Entry sw:SHUT_ADE12

ID   SHUT_ADE12              Reviewed;         782 AA.
AC   P36714;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   30-NOV-2016, entry version 50.
DE   RecName: Full=Shutoff protein;
DE   AltName: Full=100 kDa protein;
DE            Short=p100K;
DE   AltName: Full=100K-chaperone protein;
DE   AltName: Full=L4-100K;
DE   AltName: Full=Shutoff protein 100K;
GN   ORFNames=L4;
OS   Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12).
OC   Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus;
OC   Human mastadenovirus A.
OX   NCBI_TaxID=28282;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8254750;
RA   Sprengel J., Schmitz B., Heuss-Neitzel D., Zock C., Doerfler W.;
RT   "Nucleotide sequence of human adenovirus type 12 DNA: comparative
RT   functional analysis.";
RL   J. Virol. 68:379-389(1994).
CC   -!- FUNCTION: Protein that inhibits host translation while promoting
CC       late viral translation by ribosome shunting. Blocks host cap-
CC       dependent translation by binding to eIF4G, displacing MKNK1 from
CC       cap initiation complexes and preventing EIF4E phosphorylation.
CC       Binds to the tripartite leader sequence of viral late mRNAs and
CC       recruits host eIF4G, PABPC1/poly-A binding protein and 40S
CC       ribosomes subunits on viral mRNAs, allowing ribosome shunting and
CC       efficient translation of late viral mRNAs even though conventional
CC       translation via ribosome scanning from the cap has been shut off
CC       in the host cell. During assembly, acts as a chaperone protein
CC       that helps hexon proteins assembly into trimers (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with hexon protein;
CC       this interaction allows chaperoning and trimerization of hexon
CC       proteins. Interacts (via N-terminus) with host initiation factor
CC       EIF4G (via C-terminus). Interacts (via RRM domain) with viral
CC       mRNAs that contain the tripartite leader; this interaction allows
CC       ribosome shunting and expression of viral late mRNAs (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative
CC       cycle.
CC   -!- PTM: Phosphorylated. Tyrosine phosphorylation enhances
CC       preferential binding to tripartite leader mRNAs and allows
CC       ribosome shunting (By similarity). {ECO:0000250}.
CC   -!- PTM: Methylated. Asymmetric dimethylation by host PRMT1 of the
CC       Arg/Gly-rich region may regulate shutoff protein binding to hexon
CC       and promote the capsid assembly in the nucleus.
CC   -!- PTM: Might be cleaved by the viral protease. {ECO:0000250}.
CC   -!- MISCELLANEOUS: All late proteins expressed from the major late
CC       promoter are produced by alternative splicing and alternative
CC       polyadenylation of the same gene giving rise to non-overlapping
CC       ORFs. A leader sequence is present in the N-terminus of all these
CC       mRNAs and is recognized by the viral shutoff protein to provide
CC       expression although conventional translation via ribosome scanning
CC       from the cap has been shut off in the host cell (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenoviridae shutoff protein family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC       {ECO:0000305}.
DR   EMBL; X73487; CAA51894.1; -; Genomic_DNA.
DR   PIR; S33945; S33945.
DR   RefSeq; NP_040927.1; NC_001460.1.
DR   GeneID; 1460842; -.
DR   KEGG; vg:1460842; -.
DR   Proteomes; UP000004993; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019060; P:intracellular transport of viral protein in host cell; IEA:InterPro.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0039704; P:viral translational shunt; ISS:UniProtKB.
DR   InterPro; IPR003381; Adeno_100.
DR   Pfam; PF02438; Adeno_100; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Complete proteome;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus; Host cytoplasm;
KW   Host gene expression shutoff by virus; Host-virus interaction;
KW   Inhibition of eukaryotic host translation factors by virus;
KW   Late protein; Methylation; Phosphoprotein; Reference proteome;
KW   RNA-binding; Translational shunt; Transport.
FT   CHAIN         1    782       Shutoff protein.
FT                                /FTId=PRO_0000221857.
FT   DOMAIN      332    450       RRM.
FT   REGION      262    329       Binding to host EIF4G. {ECO:0000250}.
FT   COMPBIAS    717    756       Arg/Gly-rich.
FT   MOD_RES     349    349       Phosphotyrosine; by host. {ECO:0000250}.
FT   MOD_RES     665    665       Phosphotyrosine; by host. {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        80    675       ipfam:Adeno_100 [T]
SQ   SEQUENCE   782 AA;  87683 MW;  A66BC65CE3A33AB0 CRC64;
     MMDLEPQESL TAPTAPAIGA TAVMEKDKSL LIPQDAPVEQ NLGYETPPEE FEGFLQIQKQ
     PNEQNAGLED HDYLNEGDVL FKHLQRQSTI VRDAISDRSS IPVSIAELSC IYERNLFSPR
     VPPKRQANGT CEPNPRLNFY PVFAVPEALA TYHIFFKNHK IPLSCRANRS RADELLALRA
     GASIPGIVSL EEVPKIFEGL GRDEKRAANA LQKENEQNHH GNSALIELEG DNARLAVLKR
     NIEVTHFAYP AVNLPPKVMS AVMNQLLIKR AQPIDKDANL QDPEATDDGK PVVSDEQLTK
     WLGTDNSNEL QQRRKLMMAA VLVTVELECM HRFFSDITTL RKIEECLHYT FRHGYVRQAC
     KISNVELSNL VSYMGILHEN RLGQNVLHST LRDEARRDYV RDCIYLFLLH TWQTGMGVWQ
     QCLEEKNLRE LNKLLDRALK SLWTGFDERT VAAELADIIF PERLMITLQN GLPDFMSQSM
     LHNYRSFILE RSGMLPSMCC ALPSDFVPIY FRECPPPLWS HCYLLRLANY LAYHSDLMTD
     SSGEGLMECH CRCNLCTPHR SLVCNTELLS ESQVIGTFEM QGPQSDSNFT TNLRLTPGLW
     TSAYLRKFEP QDYHAHSINF YEDQSKPPKA PLTACVITQG KILAQLHAIK QAREEFLLKK
     GHGVYLDPQT GEELNLPSPL CATASPHSQH VPESRKTGYC AATLKETAAT AGNLGGRILG
     ESGRGRGRGL GRMGGGGGGQ PRRGSRGGGG RFQGRSDRRQ TVAFNQALSN ETRCEQISES
     QP
//