SHUT_ADEGX
ID SHUT_ADEGX Reviewed; 798 AA.
AC P36856;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 02-JUN-2021, entry version 54.
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 C serotype 10 (strain SA2) (FAdV-10) (Fowl adenovirus 10).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus C.
OX NCBI_TaxID=10547;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8224879; DOI=10.1016/0378-1119(93)90214-n;
RA Sheppard M.;
RT "Identification of a fowl adenovirus gene with sequence homology to the
RT 100K gene of human adenovirus.";
RL Gene 132:307-308(1993).
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; L07890; AAA72328.1; -; Genomic_DNA.
DR PIR; JN0878; JN0878.
DR PRIDE; P36856; -.
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..798
FT /note="Shutoff protein"
FT /id="PRO_0000221863"
FT DOMAIN 379..497
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..376
FT /note="Binding to host EIF4G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 740..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 711
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
SQ SEQUENCE 798 AA; 89029 MW; 04CFA042AC6A0DF4 CRC64;
MESTADGDKA RGEEPVAEGE ASDIRRGDGE FPAPEDEHPD DGEPDEPADR DDRSGESDAD
SGYYSADGGR DAECDGEAAR PDTPTDESSA PTTPSTAVRR SSGESSPDRG GCFSHSSDSE
LGCATETRDP FAAGLRKCIE RQAMILTGAL KDAHVDPPLD SMPLTVDAVQ RQLERFLFNP
DPKVPREHVE LATTFMPPFM TPKAIANYHI FCGNRPIPPS CKANRSGSEV LRAAENARFF
KRLPRWKQGV TVDDGLGDEV SPITELKDAK LVPLRDDTSR LEWAKMRGEH VRYFCYPSLH
MPPKISRMLM EVLLQPFAQE VASGPDQEDP EPVYPTAELA CIVDPEGVMQ PHGLARAIEV
DGHGSAGRPL YRSARAYGSV FREPSSIKKA QEVLHHTFHH GFVALIRETA KVNLSNYATF
HGITYNDPLN NCMLAKLMEG SDKRDYVVDS IYLFLVLTWQ TAMGMWQQAI QEETIEAYRE
AFTRLRRAIY ALETPTEISK AIVDVLMDGD RLCAEMPKLP NFTNGSQISA FRQFIMERSN
IPTTAAPFLP SDFVPLSFRQ AQPLLWDQVY LLQTAFFLCN HGGYLWEPEE TENPNPRDRT
YCPCNLCSPH RMPQHNVPLH NELLAINTFE IRTDDGKTFK LTPELWANAY LDKFEPKDYH
PFEVVHFPQH EEAFSRDLTA CVTKSPEILS LIRQIQASRE EFLLTRGKGV YKDPDTGEVL
TPQPDLQAGA ARRQALPTAY ADHARGAATS AEPSRALRPT SVATAAGNRT RGCSSARYRL
GPTLRRRSNS SWPREWST
