Entry sw: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   30-NOV-2016, entry version 33.
DE   RecName: Full=Shutoff protein;
DE   AltName: Full=100 kDa protein;
DE            Short=p100K;
DE   AltName: Full=100K-chaperone protein;
DE   AltName: Full=L4-100K;
DE   AltName: Full=Shutoff protein 100K;
GN   ORFNames=L4;
OS   Canine adenovirus serotype 1 (strain CLL) (CAdV-1) (Canine adenovirus
OS   1 (strain CLL)).
OC   Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus;
OC   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
CC       late viral translation by ribosome shunting. Blocks host cap-
CC       dependent translation by binding to eIF4G, displacing MKNK1 from
CC       cap initiation complexes and preventing EIF4E phosphorylation.
CC       Binds to the tripartite leader sequence of viral late mRNAs and
CC       recruits host eIF4G, PABPC1/poly-A binding protein and 40S
CC       ribosomes subunits on viral mRNAs, allowing ribosome shunting and
CC       efficient translation of late viral mRNAs even though conventional
CC       translation via ribosome scanning from the cap has been shut off
CC       in the host cell. During assembly, acts as a chaperone protein
CC       that helps hexon proteins assembly into trimers (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with hexon protein;
CC       this interaction allows chaperoning and trimerization of hexon
CC       proteins. Interacts (via N-terminus) with host initiation factor
CC       EIF4G (via C-terminus). Interacts (via RRM domain) with viral
CC       mRNAs that contain the tripartite leader; this interaction allows
CC       ribosome shunting and expression of viral late mRNAs (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative
CC       cycle.
CC   -!- PTM: Phosphorylated. Tyrosine phosphorylation enhances
CC       preferential binding to tripartite leader mRNAs and allows
CC       ribosome shunting (By similarity). {ECO:0000250}.
CC   -!- PTM: Might be cleaved by the viral protease. {ECO:0000250}.
CC   -!- MISCELLANEOUS: All late proteins expressed from the major late
CC       promoter are produced by alternative splicing and alternative
CC       polyadenylation of the same gene giving rise to non-overlapping
CC       ORFs. A leader sequence is present in the N-terminus of all these
CC       mRNAs and is recognized by the viral shutoff protein to provide
CC       expression although conventional translation via ribosome scanning
CC       from the cap has been shut off in the host cell (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenoviridae shutoff protein family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC       {ECO:0000305}.
DR   EMBL; U55001; AAB05446.1; -; Genomic_DNA.
DR   RefSeq; AP_000062.1; AC_000003.1.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019060; P:intracellular transport of viral protein in host cell; IEA:InterPro.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0039704; P:viral translational shunt; ISS:UniProtKB.
DR   InterPro; IPR003381; Adeno_100.
DR   Pfam; PF02438; Adeno_100; 1.
PE   2: Evidence at transcript level;
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;
KW   Late protein; Phosphoprotein; RNA-binding; Translational shunt;
KW   Transport.
FT   CHAIN         1    689       Shutoff protein.
FT                                /FTId=PRO_0000221860.
FT   DOMAIN      292    410       RRM.
FT   REGION      226    289       Binding to host EIF4G. {ECO:0000250}.
FT   MOD_RES     309    309       Phosphotyrosine; by host. {ECO:0000250}.
FT   MOD_RES     627    627       Phosphotyrosine; by host. {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        52    637       ipfam:Adeno_100 [T]
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
//