Detail Information for IndEnz0002001740
IED ID IndEnz0002001740
Enzyme Type ID protease001740
Protein Name Shutoff protein
100 kDa protein
p100K
100K-chaperone protein
L4-100K
Shutoff protein 100K
Gene Name L4
Organism Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Taxonomic Lineage Viruses Varidnaviria Bamfordvirae Preplasmiviricota Tectiliviricetes Rowavirales Adenoviridae Mastadenovirus Human mastadenovirus C Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Enzyme Sequence MESVEKEDSLTAPFEFATTASTDAANAPTTFPVEAPPLEEEEVIIEQDPGFVSEDDEDRSVPTEDKKQDQDDAEANEEQVGRGDQRHGDYLDVGDDVLLKHLQRQCAIICDALQERSDVPLAIADVSLAYERHLFSPRVPPKRQENGTCEPNPRLNFYPVFAVPEVLATYHIFFQNCKIPLSCRANRSRADKQLALRQGAVIPDIASLDEVPKIFEGLGRDEKRAANALQQENSENESHCGVLVELEGDNARLAVLKRSIEVTHFAYPALNLPPKVMSTVMSELIVRRARPLERDANLQEQTEEGLPAVGDEQLARWLETREPADLEERRKLMMAAVLVTVELECMQRFFADPEMQRKLEETLHYTFRQGYVRQACKISNVELCNLVSYLGILHENRLGQNVLHSTLKGEARRDYVRDCVYLFLCYTWQTAMGVWQQCLEERNLKELQKLLKQNLKDLWTAFNERSVAAHLADIIFPERLLKTLQQGLPDFTSQSMLQNFRNFILERSGILPATCCALPSDFVPIKYRECPPPLWGHCYLLQLANYLAYHSDIMEDVSGDGLLECHCRCNLCTPHRSLVCNSQLLSESQIIGTFELQGPSPDEKSAAPGLKLTPGLWTSAYLRKFVPEDYHAHEIRFYEDQSRPPNAELTACVITQGHILGQLQAINKARQEFLLRKGRGVYLDPQSGEELNPIPPPPQPYQQPRALASQDGTQKEAAAAAAATHGRGGILGQSGRGGFGRGGGDDGRLGQPRRSFRGRRGVRRNTVTLGRIPLAGAPEIGNRSQHRYNLRSSGAAGTACSPTQP
Enzyme Length 805
Uniprot Accession Number P24932
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Protein that inhibits host translation while promoting late viral translation by ribosome shunting. Blocks host cap-dependent translation by binding to eIF4G, displacing MKNK1 from cap initiation complexes and preventing EIF4E phosphorylation. Binds to the tripartite leader sequence of viral late mRNAs and recruits host eIF4G, PABPC1/poly-A binding protein and 40S ribosomes subunits on viral mRNAs, allowing ribosome shunting and efficient translation of late viral mRNAs even though conventional translation via ribosome scanning from the cap has been shut off in the host cell. During assembly, acts as a chaperone protein that helps hexon proteins assembly into trimers (Probable). {ECO:0000255|HAMAP-Rule:MF_04060, ECO:0000305|PubMed:15220445, ECO:0000305|PubMed:15314025, ECO:0000305|PubMed:15827182, ECO:0000305|PubMed:16081097, ECO:0000305|PubMed:7159928}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (4); Domain (1); Modified residue (2); Mutagenesis (2); Region (3)
Keywords Chaperone;Eukaryotic host gene expression shutoff by virus;Eukaryotic host translation shutoff by virus;Host cytoplasm;Host gene expression shutoff by virus;Host-virus interaction;Inhibition of eukaryotic host translation factors by virus;Late protein;Methylation;Phosphoprotein;RNA-binding;Reference proteome;Translational shunt;Transport
Interact With
Induction INDUCTION: Expressed in the late phase of the viral replicative cycle. {ECO:0000255|HAMAP-Rule:MF_04060}.
Subcellular Location SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04060, ECO:0000269|PubMed:14633984}.
Modified Residue MOD_RES 365; /note="Phosphotyrosine; by host"; /evidence="ECO:0000255|HAMAP-Rule:MF_04060, ECO:0000269|PubMed:15827182"; MOD_RES 682; /note="Phosphotyrosine; by host"; /evidence="ECO:0000255|HAMAP-Rule:MF_04060, ECO:0000269|PubMed:15827182"
Post Translational Modification PTM: Might be cleaved by the viral protease. {ECO:0000255|HAMAP-Rule:MF_04060}.; PTM: Phosphorylated. Tyrosine phosphorylation enhances preferential binding to tripartite leader mRNAs and allows ribosome shunting. {ECO:0000255|HAMAP-Rule:MF_04060, ECO:0000269|PubMed:15827182}.; PTM: Methylated. Asymmetric dimethylation by host PRMT1 of the Arg/Gly-rich region may regulate shutoff protein binding to hexon and promote the capsid assembly in the nucleus. {ECO:0000255|HAMAP-Rule:MF_04060, ECO:0000269|PubMed:19264777}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 90,138
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda