ID   PP71_HCMVM              Reviewed;         559 AA.
AC   F5HBC6;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Protein pp71;
GN   Name=UL82;
OS   Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=295027;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA   Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA   Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA   Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT   "Genetic content of wild-type human cytomegalovirus.";
RL   J. Gen. Virol. 85:1301-1312(2004).
CC   -!- FUNCTION: Stimulates viral immediate-early (IE) transcription. Plays a
CC       role in the inhibition of the host innate repsonse by targeting STING1
CC       and thus the cGAS-STING pathway. Counteracts also host DAXX-mediated
CC       repression of viral transcription. Displaces a DAXX-binding protein,
CC       ATRX, from nuclear domain 10 sites (ND10) shortly after infection.
CC       Increases the basal level of SUMOylated DAXX in infected cells.
CC       Stimulates quiescent cells to re-enter the cell cycle, proceed through
CC       G1 and enter the S phase. Interacts with hypophosphorylated forms of
CC       RB1 and induces their degradation by the proteasome without involving
CC       ubiquitin conjugation. {ECO:0000250|UniProtKB:P06726}.
CC   -!- SUBUNIT: Interacts with the host protein DAXX; this interaction takes
CC       place at ND10 and induces the reversal of DAXX-mediated repression of
CC       viral transcription. Interacts with UL35. Interacts with host
CC       TMEM173/STING1; this interaction inhibits the cGAS/STING pathway.
CC       Interacts with host RB1; this interaction mediates RB1 proteasomal
CC       degradation. {ECO:0000250|UniProtKB:P06726}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P06726}.
CC       Host nucleus {ECO:0000250|UniProtKB:P06726}. Host endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P06726}. Note=Present in the nucleus shortly
CC       after infection as well as during the late phase of viral
CC       morphogenesis. Detected at nuclear domain 10 (ND10).
CC       {ECO:0000250|UniProtKB:P06726}.
CC   -!- PTM: S-nitrosylation limits ability to undermine the cGAS/STING
CC       antiviral pathway. {ECO:0000250|UniProtKB:P06726}.
CC   -!- SIMILARITY: Belongs to the herpesviridae pp71 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY446894; AAR31634.1; -; Genomic_DNA.
DR   RefSeq; YP_081530.1; NC_006273.2.
DR   BioGRID; 1678083; 2.
DR   PRIDE; F5HBC6; -.
DR   GeneID; 3077530; -.
DR   KEGG; vg:3077530; -.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Reactome; R-HSA-9610379; HCMV Late Events.
DR   Proteomes; UP000000938; Genome.
DR   GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
DR   GO; GO:0019033; C:viral tegument; TAS:Reactome.
DR   GO; GO:0039695; P:DNA-templated viral transcription; ISS:UniProtKB.
DR   GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   InterPro; IPR008649; Herpes_UL82/UL83.
DR   Pfam; PF05784; Herpes_UL82_83; 1.
PE   3: Inferred from homology;
KW   Activator; G1/S host cell cycle checkpoint dysregulation by virus;
KW   Host endoplasmic reticulum; Host nucleus; Host-virus interaction;
KW   Modulation of host cell cycle by virus; Phosphoprotein; Reference proteome;
KW   S-nitrosylation; Virion; Virion tegument.
FT   CHAIN           1..559
FT                   /note="Protein pp71"
FT                   /id="PRO_0000418269"
FT   REGION          404..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..431
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         218
FT                   /note="S-nitrosocysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P06726"
FT   MOD_RES         223
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P06726"
SQ   SEQUENCE   559 AA;  62008 MW;  C79469D33130265B CRC64;
     MSQASSSPGE GPSSEAAAIS EAEAASGSFG RLHCQVLRLI TNVEGGSLEA GRLRLLDLRT
     NIEVSRPSVL CCFQENKSPH DTVDLTDLNI KGRCVVGEQD RLLVDLNNFG PRRLTPGSEN
     NTVSVLAFAL PLDRVPVSGL HLFQSQRRGG EENRPRMEAR AIIRRTAHHW AVRLTVTPNW
     RRRTDSSLEA GQIFVSQFAF RAGAIPLTLV DALEQLACSD PNTYIHKTET DERGQWIMLF
     LHHDSPHPPT SVFLHFSVYT HRAEVVARHN PYPHLRRLPD NGFQLLIPKS FTLTRIHPEY
     IVQIQNAFET NQTHDTIFFP ENIPGVSIEA GPLPDRVRIT LRVTLTGDQA VHLEHRQPLG
     RIHFFRRGFW TLTPGKPDKI KRPQVQLRAG LFPRSNVMRG AVSEFLPQSP GLPPTEEEEE
     EEEEDDEDDL SSTPTPTPLS EAMFAGFEEA SGDEDSDTQA GLSRALILTG QRRRSGNNGA
     LTLVIPSWHV FASLDDLVPL TVSVQHAALR PTSYLRSDMD GDVRTAADIS STLRSVPAPR
     PSPISTASTS STPRSRPRI