ID   PP65_HCMVT              Reviewed;         551 AA.
AC   P18139;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=65 kDa phosphoprotein;
DE            Short=pp65;
DE   AltName: Full=64 kDa matrix phosphoprotein;
DE            Short=pp64;
DE   AltName: Full=GP64;
DE   AltName: Full=Phosphoprotein UL83;
DE   AltName: Full=Tegument protein UL83;
GN   Name=UL83;
OS   Human cytomegalovirus (strain Towne) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=10363;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1850902; DOI=10.1016/0042-6822(91)90665-x;
RA   Pande H., Campo K., Tanamachi B., Zaia J.A.;
RT   "Human cytomegalovirus strain Towne pp65 gene: nucleotide sequence and
RT   expression in Escherichia coli.";
RL   Virology 182:220-228(1991).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-462.
RX   PubMed=2167561; DOI=10.1016/0042-6822(90)90374-z;
RA   Pande H., Lee T.D., Churchill M.A., Zaia J.A.;
RT   "Structural analysis of a 64-kDa major structural protein of human
RT   cytomegalovirus (Towne): identification of a phosphorylation site and
RT   comparison to pp65 of HCMV (AD169).";
RL   Virology 178:6-14(1990).
CC   -!- FUNCTION: Counteracts the host antiviral immune response when activated
CC       and phosphorylated, by preventing host IRF3 from entering the nucleus.
CC       Inhibits also the type I interferon production by inactivating the
CC       enzymatic activity of DNA sensor CGAS without affecting STING1.
CC       Participates in the transactivation of viral major immediate-early
CC       genes by the recruitment of host IFI16 to the promoters pf these genes.
CC       {ECO:0000250|UniProtKB:P06725}.
CC   -!- SUBUNIT: Interacts with host NCL/nucleolin. Interacts with host IFI16.
CC       Interacts with host CGAS; this interaction inhibits CGAS enzymatic
CC       activity. {ECO:0000250|UniProtKB:P06725}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P06725}.
CC       Host nucleus {ECO:0000250|UniProtKB:P06725}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P06725}. Note=As part of the incoming virion,
CC       pp65 is targeted to the nucleus immediately after infection. The newly
CC       synthesized pp65 is observed in the nucleus until some time after 48
CC       hours postinfection. Thereafter, pp65 is probably exported and
CC       accumulates in the cytoplasm. Also found in dense bodies.
CC       {ECO:0000250|UniProtKB:P06725}.
CC   -!- PTM: Phosphorylation may play a role in the localization of the
CC       protein. {ECO:0000250|UniProtKB:P06725}.
CC   -!- SIMILARITY: Belongs to the herpesviridae UL82 family. {ECO:0000305}.
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DR   EMBL; M67443; AAA45994.1; -; Genomic_DNA.
DR   PDB; 3BW9; X-ray; 1.75 A; C=93-104.
DR   PDB; 3BWA; X-ray; 1.30 A; C=178-185.
DR   PDB; 4QRR; X-ray; 3.00 A; P=113-121.
DR   PDB; 5D2L; X-ray; 3.51 A; Q/R/T/U=485-493.
DR   PDB; 5D2N; X-ray; 2.10 A; G/I=485-493.
DR   PDBsum; 3BW9; -.
DR   PDBsum; 3BWA; -.
DR   PDBsum; 4QRR; -.
DR   PDBsum; 5D2L; -.
DR   PDBsum; 5D2N; -.
DR   SMR; P18139; -.
DR   IntAct; P18139; 1.
DR   iPTMnet; P18139; -.
DR   EvolutionaryTrace; P18139; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR008649; Herpes_UL82/UL83.
DR   Pfam; PF05784; Herpes_UL82_83; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Host cytoplasm; Host nucleus;
KW   Phosphoprotein; Viral matrix protein; Virion; Virion tegument.
FT   CHAIN           1..551
FT                   /note="65 kDa phosphoprotein"
FT                   /id="PRO_0000116293"
FT   REGION          379..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         462
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:2167561"
FT   HELIX           99..102
FT                   /evidence="ECO:0007829|PDB:3BW9"
SQ   SEQUENCE   551 AA;  61638 MW;  C56D11AEB01F3C23 CRC64;
     MASVLGPISG HVLKAVFSRG DTPVLPHETR LLQTGIHVRV SQPSLILVSQ YTPDSTPCHR
     GDNQLQVQHT YFTGSEVENV SVNVHNPTGR SICPSQEPMS IYVYALPLKM LNIPSINVHH
     YPSAAERKHR HLPVADAVIH ASGKQMWQAR LTVSGLAWTR QQNQWKEPDV YYTSAFVFPT
     KDVALRHVVC AHELVCSMEN TRATKMQVIG DQYVKVYLES FCEDVPSGKL FMHVTLGSDV
     EEDLTMTRNP QPFMRPHERN GFTVLCPKNM IIKPGKISHI MLDVAFTSHE HFGLLCPKSI
     PGLSISGNLL MNGQQIFLEV QAIRETVELR QYDPVAALFF FDIDLLLQRG PQYSEHPTFT
     SQYRIQGKLE YRHTWDRHDE GAAQGDDDVW TSGSDSDEEL VTTERKTPRV TGGGAMAGAS
     TSAGRKRKSA SSATACTAGV MTRGRLKAES TVAPEEDTDE DSDNEIHNPA VFTWPPWQAG
     ILARNLVPMV ATVQGQNLKY QEFFWDANDI YRIFAELEGV WQPAAQPKRR RHRQDALPGP
     CIASTPKKHR G