SHUT_HHV2H
ID SHUT_HHV2H Reviewed; 492 AA.
AC P68340; P36699;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Virion host shutoff protein;
DE Short=Vhs;
DE EC=3.1.27.-;
GN Name=UL41;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
CC -!- FUNCTION: Minor structural protein that acts as an endoribonuclease
CC during lytic infection. Degrades host mRNAs in the cytoplasm by cutting
CC them at preferred sites, including some in regions of translation
CC initiation. Together with inhibition of host splicing by ICP27,
CC contributes to an overall decrease in host protein synthesis. Also,
CC after the onset of viral transcription, accelerates the turnover of
CC viral mRNA, thereby facilitating the sequential expression of different
CC classes of viral genes. Binds translation initiation factors eIF4H,
CC eIF4AI, and eIF4AII, thereby may interact directly with the translation
CC initiation complex and thus digest specifically mRNAs. Also impedes
CC antigen presentation by major histocompatibility complex class I and
CC class II molecules, inhibits secretion of cytokines that would
CC otherwise recruit lymphocytes and neutrophils cells to the site of
CC infection and blocks the activation of dendritic cells. Impedes the
CC alpha/beta interferon-mediated response to infection (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with human EIF4H, EIF4A1 and EIF4A2; interaction
CC with eIF4AI and EIF4A2 presumably allows Vhs protein to associate with
CC the eIF4F cap-binding complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the herpesviridae VHS protein family.
CC {ECO:0000305}.
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DR EMBL; Z86099; CAB06727.1; -; Genomic_DNA.
DR RefSeq; YP_009137193.1; NC_001798.2.
DR PRIDE; P68340; -.
DR DNASU; 1487328; -.
DR GeneID; 1487328; -.
DR KEGG; vg:1487328; -.
DR Proteomes; UP000001874; Genome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR Pfam; PF00867; XPG_I; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 3: Inferred from homology;
KW Decay of host mRNAs by virus; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Host gene expression shutoff by virus; Host mRNA suppression by virus;
KW Host-virus interaction; Hydrolase; Interferon antiviral system evasion;
KW Late protein; Nuclease; Reference proteome; RNA-binding;
KW Viral immunoevasion; Virion.
FT CHAIN 1..492
FT /note="Virion host shutoff protein"
FT /id="PRO_0000116056"
FT REGION 110..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 55244 MW; 56B062B3088B439F CRC64;
MGLFGMMKFA QTHHLVKRRG LRAPEGYFTP IAVDLWNVMY TLVVKYQRRY PSYDREAITL
HCLCSMLRVF TQKSLFPIFV TDRGVECTEP VVFGAKAILA RTTAQCRTDE EASDVDASPP
PSPITDSRPS FAFSNMRRRG HAFAPGDRGT RAAGPGPAAP SGAPSKPALR LAHLFCIRVL
RALGYAYINS GQLEADDACA NLYHTNTVAY VHTTDTDLLL MGCDIVLDIS TGYIPTIHCR
DLLQYFKMSY PQFLALFVRC HTDLHPNNTY ASVEDVLREC HWTAPSRSQA RRAARRERAN
SRSLESMPTL TAAPVGLETR ISWTEILAQQ IAGEDDYEED PPLQPPDVAG GPRDGARSSS
SEILTPPELV QVPNAQRVAE HRGYVAGRRR HVIHDAPEAL DWLPDPMTIA ELVEHRYVKY
VISLISPKER GPWTLLKRLP IYQDLRDEDL ARSIVTRHIT APDIADRFLA QLWAHAPPPA
FYKDVLAKFW DE