ID   SHUT_ADE41              Reviewed;         777 AA.
AC   P11824;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   03-AUG-2022, entry version 68.
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 F serotype 41 (HAdV-41) (Human adenovirus 41).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX   NCBI_TaxID=10524;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tak;
RX   PubMed=2349115; DOI=10.1093/nar/18.10.3069;
RA   Slemenda S.B., Pieniazek N.J., Velarde J. Jr., Pieniazek D., Luftig R.B.;
RT   "Nucleotide sequence of the region coding for 100K and 33K proteins of
RT   human enteric adenovirus type 41 (Tak).";
RL   Nucleic Acids Res. 18:3069-3069(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-651.
RX   PubMed=3279700; DOI=10.1016/0042-6822(88)90227-9;
RA   Vos H.L., der Lee F.M., Reemst A.M.C.B., van Loon A.E., Sussenbach J.S.;
RT   "The genes encoding the DNA binding protein and the 23K protease of
RT   adenovirus types 40 and 41.";
RL   Virology 163:1-10(1988).
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; X52532; CAA36760.1; -; Genomic_DNA.
DR   EMBL; M21163; AAA42464.1; -; Genomic_DNA.
DR   PIR; S10207; WMAD41.
DR   PRIDE; P11824; -.
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..777
FT                   /note="Shutoff protein"
FT                   /id="PRO_0000221859"
FT   DOMAIN          317..435
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..314
FT                   /note="Binding to host EIF4G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT   REGION          261..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         334
FT                   /note="Phosphotyrosine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT   MOD_RES         649
FT                   /note="Phosphotyrosine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
SQ   SEQUENCE   777 AA;  87309 MW;  BCA13832FAC1AFAA CRC64;
     MEEDLIQPQP DSETLTSPTS EVGAVELVEH EDDERVEQDP GYVTPPKDGK ESVPVSPLTE
     ADYLGGEDDV LLKHVLRQST IVQEAFKDYS GFPLTVEELS RTYEANLFSP RVPPKKQANG
     TCEPNPRLNF YPVFAVPEAL ATYHIFFKNQ RIPLSCRANR TQGDRILHLK AGAHIPEIVS
     LEEVPKIFEG LGKDEKRAAN ALQKSETENQ NVLVELDGDN ARLAVLKRTI EVSHFAYPAL
     NLPPKVMRSV MDHLLIKRVE PLDSDQPEQN SEDGQPVVSD DDLARWLDSH DPTTLQERRK
     MMMAVILVTV ELECLQRFFA NPQTLRKIEE SLHYAFRHGY VRQACKISNV ELSNLVSYMG
     ILHENRLGQN VLHCTLQGEA RRDYVRDCIY LFLILTWQTA MGVWQQCLEE RNLRELEKLL
     VRNRRELWTA FSERTAACQL ADLIFPERLM QTLQNGLPDF VSQSILQNFR SFILERSGIL
     PAMSCALPSD FVPLCYRECP PPLWSHCYLL RLANYLAHHS DLMENSSGEG LLECHCRCNL
     CTPHRSLVCN TELLSETQVI GTFEIQGPER QEGASNLKLT PALWTSAYLR KFIPEDYHAH
     QIKFYEDQSR PPKAPLTACV ITQSQILAQL QAIQQARQEF LLKKGHGVYL DPQTGEELNT
     PSPSAAASCR PQKHAAQREQ ASHCGSAVPK ATETARAVGR GGGILGRQPG RGSFRRGGNG
     ELGKSRRGAG GQTPQGRGGR NHRQRRGTVF QRTRSEPASD GESRTVPAAA RLVESQP