| IED ID | IndEnz0002018863 |
| Enzyme Type ID | protease018863 |
| Protein Name |
Pre-protein VI pVI Cleaved into: Endosome lysis protein; Protease cofactor pVI-C |
| Gene Name | L3 |
| Organism | Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12) |
| Taxonomic Lineage | Viruses Varidnaviria Bamfordvirae Preplasmiviricota Tectiliviricetes Rowavirales Adenoviridae Mastadenovirus Human mastadenovirus A Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12) |
| Enzyme Sequence | MEDINFSSLAPRHGTRPYMGTWNEIGTSQLNGGAFNWNSIWSGLKNFGSTIKTYGTKAWNSQTGQMLRDKLKDQNFQQKVVDGLASGINGVVDIANQAVQKKIANRLEPRPDEVMVEEKLPPLETVPGSVPTKGEKRPRPDAEETLVTHTTEPPSYEEAIKQGAALSPTTYPMTKPILPMATRVYGKNENVPMTLELPPLPEPTIADPVGSVPVASVPVASTVSRPAVRPVAVASLRNPRSSNWQSTLNSIVGLGVKSLKRRRCY |
| Enzyme Length | 265 |
| Uniprot Accession Number | P35988 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Pre-protein VI]: During virus assembly, promotes hexon trimers nuclear import through nuclear pore complexes via an importin alpha/beta-dependent mechanism. By analogy to herpesviruses capsid assembly, might act as a chaperone to promote the formation of the icosahedral capsid. {ECO:0000255|HAMAP-Rule:MF_04048}.; FUNCTION: [Endosome lysis protein]: Structural component of the virion that provides increased stability to the particle shell through its interaction with the core-capsid bridging protein and the hexon-linking protein VIII. Fibers shedding during virus entry into host cell allows the endosome lysis protein to be exposed as a membrane-lytic peptide. Exhibits pH-independent membrane fragmentation activity and probably mediates viral rapid escape from host endosome via organellar membrane lysis. It is not clear if it then remains partially associated with the capsid and involved in the intracellular microtubule-dependent transport of capsid to the nucleus, or if it is lost during endosomal penetration. {ECO:0000255|HAMAP-Rule:MF_04048}.; FUNCTION: [Protease cofactor]: Cofactor that activates the viral protease. Binds to viral protease in a 1:1 ratio. {ECO:0000255|HAMAP-Rule:MF_04048}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Disulfide bond (1); Modified residue (1); Motif (5); Propeptide (1); Region (6); Site (2) |
| Keywords | Capsid protein;Cytoplasmic inwards viral transport;Direct protein sequencing;Disulfide bond;Host cytoplasm;Host nucleus;Host-virus interaction;Late protein;Microtubular inwards viral transport;Phosphoprotein;Ubl conjugation;Viral capsid assembly;Viral penetration into host cytoplasm;Viral penetration via lysis of host organellar membrane;Viral release from host cell;Virion;Virus entry into host cell |
| Interact With | |
| Induction | INDUCTION: Expressed in the late phase of the viral replicative cycle. {ECO:0000255|HAMAP-Rule:MF_04048}. |
| Subcellular Location | SUBCELLULAR LOCATION: [Pre-protein VI]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04048}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04048}. Note=Shuttles between host cytoplasm and nucleus. {ECO:0000255|HAMAP-Rule:MF_04048}.; SUBCELLULAR LOCATION: [Endosome lysis protein]: Virion {ECO:0000255|HAMAP-Rule:MF_04048}. Note=Associates with the base of each peripentonal hexon on the capsid interior. Present in around 360 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04048}. |
| Modified Residue | MOD_RES 148; /note=Phosphothreonine; by host; /evidence=ECO:0000255|HAMAP-Rule:MF_04048 |
| Post Translational Modification | PTM: Ubiquitinated by Nedd4 following partial capsid disassembly; which might play a role in intracellular virus movement during entry. {ECO:0000255|HAMAP-Rule:MF_04048}.; PTM: [Protease cofactor]: Contains the major nuclear import and export signals. Proteolytically removed during virion maturation. The processing of the C-terminus turns the precursor into a mature viral structural protein and abrogates its ability to promote hexon import and act as a potential chaperone protein. {ECO:0000255|HAMAP-Rule:MF_04048}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 67..76; /note=Nuclear export signal; /evidence=ECO:0000255|HAMAP-Rule:MF_04048; MOTIF 136..140; /note=Nuclear localization signal; /evidence=ECO:0000255|HAMAP-Rule:MF_04048; MOTIF 153..156; /note=PPXY motif; /evidence=ECO:0000255|HAMAP-Rule:MF_04048; MOTIF 246..257; /note=Nuclear export signal; /evidence=ECO:0000255|HAMAP-Rule:MF_04048; MOTIF 260..263; /note=Nuclear localization signal; /evidence=ECO:0000255|HAMAP-Rule:MF_04048 |
| Gene Encoded By | |
| Mass | 28,912 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |