SHUT_ADE40
ID SHUT_ADE40 Reviewed; 770 AA.
AC P11823;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 81.
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 Human adenovirus F serotype 40 (HAdV-40) (Human adenovirus 40).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX NCBI_TaxID=28284;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugan;
RX PubMed=8263936; DOI=10.1006/jmbi.1993.1687;
RA Davison A.J., Telford E.A., Watson M.S., McBride K., Mautner V.;
RT "The DNA sequence of adenovirus type 40.";
RL J. Mol. Biol. 234:1308-1316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-477.
RX PubMed=3279700; DOI=10.1016/0042-6822(88)90227-9;
RA Vos H.L., der Lee F.M., Reemst A.M.C.B., van Loon A.E., Sussenbach J.S.;
RT "The genes encoding the DNA binding protein and the 23K protease of
RT adenovirus types 40 and 41.";
RL Virology 163:1-10(1988).
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}.
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DR EMBL; L19443; AAC13970.1; -; Genomic_DNA.
DR EMBL; M19540; AAA52197.1; -; Genomic_DNA.
DR PIR; C28645; WMAD40.
DR RefSeq; NP_040865.1; NC_001454.1.
DR PRIDE; P11823; -.
DR DNASU; 2715920; -.
DR GeneID; 2715920; -.
DR KEGG; vg:2715920; -.
DR Proteomes; UP000151954; Genome.
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; Reference proteome; RNA-binding;
KW Translational shunt; Transport.
FT CHAIN 1..770
FT /note="Shutoff protein"
FT /id="PRO_0000221858"
FT DOMAIN 315..433
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..312
FT /note="Binding to host EIF4G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 661..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT MOD_RES 647
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT CONFLICT 18
FT /note="N -> T (in Ref. 2; AAA52197)"
SQ SEQUENCE 770 AA; 86458 MW; 8666F5B48B74C1BF CRC64;
MEEDLKLQPD SETLTTPNSE VGAVELVKHE EENEQVEQDP GYVTPPEDGK EPVAALSEPN
YLGGEDDVLL KHIARQSTIV REALKECTQT PLTVEELSRA YEANLFSPRV PPKKQPNGTC
ETNPRLNFYP VFAVPEALAT YHIFFKNQRI PLSCRANRTR GDGLLHLKAG AHIPEIVSLE
EVPKIFEGLG KDEKRAANAL QKNETENQNV LVELEGDNAR LAVLKRTIEV SHFAYPALNL
PPKVMRSVMD QVLIKRAEPI DPQQPDLNSE DGQPVVSDDE LARWLGTQDP SELQERRKMM
MAAVLVTVEL ECLQRFFANP QTLRKVEESL HYAFRHGYVR QACKISNVEL SNLISYMGIL
HENRLGQNVL HCTLQGEARR DYVRDCIYLF LILTWQTAMG VWQQCLEEQN LQELNKLLVR
ARRELWTSFD ERTVARQLAN LIFPERLMQT LQNGLPDFVS QSILQNFRSF VLERSGILPA
MSCALPSDFV PLCYRECPPP LWSHCYLLRL ANYLAHHSDL MEDSSGDGLL ECHCRCNLCT
PHRSLVCNTE LLSETQVIGT FEIQGPEQQE GASSLKLTPA LWTSAYLRKF IPEDYHAHQI
KFYEDQSRPP KVPLTACVIT QSQILAQLQA IQQARQEFLL KKGHGVYLDP QTGEELNTPS
LSAAASCRSQ KHATQGKQAS HRATAIPAET TKAVGRGGDV GRQPGRGSFR RGGGGADGEL
GQPRRGGPRG RGGRNHRQRQ GTIFQKTRSE PTSENYPAPA TATMFTESQP
