SHUT_ADECC
ID SHUT_ADECC Reviewed; 689 AA.
AC P68966; Q65957;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 46.
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 Canine adenovirus serotype 1 (strain CLL) (CAdV-1) (Canine adenovirus 1
OS (strain CLL)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX NCBI_TaxID=69150;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Campbell J.B., Zhao Y.;
RT "DNA sequence and genomic organization of canine adenovirus type 1.";
RL Submitted (AUG-1996) 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; U55001; AAB05446.1; -; Genomic_DNA.
DR RefSeq; AP_000062.1; AC_000003.1.
DR SMR; P68966; -.
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..689
FT /note="Shutoff protein"
FT /id="PRO_0000221860"
FT DOMAIN 292..410
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..289
FT /note="Binding to host EIF4G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 625..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 309
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT MOD_RES 627
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
SQ SEQUENCE 689 AA; 77373 MW; 6062D58E0ACE7763 CRC64;
MSEEPVSGTT VEIEEDTHTP PNSPVLETFS LSPEPEAEAC PNTDRYLSAN LLCKHLQRQS
AIVLDSIKDQ LQVPTSVSEL SCAYERSLLC PNIPPKQQSN GTCEANPKLN FYPTFLVPET
LATYHIFFVN QKIPVSCKAN RAKADKALTL QEGDCLPDYE TMDTVSRVFE GLGGEVVAEN
ALQNNDSVLV ELKEDNPRLA VLKRNLSVSH FAYPAVHLPP KIITTVMNNL LVKRANPSAD
VSELDPDGGQ EVVSDTELSR WLNTSDPETL EKQRKLVMGS VLVTVVLECM QRLFTSKDMV
KKIGETLHYT FRHGYVSLAC KISNVELTNV VTYMGILHEN RLGQTTLHHT IQGETRRDYI
RDSIFLILIH TWQTAMGIWQ QCLEEENLKE LAKLVQKIKK PLYTETSQRL MGKQLANVVF
PPKLLETFNK GLPDIVNQSM MQNFRSFILE RSGILPSMTC ALPTDFIPIH FKECPPTMWP
YTYLLRLANF FMYHNDLCYD MEGEGLLEHY CRCNLCTPHR CLATNPAMLN ETQLIGTFDI
RGPGGENGAE SSSGLKLTAG MWTSAFLRKF ESSDYHAHKI HFYENQSKPP SVEPTPCVIT
QSSILAQLHD IKKAREEFLL KKGQGQYLDP HTGEPLNAAG PSVESGHEFQ GDGRHREPKR
GRHFRQRGGP RKPPRAHAGG EPDVRGTTS
