-apoptotic activity.
CC Interacts with of host BCL2L11 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Host mitochondrion. Note=also observed in the
CC perinuclear region of the cell. {ECO:0000250}.
CC -!- MISCELLANEOUS: EA-R is part of the restricted EA-complex.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; DQ279927; ABB89223.1; -; Genomic_DNA.
DR RefSeq; YP_001129442.1; NC_009334.1.
DR RefSeq; YP_401646.1; NC_007605.1.
DR PDB; 2WH6; X-ray; 1.50 A; A=1-160.
DR PDB; 4OYD; X-ray; 1.80 A; A/C=2-158.
DR PDBsum; 2WH6; -.
DR PDBsum; 4OYD; -.
DR BMRB; P0C6Z1; -.
DR SMR; P0C6Z1; -.
DR DNASU; 3783706; -.
DR GeneID; 3783706; -.
DR GeneID; 5176205; -.
DR KEGG; vg:3783706; -.
DR KEGG; vg:5176205; -.
DR Proteomes; UP000007639; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR Pfam; PF00452; Bcl-2; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01258; BH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Early protein; Glycoprotein; Host membrane;
KW Host mitochondrion; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..191
FT /note="Apoptosis regulator BHRF1"
FT /id="PRO_0000375928"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..18
FT /note="Interaction with host VRK2"
FT /evidence="ECO:0000250"
FT REGION 89..142
FT /note="Interaction with host VRK2"
FT /evidence="ECO:0000250"
FT MOTIF 89..109
FT /note="BH1"
FT MOTIF 142..157
FT /note="BH2"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:2WH6"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:2WH6"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:2WH6"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:2WH6"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:2WH6"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2WH6"
FT HELIX 98..117
FT /evidence="ECO:0007829|PDB:2WH6"
FT HELIX 123..137
FT /evidence="ECO:0007829|PDB:2WH6"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2WH6"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:2WH6"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:2WH6"
SQ SEQUENCE 191 AA; 21893 MW; 8108BCB94F81DC8B CRC64;
MAYSTREILL ALCIRDSRVH GNGTLHPVLE LAARETPLRL SPEDTVVLRY HVLLEEIIER
NSETFTETWN RFITHTEHVD LDFNSVFLEI FHRGDPSLGR ALAWMAWCMH ACRTLCCNQS
TPYYVVDLSV RGMLEASEGL DGWIHQQGGW STLIEDNIPG SRRFSWTLFL AGLTLSLLVI
CSYLFISRGR H