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 02-JUN-2021, entry version 65.
DE RecName: Full=Shutoff protein {ECO:0000255|HAMAP-Rule:MF_04060};
DE AltName: Full=100 kDa protein {ECO:0000255|HAMAP-Rule:MF_04060};
DE Short=p100K {ECO:0000255|HAMAP-Rule:MF_04060};
DE AltName: Full=100K-chaperone protein {ECO:0000255|HAMAP-Rule:MF_04060};
DE AltName: Full=L4-100K {ECO:0000255|HAMAP-Rule:MF_04060};
DE AltName: Full=Shutoff protein 100K {ECO:0000255|HAMAP-Rule:MF_04060};
GN Name=L4 {ECO:0000255|HAMAP-Rule:MF_04060};
OS Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; 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; DOI=10.1128/jvi.68.1.379-389.1994;
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 late
CC viral translation by ribosome shunting. Blocks host cap-dependent
CC translation by binding to eIF4G, displacing MKNK1 from cap initiation
CC complexes and preventing EIF4E phosphorylation. Binds to the tripartite
CC leader sequence of viral late mRNAs and recruits host eIF4G,
CC PABPC1/poly-A binding protein and 40S ribosomes subunits on viral
CC mRNAs, allowing ribosome shunting and efficient translation of late
CC viral mRNAs even though conventional translation via ribosome scanning
CC from the cap has been shut off in the host cell. During assembly, acts
CC as a chaperone protein that helps hexon proteins assembly into trimers.
CC {ECO:0000255|HAMAP-Rule:MF_04060}.
CC -!- SUBUNIT: Monomer. Interacts with hexon protein; this interaction allows
CC chaperoning and trimerization of hexon proteins. Interacts (via N-
CC terminus) with host initiation factor EIF4G (via C-terminus). Interacts
CC (via RRM domain) with viral mRNAs that contain the tripartite leader;
CC this interaction allows ribosome shunting and expression of viral late
CC mRNAs. {ECO:0000255|HAMAP-Rule:MF_04060}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04060}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04060}.
CC -!- PTM: Might be cleaved by the viral protease. {ECO:0000255|HAMAP-
CC Rule:MF_04060}.
CC -!- PTM: Phosphorylated. Tyrosine phosphorylation enhances preferential
CC binding to tripartite leader mRNAs and allows ribosome shunting.
CC {ECO:0000255|HAMAP-Rule:MF_04060}.
CC -!- PTM: Methylated. Asymmetric dimethylation by host PRMT1 of the Arg/Gly-
CC rich region may regulate shutoff protein binding to hexon and promote
CC the capsid assembly in the nucleus. {ECO:0000255|HAMAP-Rule:MF_04060}.
CC -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC are produced by alternative splicing and alternative polyadenylation of
CC the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC present in the N-terminus of all these mRNAs and is recognized by the
CC viral shutoff protein to provide expression although conventional
CC translation via ribosome scanning from the cap has been shut off in the
CC host cell. {ECO:0000255|HAMAP-Rule:MF_04060}.
CC -!- SIMILARITY: Belongs to the adenoviridae shutoff protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04060}.
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DR EMBL; X73487; CAA51894.1; -; Genomic_DNA.
DR PIR; S33945; S33945.
DR RefSeq; NP_040927.1; NC_001460.1.
DR DNASU; 1460842; -.
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-UniRule.
DR GO; GO:0019060; P:intracellular transport of viral protein in host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-UniRule.
DR GO; GO:0039704; P:viral translational shunt; ISS:UniProtKB.
DR HAMAP; MF_04060; ADV_SHUT; 1.
DR InterPro; IPR003381; L4.
DR Pfam; PF02438; Adeno_100; 1.
PE 3: Inferred from homology;
KW Chaperone; 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; Late protein;
KW Methylation; Phosphoprotein; RNA-binding; Translational shunt; Transport.
FT CHAIN 1..782
FT /note="Shutoff protein"
FT /id="PRO_0000221857"
FT DOMAIN 332..450
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 262..329
FT /note="Binding to host EIF4G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 715..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT MOD_RES 665
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
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
