MEQ_GAHVM
ID MEQ_GAHVM Reviewed; 339 AA.
AC Q9DGW5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Oncoprotein MEQ;
DE Short=MEQ;
GN Name=MDV005; Synonyms=MDV076;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
RN [2]
RP INTERACTION WITH HOST JUN.
RX PubMed=7769661; DOI=10.1128/jvi.69.7.4037-4044.1995;
RA Qian Z., Brunovskis P., Rauscher F. III, Lee L., Kung H.J.;
RT "Transactivation activity of Meq, a Marek's disease herpesvirus bZIP
RT protein persistently expressed in latently infected transformed T cells.";
RL J. Virol. 69:4037-4044(1995).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=9060682; DOI=10.1128/jvi.71.4.3188-3196.1997;
RA Liu J.L., Lee L.F., Ye Y., Qian Z., Kung H.J.;
RT "Nucleolar and nuclear localization properties of a herpesvirus bZIP
RT oncoprotein, MEQ.";
RL J. Virol. 71:3188-3196(1997).
RN [4]
RP FUNCTION.
RX PubMed=9420237; DOI=10.1128/jvi.72.1.388-395.1998;
RA Liu J.L., Ye Y., Lee L.F., Kung H.J.;
RT "Transforming potential of the herpesvirus oncoprotein MEQ: morphological
RT transformation, serum-independent growth, and inhibition of apoptosis.";
RL J. Virol. 72:388-395(1998).
RN [5]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-42 BY HOST CDK2, AND
RP MUTAGENESIS OF SER-42.
RX PubMed=10196317; DOI=10.1128/jvi.73.5.4208-4219.1999;
RA Liu J.L., Ye Y., Qian Z., Qian Y., Templeton D.J., Lee L.F., Kung H.J.;
RT "Functional interactions between herpesvirus oncoprotein MEQ and cell cycle
RT regulator CDK2.";
RL J. Virol. 73:4208-4219(1999).
RN [6]
RP REVIEW.
RX PubMed=11022789; DOI=10.1023/a:1008132313289;
RA Liu J.L., Kung H.J.;
RT "Marek's disease herpesvirus transforming protein MEQ: a c-Jun analogue
RT with an alternative life style.";
RL Virus Genes 21:51-64(2000).
RN [7]
RP SUBUNIT.
RX PubMed=19692466; DOI=10.1128/jvi.01393-09;
RA Brown A.C., Smith L.P., Kgosana L., Baigent S.J., Nair V., Allday M.J.;
RT "Homodimerization of the Meq viral oncoprotein is necessary for induction
RT of T-cell lymphoma by Marek's disease virus.";
RL J. Virol. 83:11142-11151(2009).
CC -!- FUNCTION: Functions as a DNA-binding transcription factor. Promotes
CC transformation, host cell growth, host cell-cycle progression through
CC G1/S phase, and possesses antiapoptotic activity. Forms functional
CC heterodimers with host JUN. These heterodimers bind with high affinity
CC DNA sequences called MEQ-responsive elements MERE I (TGACA/GTCA), while
CC MEQ homodimers bind a second type of sites termed MERE II (ACACA). Both
CC homo and heterodimerization of MEQ are required for oncogenesis.
CC {ECO:0000269|PubMed:9420237}.
CC -!- SUBUNIT: Homodimer. Interacts with host JUN; this interaction allows
CC MEQ to engage in host cell processes by disguising itself as a cellular
CC JUN. {ECO:0000269|PubMed:19692466, ECO:0000269|PubMed:7769661}.
CC -!- INTERACTION:
CC Q9DGW5; P18846: ATF1; Xeno; NbExp=2; IntAct=EBI-10889526, EBI-852794;
CC Q9DGW5; P15336: ATF2; Xeno; NbExp=2; IntAct=EBI-10889526, EBI-1170906;
CC Q9DGW5; P17544: ATF7; Xeno; NbExp=2; IntAct=EBI-10889526, EBI-765623;
CC Q9DGW5; O14867: BACH1; Xeno; NbExp=2; IntAct=EBI-10889526, EBI-1263541;
CC Q9DGW5; P16220: CREB1; Xeno; NbExp=2; IntAct=EBI-10889526, EBI-711855;
CC Q9DGW5; P0C746: HBZ; Xeno; NbExp=2; IntAct=EBI-10889526, EBI-10890294;
CC Q9DGW5; P05412: JUN; Xeno; NbExp=3; IntAct=EBI-10889526, EBI-852823;
CC Q9DGW5; P18870: JUN; Xeno; NbExp=5; IntAct=EBI-10889526, EBI-445826;
CC Q9DGW5; P09450: Junb; Xeno; NbExp=2; IntAct=EBI-10889526, EBI-5347760;
CC Q9DGW5; P17275: JUNB; Xeno; NbExp=2; IntAct=EBI-10889526, EBI-748062;
CC Q9DGW5; P17535: JUND; Xeno; NbExp=2; IntAct=EBI-10889526, EBI-2682803;
CC Q9DGW5; Q16621: NFE2; Xeno; NbExp=2; IntAct=EBI-10889526, EBI-726369;
CC Q9DGW5; Q16649: NFIL3; Xeno; NbExp=3; IntAct=EBI-10889526, EBI-3951858;
CC Q9DGW5; Q5ZIZ6: RCJMB04_22g9; Xeno; NbExp=3; IntAct=EBI-10889526, EBI-10889881;
CC Q9DGW5; P08106; Xeno; NbExp=5; IntAct=EBI-10889526, EBI-1636307;
CC -!- SUBCELLULAR LOCATION: Host nucleus, host nucleolus
CC {ECO:0000269|PubMed:10196317, ECO:0000269|PubMed:9060682}.
CC Note=Expressed in both the nucleus and the cytoplasm during the G1/S
CC boundary and early S phase of host cell cycle.
CC -!- PTM: Phosphorylated by host CDK2; this phosphorylation greatly reduces
CC the DNA binding activity of MEQ. {ECO:0000269|PubMed:10196317}.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
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DR EMBL; AF243438; AAG14255.1; -; Genomic_DNA.
DR EMBL; AF243438; AAG14278.1; -; Genomic_DNA.
DR RefSeq; YP_001033919.1; NC_002229.3.
DR RefSeq; YP_001033993.1; NC_002229.3.
DR SMR; Q9DGW5; -.
DR DIP; DIP-61102N; -.
DR IntAct; Q9DGW5; 19.
DR iPTMnet; Q9DGW5; -.
DR GeneID; 4811549; -.
DR GeneID; 4811550; -.
DR KEGG; vg:4811549; -.
DR KEGG; vg:4811550; -.
DR Proteomes; UP000008072; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IDA:AgBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:AgBase.
DR GO; GO:0042802; F:identical protein binding; TAS:AgBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:0008134; F:transcription factor binding; IDA:AgBase.
DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0019056; P:modulation by virus of host transcription; IDA:AgBase.
DR GO; GO:0032897; P:negative regulation of viral transcription; IMP:AgBase.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:AgBase.
DR GO; GO:0046719; P:regulation by virus of viral protein levels in host cell; TAS:AgBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; TAS:AgBase.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW DNA-binding; G1/S host cell cycle checkpoint dysregulation by virus;
KW Host nucleus; Host-virus interaction;
KW Modulation of host cell apoptosis by virus;
KW Modulation of host cell cycle by virus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..339
FT /note="Oncoprotein MEQ"
FT /id="PRO_0000406419"
FT DOMAIN 57..120
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..84
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 85..113
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 120..339
FT /note="Transactivation domain"
FT REGION 145..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 62..78
FT /note="Nuclear localization signal"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine; by host CDK2"
FT /evidence="ECO:0000269|PubMed:10196317"
FT MUTAGEN 42
FT /note="S->G: About 95% loss of phosphorylation by host
FT CDK2."
FT /evidence="ECO:0000269|PubMed:10196317"
SQ SEQUENCE 339 AA; 37224 MW; D2B1E34450B8463A CRC64;
MSQEPEPGAM PYSPADDPSP LDLSLGSTSR RKKRKSHDIP NSPSKHPFPD GLSEEEKQKL
ERRRKRNRDA ARRRRRKQTD YVDKLHEACE ELQRANEHLR KEIRDLRTEC TSLRVQLACH
EPVCPMAVPL TVTLGLLTTP HDPVPEPPIC TPPPPSPDEP NAPHCSGSQP PICTPPPPDT
EELCAQLCST PPPPISTPHI IYAPGPSPLQ PPICTPAPPD AEELCAQLCS TPPPPICTPH
SLFCPPQPPS PEGIFPALCP VTEPCTPPSP GTVYAQLCPV GQVPLFTPSP PHPAPEPERL
YARLTEDPEQ DSLYSGQIYT QFPSDTQSTV WWFPGDGRP
