| IED ID | IndEnz0002009799 |
| Enzyme Type ID | protease009799 |
| Protein Name |
Shutoff protein 100 kDa protein p100K 100K-chaperone protein L4-100K Shutoff protein 100K |
| Gene Name | L4 |
| Organism | Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5) |
| Taxonomic Lineage | Viruses Varidnaviria Bamfordvirae Preplasmiviricota Tectiliviricetes Rowavirales Adenoviridae Mastadenovirus Human mastadenovirus C Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5) |
| Enzyme Sequence | MESVEKKDSLTAPSEFATTASTDAANAPTTFPVEAPPLEEEEVIIEQDPGFVSEDDEDRSVPTEDKKQDQDNAEANEEQVGRGDERHGDYLDVGDDVLLKHLQRQCAIICDALQERSDVPLAIADVSLAYERHLFSPRVPPKRQENGTCEPNPRLNFYPVFAVPEVLATYHIFFQNCKIPLSCRANRSRADKQLALRQGAVIPDIASLNEVPKIFEGLGRDEKRAANALQQENSENESHSGVLVELEGDNARLAVLKRSIEVTHFAYPALNLPPKVMSTVMSELIVRRAQPLERDANLQEQTEEGLPAVGDEQLARWLQTREPADLEERRKLMMAAVLVTVELECMQRFFADPEMQRKLEETLHYTFRQGYVRQACKISNVELCNLVSYLGILHENRLGQNVLHSTLKGEARRDYVRDCVYLFLCYTWQTAMGVWQQCLEECNLKELQKLLKQNLKDLWTAFNERSVAAHLADIIFPERLLKTLQQGLPDFTSQSMLQNFRNFILERSGILPATCCALPSDFVPIKYRECPPPLWGHCYLLQLANYLAYHSDIMEDVSGDGLLECHCRCNLCTPHRSLVCNSQLLNESQIIGTFELQGPSPDEKSAAPGLKLTPGLWTSAYLRKFVPEDYHAHEIRFYEDQSRPPNAELTACVITQGHILGQLQAINKARQEFLLRKGRGVYLDPQSGEELNPIPPPPQPYQQQPRALASQDGTQKEAAAAAATHGRGGILGQSGRGGFGRGGGGHDGRLGEPRRGSFRGRRGVRRNTVTLGRIPLAGAPEIGNRFQHGYNLRSSGAAGTARSPTQP |
| Enzyme Length | 807 |
| Uniprot Accession Number | P24933 |
| 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. {ECO:0000255|HAMAP-Rule:MF_04060}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (4); Domain (1); Modified residue (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;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; MOD_RES 682; /note=Phosphotyrosine; by host; /evidence=ECO:0000255|HAMAP-Rule:MF_04060 |
| 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}.; 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 | 17363894; |
| Motif | |
| Gene Encoded By | |
| Mass | 90,213 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |