SHUT_ADE05
ID SHUT_ADE05 Reviewed; 807 AA.
AC P24933; P03268;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 29-SEP-2021, entry version 77.
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 C serotype 5 (HAdV-5) (Human adenovirus 5).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=28285;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA Chroboczek J., Bieber F., Jacrot B.;
RT "The sequence of the genome of adenovirus type 5 and its comparison with
RT the genome of adenovirus type 2.";
RL Virology 186:280-285(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-593.
RX PubMed=6117824; DOI=10.1093/nar/9.18.4439;
RA Kruijer W., van Schaik F.M.A., Sussenbach J.S.;
RT "Structure and organization of the gene coding for the DNA binding protein
RT of adenovirus type 5.";
RL Nucleic Acids Res. 9:4439-4457(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=23142869; DOI=10.1038/nmeth.2227;
RA Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.;
RT "De novo derivation of proteomes from transcriptomes for transcript and
RT protein identification.";
RL Nat. Methods 9:1207-1211(2012).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=14633984; DOI=10.1093/emboj/cdg614;
RA Wodrich H., Guan T., Cingolani G., Von Seggern D., Nemerow G., Gerace L.;
RT "Switch from capsid protein import to adenovirus assembly by cleavage of
RT nuclear transport signals.";
RL EMBO J. 22:6245-6255(2003).
RN [5]
RP METHYLATION AT ARG/GLY REGION.
RX PubMed=19264777; DOI=10.1128/jvi.02493-08;
RA Koyuncu O.O., Dobner T.;
RT "Arginine methylation of human adenovirus type 5 L4 100-kilodalton protein
RT is required for efficient virus production.";
RL J. Virol. 83:4778-4790(2009).
RN [6]
RP REVIEW.
RX PubMed=21655914; DOI=10.1007/s00018-011-0740-4;
RA Szolajska E., Chroboczek J.;
RT "Faithful chaperones.";
RL Cell. Mol. Life Sci. 68:3307-3322(2011).
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 ECO:0000269|PubMed:14633984}.
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 ECO:0000269|PubMed:19264777}.
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; M73260; AAA96412.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X02997; CAA26756.1; -; Genomic_DNA.
DR PIR; A39449; WMAD15.
DR RefSeq; AP_000214.1; AC_000008.1.
DR IntAct; P24933; 1.
DR MINT; P24933; -.
DR Proteomes; UP000004992; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046729; C:viral procapsid; IMP:CACAO.
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 1: Evidence at protein 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; Late protein;
KW Methylation; Phosphoprotein; RNA-binding; Translational shunt; Transport.
FT CHAIN 1..807
FT /note="Shutoff protein"
FT /id="PRO_0000221856"
FT DOMAIN 348..466
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..345
FT /note="Binding to host EIF4G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT REGION 684..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 365
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
FT MOD_RES 682
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04060"
SQ SEQUENCE 807 AA; 90213 MW; CF17561EDA7CBADF CRC64;
MESVEKKDSL TAPSEFATTA STDAANAPTT FPVEAPPLEE EEVIIEQDPG FVSEDDEDRS
VPTEDKKQDQ DNAEANEEQV GRGDERHGDY LDVGDDVLLK HLQRQCAIIC DALQERSDVP
LAIADVSLAY ERHLFSPRVP PKRQENGTCE PNPRLNFYPV FAVPEVLATY HIFFQNCKIP
LSCRANRSRA DKQLALRQGA VIPDIASLNE VPKIFEGLGR DEKRAANALQ QENSENESHS
GVLVELEGDN ARLAVLKRSI EVTHFAYPAL NLPPKVMSTV MSELIVRRAQ PLERDANLQE
QTEEGLPAVG DEQLARWLQT REPADLEERR KLMMAAVLVT VELECMQRFF ADPEMQRKLE
ETLHYTFRQG YVRQACKISN VELCNLVSYL GILHENRLGQ NVLHSTLKGE ARRDYVRDCV
YLFLCYTWQT AMGVWQQCLE ECNLKELQKL LKQNLKDLWT AFNERSVAAH LADIIFPERL
LKTLQQGLPD FTSQSMLQNF RNFILERSGI LPATCCALPS DFVPIKYREC PPPLWGHCYL
LQLANYLAYH SDIMEDVSGD GLLECHCRCN LCTPHRSLVC NSQLLNESQI IGTFELQGPS
PDEKSAAPGL KLTPGLWTSA YLRKFVPEDY HAHEIRFYED QSRPPNAELT ACVITQGHIL
GQLQAINKAR QEFLLRKGRG VYLDPQSGEE LNPIPPPPQP YQQQPRALAS QDGTQKEAAA
AAATHGRGGI LGQSGRGGFG RGGGGHDGRL GEPRRGSFRG RRGVRRNTVT LGRIPLAGAP
EIGNRFQHGY NLRSSGAAGT ARSPTQP
