Entry sw: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   30-NOV-2016, entry version 43.
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;
OS   Fowl adenovirus C serotype 10 (strain SA2) (FAdV-10) (Fowl adenovirus
OS   10).
OC   Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Aviadenovirus;
OC   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
RT   the 100K gene of human adenovirus.";
RL   Gene 132:307-308(1993).
CC   -!- FUNCTION: Protein that inhibits host translation while promoting
CC       late viral translation by ribosome shunting. Blocks host cap-
CC       dependent translation. Binds to the bipartite leader sequence of
CC       viral late mRNAs and allows ribosome shunting and efficient
CC       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. {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 bipartite leader mRNAs and allows ribosome
CC       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}.
DR   EMBL; L07890; AAA72328.1; -; Genomic_DNA.
DR   PIR; JN0878; JN0878.
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    798       Shutoff protein.
FT                                /FTId=PRO_0000221863.
FT   MOD_RES     711    711       Phosphotyrosine; by host. {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       135    720       ipfam:Adeno_100 [T]
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
//