SHUT_ADEG1
ID SHUT_ADEG1 Reviewed; 984 AA.
AC Q64760;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, 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 Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian
OS adenovirus gal1 (strain Phelps)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus A.
OX NCBI_TaxID=10553;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8627769; DOI=10.1128/jvi.70.5.2939-2949.1996;
RA Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.;
RT "The complete DNA sequence and genomic organization of the avian adenovirus
RT CELO.";
RL J. Virol. 70:2939-2949(1996).
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; U46933; AAC54915.1; -; Genomic_DNA.
DR RefSeq; NP_043889.1; NC_001720.1.
DR GeneID; 1476563; -.
DR KEGG; vg:1476563; -.
DR Proteomes; UP000001594; 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; Reference proteome; RNA-binding;
KW Translational shunt; Transport.
FT CHAIN 1..984
FT /note="Shutoff protein"
FT /id="PRO_0000221862"
FT DOMAIN 479..597
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 131..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..476
FT /note="Binding to host EIF4G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 810..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 812
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
SQ SEQUENCE 984 AA; 109912 MW; 55A8E2F47496D97D CRC64;
MADKITREEK TIATLDLVLR VVVDAGNWDV FSKRLVRYTR EQYGIELPED IGDLPDTSEV
SKVLLSHLGE DKAVLSAYRI AELTQPSEMD RAKVTEGGLA VLNASRDESE AQNPSNPEPE
SIESDAVEDL GVAAESDPSD DEPDPEPEYD HREADHDSDA DSGYYSADGG RPGTPVDEEP
QDDSPSSEET ASTVIEEAQT SASNDSHDDD THRDDGSASE EDLERDALVA PADPFPNLRK
CFERQAMMLT GALKDAADTA DPPETLSVDS VQRQLERFVF NPDRRVPAEH LEVRYNFYPP
FLTPKAIASY HIFAVTASIP LSCKANRSGS DLLAKAKEST FFKRLPKWRL GIEIDDGLGT
EVTAVTELEE AKMVPLKDDV SRLQWAKMRG EHIRFFSYPS LHMPPKISRM LMETLLQPFA
DENQKAEEAL PCLSDEEVLA IVDPTGRLHG EDALKAVEKR RAAVTMAVRY TATLELMERV
FREPSMVKKM QEVLHHTFHH GFVALVRETA KVNLSNYATF HGLTYNNPLN NCIMSKLLEG
ADKEDYVVDS IYLFLVLTWQ TAMGMWQQAI DDMTIQMYTE VFTKNKYRLY SLPNPTAIGK
AIVDILMDYD RLTEEMRKAL PNFTCQSQIT AFRHFLLERS NIPAVAAPFM PSDFVPLAYK
QSPPLLWDQV YLLQLAFYLT KHGGYLWEAP EEEANNPSNR TYCPCNLCSP HRMPGHNAAL
HNEILAIGTF EIRSPDGKTF KLTPELWTNA YLDKFDAEDF HPFTVFHYPE NASRFASTLK
ACVTQSPEIL SLIRQIQESR EEFLLTKGKG VYKDPNTGET ISRQPRDTAR AQHAGDGQAL
PAPGAYTTGG NRAETAPAGA VRLAPDYQDG QFPIAKVGPH YHGPKNVRRE DQGYRGGPGG
VRGEREVVLS RRAGGRRFGR RNTRQSGYNE RANRYFGRGG GGSVRGQQGE HPTTSPSASE
PPAPSRILAR GTPPSPERRD RQEE
