ID   SHUT_ADEP3              Reviewed;         838 AA.
AC   Q9YTR7;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 67.
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   Porcine adenovirus A serotype 3 (PAdV-3) (Porcine adenovirus 3).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Porcine mastadenovirus A.
OX   NCBI_TaxID=35265;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=6618;
RX   PubMed=9837805; DOI=10.1006/viro.1998.9418;
RA   Reddy P.S., Idamakanti N., Song J.Y., Lee J.B., Hyun B.H., Park J.H.,
RA   Cha S.H., Bae Y.T., Tikoo S.K., Babiuk L.A.;
RT   "Nucleotide sequence and transcription map of porcine adenovirus type 3.";
RL   Virology 251:414-426(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6618 / IAF;
RA   Larocque D., Malenfant F., Massie B., Dea S.;
RT   "Porcine adenovirus serotype 3, complete genome.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF083132; AAC99445.1; -; Genomic_DNA.
DR   EMBL; AJ237815; CAB41033.1; -; Genomic_DNA.
DR   EMBL; AB026117; BAA76971.1; -; Genomic_DNA.
DR   RefSeq; YP_009213.1; AC_000189.1.
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..838
FT                   /note="Shutoff protein"
FT                   /id="PRO_0000221864"
FT   DOMAIN          356..474
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..353
FT                   /note="Binding to host EIF4G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT   REGION          693..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..36
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..785
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         373
FT                   /note="Phosphotyrosine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT   MOD_RES         690
FT                   /note="Phosphotyrosine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
SQ   SEQUENCE   838 AA;  94103 MW;  D7EE710DE03F5065 CRC64;
     MEDQHSAASE LGSSAAPTLP PPPPPPPPPT SPPPSLQQRQ QEPTETDDAE DTCSSSSSSS
     ASSECFVSPL EDTSSEDSAD TVLPSEPRRD EEEQEEDSPD RYMDADVLQR HLLRQSTILR
     QVLQEAAPGA AAEAAEAPSV AELSRRLEAA LFSPATPPRR QENGTCAPDP RLNFYPVFML
     PEALATYLLF FHNQKIPVSC RANRPRADAH WRLPSGTPLP DYPTTDEVYK IFEGLGDEEP
     ACANQDLKER DSVLVELKLD NPRLAVVKQC IAVTHFAYPA LALPPKVMST LMQTLLVRRA
     SPLPDEGETP LEDLLVVSDE QLARWMHTSD PKVLEERRKT VTAACMVTVQ LHCMHTFLTS
     REMVRRLGEC LHYMFRQGYV KLASKIANME LSNLVSYLGM LHENRLGQHV LHHTLKHEAR
     RDYVRDTIYL YLVYTWQTAM GVWQQCLEDR NLRALETSLA RARQSLWTGF DERTIAQDLA
     AFLFPTKLVE TLQRSLPDFA SQSMMHAFRS FVLERSGILP AVCNALPSDF VPTVYRECPP
     PLWAHCYLLR LANFLMYHCD LAEDTSGEGL FECYCRCNLC APHRCLATNT ALLNEVQAIN
     TFELQRPPKP DGTLPPPFKL TPGLWTSAFL RHFVSEDYHS DRILFYEDVS RPPRVEPSAC
     VITHSAILAQ LHDIKKAREE FLLTKGHGVY LDPHTGEELN TAAPSTAHHA APPEEAHPQQ
     HQHQQQPSHR RRHHRSSYAD RVRSELHAYG GATGSSRDPV SGGCSARGTH SRDAARRRGS
     QQRDQRQLRR QFAQYPRGTG GGGGTGHTDE AIQALLHQQQ QQQEHQPAQE LRRPQRGS