| IED ID | IndEnz0002016406 |
| Enzyme Type ID | protease016406 |
| Protein Name |
Pre-hexon-linking protein IIIa Capsid vertex-specific component IIIa CVSC Protein IIIa pIIIa Cleaved into: Hexon-linking protein IIIa |
| Gene Name | L1 |
| 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 | MMQDATDPAVRAALQSQPSGLNSTDDWRQVMDRIMSLTARNPDAFRQQPQANRLSAILEAVVPARANPTHEKVLAIVNALAENRAIRPDEAGLVYDALLQRVARYNSGNVQTNLDRLVGDVREAVAQRERAQQQGNLGSMVALNAFLSTQPANVPRGQEDYTNFVSALRLMVTETPQSEVYQSGPDYFFQTSRQGLQTVNLSQAFKNLQGLWGVRAPTGDRATVSSLLTPNSRLLLLLIAPFTDSGSVSRDTYLGHLLTLYREAIGQAHVDEHTFQEITSVSRALGQEDTGSLEATLNYLLTNRRQKIPSLHSLNSEEERILRYVQQSVSLNLMRDGVTPSVALDMTARNMEPGMYASNRPFINRLMDYLHRAAAVNPEYFTNAILNPHWLPPPGFYTGGFEVPEGNDGFLWDDIDDSVFSPQPQTLLELQQREQAEAALRKESFRRPSSLSDLGAAAPRSDASSPFPSLIGSLTSTRTTRPRLLGEEEYLNNSLLQPQREKNLPPAFPNNGIESLVDKMSRWKTYAQEHRDVPGPRPPTRRQRHDRQRGLVWEDDDSADDSSVLDLGGSGNPFAHLRPRLGRMF |
| Enzyme Length | 585 |
| Uniprot Accession Number | P12537 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Structural component of the virion that acts as a cement protein on the capsid exterior and which mediates the interactions between the hexons, including the peripentonal hexons, and reaches all the way to the penton vertices. Two hexon linking proteins IIIa, one from each facet, stabilize the unique edge interface between a pair of facets. As the virus enters the host cell, hexon linking proteins IIIa are shed concomitant with virion acidification in the endosome. During virus assembly, seems to play a role in the serotype specificity of the packaging of viral DNA via its interaction with packaging protein 3. {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000269|PubMed:20798312, ECO:0000269|PubMed:21632753, ECO:0000269|PubMed:25071205}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Compositional bias (2); Modified residue (12); Propeptide (1); Region (5); Site (1) |
| Keywords | 3D-structure;Capsid decoration protein;Capsid protein;Host nucleus;Late protein;Phosphoprotein;Viral genome packaging;Viral release from host cell;Virion |
| Interact With | |
| Induction | INDUCTION: Expressed in the late phase of the viral replicative cycle. {ECO:0000255|HAMAP-Rule:MF_04047}. |
| Subcellular Location | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000269|PubMed:18786542, ECO:0000269|PubMed:20798312, ECO:0000269|PubMed:25071205}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000305}. Note=Surrounds the border of each facet on the capsid exterior. Present in around 60 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000269|PubMed:25071205}. |
| Modified Residue | MOD_RES 225; /note="Phosphoserine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 274; /note="Phosphothreonine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 310; /note="Phosphoserine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 444; /note="Phosphoserine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 449; /note="Phosphoserine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 450; /note="Phosphoserine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 452; /note="Phosphoserine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 469; /note="Phosphoserine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 473; /note="Phosphoserine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 490; /note="Phosphotyrosine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 494; /note="Phosphoserine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047"; MOD_RES 515; /note="Phosphoserine; by host"; /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047" |
| Post Translational Modification | PTM: Cleaved near the C-terminus by the viral protease during virion maturation to form the mature protein. {ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-Rule:MF_04047}. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (1); X-ray crystallography (1) |
| Cross Reference PDB | 6B1T; 6CGV; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 65,253 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |