ID   EAR_EBVG                Reviewed;         191 AA.
AC   P0C736;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 47.
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 GD1) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10376;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA   Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA   Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT   "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT   nasopharyngeal carcinoma patient.";
RL   J. Virol. 79:15323-15330(2005).
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 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; AY961628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PDB; 2V6Q; X-ray; 2.70 A; A=1-160.
DR   PDBsum; 2V6Q; -.
DR   BMRB; P0C736; -.
DR   SMR; P0C736; -.
DR   IntAct; P0C736; 14.
DR   MINT; P0C736; -.
DR   EvolutionaryTrace; P0C736; -.
DR   Proteomes; UP000007641; 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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..191
FT                   /note="Apoptosis regulator BHRF1"
FT                   /id="PRO_0000375929"
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:2V6Q"
FT   HELIX           27..35
FT                   /evidence="ECO:0007829|PDB:2V6Q"
FT   HELIX           45..60
FT                   /evidence="ECO:0007829|PDB:2V6Q"
FT   HELIX           62..75
FT                   /evidence="ECO:0007829|PDB:2V6Q"
FT   HELIX           79..91
FT                   /evidence="ECO:0007829|PDB:2V6Q"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:2V6Q"
FT   HELIX           98..117
FT                   /evidence="ECO:0007829|PDB:2V6Q"
FT   HELIX           123..137
FT                   /evidence="ECO:0007829|PDB:2V6Q"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:2V6Q"
FT   HELIX           141..146
FT                   /evidence="ECO:0007829|PDB:2V6Q"
FT   HELIX           150..155
FT                   /evidence="ECO:0007829|PDB:2V6Q"
SQ   SEQUENCE   191 AA;  21879 MW;  60C7804A80A00E9F CRC64;
     MAYSTREILL ALCIRDSRVH GNGTLHPVLE LAARETPLRL SPEDTVVLRY HVLLEEIIER
     NSETFTETWN RFITHTEHVD LDFNSVFVEI FHRGDPSLGR ALAWMAWCMH ACRTLCCNQS
     TPYYVVDLSV RGMLEASEGL DGWIHQQGGW STLIEDNIPG SRRFSWTLFL AGLTLSLLVI
     CSYLFISRGR H