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Database: UniProt
Entry: ARBH_MHV68
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ID   ARBH_MHV68              Reviewed;         171 AA.
AC   P89884;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   29-SEP-2021, entry version 98.
DE   RecName: Full=Apoptosis regulator Bcl-2 homolog;
DE            Short=vBcl-2;
DE   AltName: Full=Protein M11;
GN   Name=vBCL2;
OS   Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=33708;
OH   NCBI_TaxID=10129; Apodemus sylvaticus (European woodmouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8083987; DOI=10.1128/jvi.68.10.6496-6504.1994;
RA   Stewart J.P., Janjua N.J., Sunil-Chandra N.P., Nash A.A., Arrand J.R.;
RT   "Characterization of murine gammaherpesvirus 68 glycoprotein B (gB)
RT   homolog: similarity to Epstein-Barr virus gB (gp110).";
RL   J. Virol. 68:6496-6504(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8648686; DOI=10.1128/jvi.70.6.3528-3535.1996;
RA   Stewart J.P., Janjua N.J., Pepper S.D., Bennion G., Mackett M., Allen T.,
RA   Nash A.A., Arrand J.R.;
RT   "Identification and characterization of murine gammaherpesvirus 68 gp150: a
RT   virion membrane glycoprotein.";
RL   J. Virol. 70:3528-3535(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8638414; DOI=10.1006/viro.1996.0274;
RA   Pepper S.D., Stewart J.P., Arrand J.R., Mackett M.;
RT   "Murine gammaherpesvirus-68 encodes homologues of thymidine kinase and
RT   glycoprotein H: sequence, expression, and characterization of pyrimidine
RT   kinase activity.";
RL   Virology 219:475-479(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G2.4;
RX   PubMed=9191940; DOI=10.1099/0022-1317-78-6-1425;
RA   Mackett M., Stewart J.P., de V Pepper S., Chee M., Efstathiou S.,
RA   Nash A.A., Arrand J.R.;
RT   "Genetic content and preliminary transcriptional analysis of a
RT   representative region of murine gammaherpesvirus 68.";
RL   J. Gen. Virol. 78:1425-1433(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9225045; DOI=10.1099/0022-1317-78-7-1675;
RA   Bowden R.J., Simas J.P., Davis A.J., Efstathiou S.;
RT   "Murine gammaherpesvirus 68 encodes tRNA-like sequences which are expressed
RT   during latency.";
RL   J. Gen. Virol. 78:1675-1687(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G2.4;
RX   PubMed=9223479; DOI=10.1128/jvi.71.8.5894-5904.1997;
RA   Virgin H.W., Latreille P., Wamsley P., Hallsworth K., Weck K.E.,
RA   Dal Canto A.J., Speck S.H.;
RT   "Complete sequence and genomic analysis of murine gammaherpesvirus 68.";
RL   J. Virol. 71:5894-5904(1997).
RN   [7]
RP   FUNCTION.
RX   PubMed=10573168; DOI=10.1099/0022-1317-80-10-2737;
RA   Wang G.H., Garvey T.L., Cohen J.I.;
RT   "The murine gammaherpesvirus-68 M11 protein inhibits Fas- and TNF-induced
RT   apoptosis.";
RL   J. Gen. Virol. 80:2737-2740(1999).
RN   [8]
RP   FUNCTION.
RX   PubMed=11205127; DOI=10.1007/s007050070030;
RA   Roy D.J., Ebrahimi B.C., Dutia B.M., Nash A.A., Stewart J.P.;
RT   "Murine gammaherpesvirus M11 gene product inhibits apoptosis and is
RT   expressed during virus persistence.";
RL   Arch. Virol. 145:2411-2420(2000).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15604429; DOI=10.1099/vir.0.80480-0;
RA   de Lima B.D., May J.S., Marques S., Simas J.P., Stevenson P.G.;
RT   "Murine gammaherpesvirus 68 bcl-2 homologue contributes to latency
RT   establishment in vivo.";
RL   J. Gen. Virol. 86:31-40(2005).
RN   [10]
RP   STRUCTURE BY NMR OF 1-136.
RX   PubMed=16201011; DOI=10.1371/journal.ppat.0010010;
RA   Loh J., Huang Q., Petros A.M., Nettesheim D., van Dyk L.F., Labrada L.,
RA   Speck S.H., Levine B., Olejniczak E.T., Virgin H.W.;
RT   "A surface groove essential for viral Bcl-2 function during chronic
RT   infection in vivo.";
RL   PLoS Pathog. 1:E10-E10(2005).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-136, INTERACTION WITH HOST
RP   BECN1, FUNCTION, SUBCELLULAR LOCATION, AND DISULFIDE BOND.
RX   PubMed=18797192; DOI=10.4161/auto.6803;
RA   Sinha S., Colbert C.L., Becker N., Wei Y., Levine B.;
RT   "Molecular basis of the regulation of Beclin 1-dependent autophagy by the
RT   gamma-herpesvirus 68 Bcl-2 homolog M11.";
RL   Autophagy 4:989-997(2008).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 5-135, FUNCTION, SUBCELLULAR
RP   LOCATION, AND INTERACTION WITH BECN1; BAX AND BAK.
RX   PubMed=18248095; DOI=10.1371/journal.ppat.0040025;
RA   Ku B., Woo J.S., Liang C., Lee K.H., Hong H.S., E X., Kim K.S., Jung J.U.,
RA   Oh B.H.;
RT   "Structural and biochemical bases for the inhibition of autophagy and
RT   apoptosis by viral BCL-2 of murine gamma-herpesvirus 68.";
RL   PLoS Pathog. 4:E25-E25(2008).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-136, AND DISULFIDE BONDS.
RX   PubMed=24443581; DOI=10.1074/jbc.m113.515361;
RA   Su M., Mei Y., Sanishvili R., Levine B., Colbert C.L., Sinha S.;
RT   "Targeting gamma-herpesvirus 68 Bcl-2-mediated down-regulation of
RT   autophagy.";
RL   J. Biol. Chem. 289:8029-8040(2014).
CC   -!- FUNCTION: Plays a role in the protection against apoptosis mediated by
CC       cytotoxic cells during the immune response to acute and persistent
CC       viral infection. Contributes therefore to latency establishment. Plays
CC       also a role in the inhibition of host starvation-induced autophagy
CC       which ultimately contributes to the viral chronic infection.
CC       {ECO:0000269|PubMed:10573168, ECO:0000269|PubMed:11205127,
CC       ECO:0000269|PubMed:15604429, ECO:0000269|PubMed:18248095,
CC       ECO:0000269|PubMed:18797192}.
CC   -!- SUBUNIT: Interacts with host BECN1; this interaction inhibits host
CC       autophagy. Interacts with host BAK1 and BAX.
CC       {ECO:0000269|PubMed:18248095, ECO:0000269|PubMed:18797192}.
CC   -!- INTERACTION:
CC       P89884; Q14457: BECN1; Xeno; NbExp=4; IntAct=EBI-8849581, EBI-949378;
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:15604429,
CC       ECO:0000269|PubMed:18248095, ECO:0000269|PubMed:18797192}.
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DR   EMBL; U91858; AAB50016.1; -; Genomic_DNA.
DR   EMBL; U97553; AAB66423.1; -; Genomic_DNA.
DR   EMBL; AF105037; AAF19336.1; -; Genomic_DNA.
DR   EMBL; GQ421301; ACV65512.1; -; Genomic_DNA.
DR   RefSeq; NP_044912.1; NC_001826.2.
DR   PDB; 2ABO; NMR; -; A=1-136.
DR   PDB; 3BL2; X-ray; 2.30 A; A/B=5-135.
DR   PDB; 3DVU; X-ray; 2.50 A; A/B=2-136.
DR   PDB; 4MI8; X-ray; 2.10 A; A/B=2-136.
DR   PDBsum; 2ABO; -.
DR   PDBsum; 3BL2; -.
DR   PDBsum; 3DVU; -.
DR   PDBsum; 4MI8; -.
DR   SMR; P89884; -.
DR   DIP; DIP-47218N; -.
DR   IntAct; P89884; 13.
DR   MINT; P89884; -.
DR   GeneID; 1497180; -.
DR   KEGG; vg:1497180; -.
DR   EvolutionaryTrace; P89884; -.
DR   Proteomes; UP000099649; Genome.
DR   Proteomes; UP000175018; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019050; P:suppression by virus of host apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.437.10; -; 1.
DR   InterPro; IPR029450; Apo_reg_M11.
DR   InterPro; IPR036834; Bcl-2-like_sf.
DR   Pfam; PF15286; Bcl-2_3; 1.
DR   SUPFAM; SSF56854; SSF56854; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Host cytoplasm; Host-virus interaction;
KW   Inhibition of host apoptosis by viral BCL2-like protein;
KW   Inhibition of host autophagy by virus;
KW   Modulation of host cell apoptosis by virus; Reference proteome.
FT   CHAIN           1..171
FT                   /note="Apoptosis regulator Bcl-2 homolog"
FT                   /id="PRO_0000443226"
FT   DISULFID        29
FT                   /note="Interchain (with C-104)"
FT   DISULFID        104
FT                   /note="Interchain (with C-29)"
FT   HELIX           7..22
FT                   /evidence="ECO:0007829|PDB:4MI8"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:4MI8"
FT   HELIX           32..55
FT                   /evidence="ECO:0007829|PDB:4MI8"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:4MI8"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:4MI8"
FT   HELIX           67..80
FT                   /evidence="ECO:0007829|PDB:4MI8"
FT   HELIX           85..101
FT                   /evidence="ECO:0007829|PDB:4MI8"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:2ABO"
FT   HELIX           110..125
FT                   /evidence="ECO:0007829|PDB:4MI8"
FT   HELIX           128..131
FT                   /evidence="ECO:0007829|PDB:4MI8"
SQ   SEQUENCE   171 AA;  19743 MW;  43937262635E3446 CRC64;
     MSHKKSGTYW ATLITAFLKT VSKVEELDCV DSAVLVDVSK IITLTQEFRR HYDSVYRADY
     GPALKNWKRD LSKLFTSLFV DVINSGRIVG FFDVGRYVCE EVLCPGSWTE DHELLNDCMT
     HFFIENNLMN HFPLEDIFLA QRKFQTTGFT FLLHALAKVL PRIYSGNVIY V
//
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