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Database: UniProt
Entry: UL42_HCMVA
LinkDB: UL42_HCMVA
Original site: UL42_HCMVA 
ID   UL42_HCMVA              Reviewed;         125 AA.
AC   P16815; Q7M6F8;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Protein UL42;
GN   Name=UL42;
OS   Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=10360;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA   Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA   Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA   Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT   "Analysis of the protein-coding content of the sequence of human
RT   cytomegalovirus strain AD169.";
RL   Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX   PubMed=9371656; DOI=10.1128/jvi.71.12.9833-9836.1997;
RA   Dargan D.J., Jamieson F.E., Maclean J., Dolan A., Addison C., McGeoch D.J.;
RT   "The published DNA sequence of human cytomegalovirus strain AD169 lacks 929
RT   base pairs of DNA affecting genes UL42 and UL43.";
RL   J. Virol. 71:9833-9836(1997).
RN   [3]
RP   GENOME REANNOTATION.
RX   PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA   Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA   McGeoch D.J., Hayward G.S.;
RT   "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT   cytomegalovirus genome.";
RL   J. Gen. Virol. 84:17-28(2003).
RN   [4]
RP   ERRATUM OF PUBMED:12533697.
RA   Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA   McGeoch D.J., Hayward G.S.;
RL   J. Virol. 78:13395-13395(2004).
RN   [5]
RP   FUNCTION, INTERACTION WITH HOST STING1 AND CGAS, AND SUBCELLULAR LOCATION.
RX   PubMed=31107917; DOI=10.1371/journal.ppat.1007691;
RA   Fu Y.Z., Guo Y., Zou H.M., Su S., Wang S.Y., Yang Q., Luo M.H., Wang Y.Y.;
RT   "Human cytomegalovirus protein UL42 antagonizes cGAS/MITA-mediated innate
RT   antiviral response.";
RL   PLoS Pathog. 15:e1007691-e1007691(2019).
CC   -!- FUNCTION: Plays a role in the inhibition of host innate immune response
CC       to promote latent infection (PubMed:31107917). Mechanistically,
CC       suppresses viral DNA-triggered signaling by impairing DNA binding and
CC       oligomerization of CGAS. Impairs also the translocation of host STING1
CC       from the endoplasmic reticulum to perinuclear punctate structures which
CC       is an essential step for its activation (PubMed:31107917). Regulates
CC       the function of host NEDD4 family ubiquitin E3 ligases through its PPxY
CC       motif and thereby prevents the excessive ubiquitination of gB and its
CC       degradation by inhibiting these E3 ligases (By similarity).
CC       {ECO:0000250|UniProtKB:D5LX53, ECO:0000269|PubMed:31107917}.
CC   -!- SUBUNIT: Interacts with host ITCH; this interaction induces the
CC       ubiquitination and subsequent degradation of ITCH. Interacts with host
CC       STING1 (PubMed:31107917). Interacts with CGAS (PubMed:31107917).
CC       {ECO:0000250|UniProtKB:F5HHZ3, ECO:0000269|PubMed:31107917}.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000250|UniProtKB:F5HHZ3};
CC       Single-pass membrane protein {ECO:0000250|UniProtKB:F5HHZ3}. Host
CC       cytoplasm {ECO:0000269|PubMed:31107917}. Note=Accumulates in the
CC       perinuclear region of the host cytoplasm, with some dispersal into the
CC       cytoplasm in a fine-speckled pattern. {ECO:0000250|UniProtKB:F5HHZ3}.
CC   -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC       essential for viral particle budding. They recruit proteins of the host
CC       ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC       ESCRT-associated proteins. Contains two L domains: PPXY motifs which
CC       are involved in the interaction with ITCH, a member of the NEDD4
CC       family. {ECO:0000250|UniProtKB:D5LX53}.
CC   -!- SIMILARITY: Belongs to the Cytomegalovirus UL42 protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA35401.1; Type=Miscellaneous discrepancy; Note=Internal deletion.; Evidence={ECO:0000305};
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DR   EMBL; X17403; CAA35401.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; Y13735; CAA74074.1; -; Genomic_DNA.
DR   EMBL; BK000394; DAA00234.1; -; Genomic_DNA.
DR   PIR; S09805; S09805.
DR   RefSeq; YP_081500.1; NC_006273.2.
DR   SMR; P16815; -.
DR   BioGRID; 1677993; 1.
DR   DNASU; 3077440; -.
DR   GeneID; 3077440; -.
DR   KEGG; vg:3077440; -.
DR   Proteomes; UP000008991; Genome.
DR   Proteomes; UP000008992; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR035110; UL42.
DR   Pfam; PF17638; UL42; 1.
PE   1: Evidence at protein level;
KW   Host cytoplasm; Host membrane; Host-virus interaction;
KW   Inhibition of host innate immune response by virus; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix;
KW   Viral immunoevasion.
FT   CHAIN           1..125
FT                   /note="Protein UL42"
FT                   /id="PRO_0000115325"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           16..19
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:D5LX53"
FT   MOTIF           42..45
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:D5LX53"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..47
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   125 AA;  13668 MW;  79870B50807CCB66 CRC64;
     MEPTPMLRDR DHDDAPPTYE QAMGLCPTTV STPPPPPPDC SPPPYRPPYC LVSSPSPRHT
     FDMDMMEMPA TMHPTTGAYF DNGWKWTFAL LVVAILGIIF LAVVFTVVIN RDSANITTGT
     QASSG
//
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