Entry sw:SHUT_ADEP3

ID   SHUT_ADEP3              Reviewed;         838 AA.
AC   Q9YTR7;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   30-NOV-2016, entry version 50.
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   Porcine adenovirus A serotype 3 (PAdV-3) (Porcine adenovirus 3).
OC   Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus;
OC   Porcine mastadenovirus A.
OX   NCBI_TaxID=35265;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=6618;
RX   PubMed=9837805; DOI=10.1006/viro.1998.9418;
RA   Reddy P.S., Idamakanti N., Song J.Y., Lee J.B., Hyun B.H., Park J.H.,
RA   Cha S.H., Bae Y.T., Tikoo S.K., Babiuk L.A.;
RT   "Nucleotide sequence and transcription map of porcine adenovirus type
RT   3.";
RL   Virology 251:414-426(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6618 / IAF;
RA   Larocque D., Malenfant F., Massie B., Dea S.;
RT   "Porcine adenovirus serotype 3, complete genome.";
RL   Submitted (FEB-1999) 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; AF083132; AAC99445.1; -; Genomic_DNA.
DR   EMBL; AJ237815; CAB41033.1; -; Genomic_DNA.
DR   EMBL; AB026117; BAA76971.1; -; Genomic_DNA.
DR   RefSeq; YP_009213.1; AC_000189.1.
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    838       Shutoff protein.
FT                                /FTId=PRO_0000221864.
FT   DOMAIN      356    474       RRM.
FT   MOD_RES     373    373       Phosphotyrosine; by host. {ECO:0000250}.
FT   MOD_RES     690    690       Phosphotyrosine; by host. {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       108    700       ipfam:Adeno_100 [T]
SQ   SEQUENCE   838 AA;  94103 MW;  D7EE710DE03F5065 CRC64;
     MEDQHSAASE LGSSAAPTLP PPPPPPPPPT SPPPSLQQRQ QEPTETDDAE DTCSSSSSSS
     ASSECFVSPL EDTSSEDSAD TVLPSEPRRD EEEQEEDSPD RYMDADVLQR HLLRQSTILR
     QVLQEAAPGA AAEAAEAPSV AELSRRLEAA LFSPATPPRR QENGTCAPDP RLNFYPVFML
     PEALATYLLF FHNQKIPVSC RANRPRADAH WRLPSGTPLP DYPTTDEVYK IFEGLGDEEP
     ACANQDLKER DSVLVELKLD NPRLAVVKQC IAVTHFAYPA LALPPKVMST LMQTLLVRRA
     SPLPDEGETP LEDLLVVSDE QLARWMHTSD PKVLEERRKT VTAACMVTVQ LHCMHTFLTS
     REMVRRLGEC LHYMFRQGYV KLASKIANME LSNLVSYLGM LHENRLGQHV LHHTLKHEAR
     RDYVRDTIYL YLVYTWQTAM GVWQQCLEDR NLRALETSLA RARQSLWTGF DERTIAQDLA
     AFLFPTKLVE TLQRSLPDFA SQSMMHAFRS FVLERSGILP AVCNALPSDF VPTVYRECPP
     PLWAHCYLLR LANFLMYHCD LAEDTSGEGL FECYCRCNLC APHRCLATNT ALLNEVQAIN
     TFELQRPPKP DGTLPPPFKL TPGLWTSAFL RHFVSEDYHS DRILFYEDVS RPPRVEPSAC
     VITHSAILAQ LHDIKKAREE FLLTKGHGVY LDPHTGEELN TAAPSTAHHA APPEEAHPQQ
     HQHQQQPSHR RRHHRSSYAD RVRSELHAYG GATGSSRDPV SGGCSARGTH SRDAARRRGS
     QQRDQRQLRR QFAQYPRGTG GGGGTGHTDE AIQALLHQQQ QQQEHQPAQE LRRPQRGS
//