A0A3Q9HLI8 · A0A3Q9HLI8_9ADEN
- ProteinPre-hexon-linking protein IIIa
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids585 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Structural component of the virion that acts as a cement protein on the capsid exterior 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.
Miscellaneous
All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 570-571 | Cleavage; by viral protease | ||||
Sequence: SG |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | host cell nucleus | |
Cellular Component | viral capsid, decoration |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended namePre-hexon-linking protein IIIa
- Alternative names
- Cleaved into 1 chains
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Mastadenovirus
Accessions
- Primary accessionA0A3Q9HLI8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Surrounds the border of each facet on the capsid exterior. Present in around 60 copies per virion.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5023351816 | 1-570 | Hexon-linking protein IIIa | |||
Sequence: MMQDATDPAVRAALQSQPSGLNSTDDWRQVMDRIMSLTARNPDAFRQQPQANRLSAILEAVVPARANPTHEKVLAIVNALAENRAIRPDEAGLVYDALLQRVARYNSGNVQTNLDRLVGDVREAVAQRERAQQQGNLGSMVALNAFLSTQPANVPRGQEDYTNFVSALRLMVTETPQSEVYQSGPDYFFQTSRQGLQTVNLSQAFKNLQGLWGVRAPTGDRATVSSLLTPNSRLLLLLIAPFTDSGSVSRDTYLGHLLTLYREAIGQAHVDEHTFQEITSVSRALGQEDTGSLEATLNYLLTNRRQKIPSLHSLNSEEERILRYVQQSVSLNLMRDGVTPSVALDMTARNMEPGMYASNRPFINRLMDYLHRAAAVNPEYFTNAILNPHWLPPPGFYTGGFEVPEGNDGFLWDDIDDSVFSPQPQTLLELHQREQAEAALRKESFRRPSSLSDLGAAAPRSDASSPFPSLIGSLTSTRTTRPRLLGEEEYLNNSLLQPQREKNLPPAFPNNGIESLVDKMSRWKTYAQEHRDVPGPRPPTRRQRHDRQRGLVWEDDDSADDSSVLDLGGS | ||||||
Chain | PRO_5023351817 | 1-585 | Pre-hexon-linking protein IIIa | |||
Sequence: MMQDATDPAVRAALQSQPSGLNSTDDWRQVMDRIMSLTARNPDAFRQQPQANRLSAILEAVVPARANPTHEKVLAIVNALAENRAIRPDEAGLVYDALLQRVARYNSGNVQTNLDRLVGDVREAVAQRERAQQQGNLGSMVALNAFLSTQPANVPRGQEDYTNFVSALRLMVTETPQSEVYQSGPDYFFQTSRQGLQTVNLSQAFKNLQGLWGVRAPTGDRATVSSLLTPNSRLLLLLIAPFTDSGSVSRDTYLGHLLTLYREAIGQAHVDEHTFQEITSVSRALGQEDTGSLEATLNYLLTNRRQKIPSLHSLNSEEERILRYVQQSVSLNLMRDGVTPSVALDMTARNMEPGMYASNRPFINRLMDYLHRAAAVNPEYFTNAILNPHWLPPPGFYTGGFEVPEGNDGFLWDDIDDSVFSPQPQTLLELHQREQAEAALRKESFRRPSSLSDLGAAAPRSDASSPFPSLIGSLTSTRTTRPRLLGEEEYLNNSLLQPQREKNLPPAFPNNGIESLVDKMSRWKTYAQEHRDVPGPRPPTRRQRHDRQRGLVWEDDDSADDSSVLDLGGSGNPFAHLRPRLGRMF | ||||||
Modified residue | 225 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 274 | Phosphothreonine; by host | ||||
Sequence: T | ||||||
Modified residue | 310 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 444 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 449 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 450 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 452 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 469 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 473 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 490 | Phosphotyrosine; by host | ||||
Sequence: Y | ||||||
Modified residue | 494 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 515 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Propeptide | PRO_5018798329 | 571-585 | ||||
Sequence: GNPFAHLRPRLGRMF |
Post-translational modification
Cleaved near the C-terminus by the viral protease during virion maturation to form the mature protein.
Keywords
- PTM
Expression
Induction
Expressed in the late phase of the viral replicative cycle.
Keywords
- Developmental stage
Interaction
Subunit
Interacts with hexon proteins; this interaction tethers the peripentonal hexons to hexons situated in the facet. Interacts with the penton protein (via N-terminus). Interacts with packaging protein 3; this interaction is required to promote correct genome packaging.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-24 | Disordered | ||||
Sequence: MMQDATDPAVRAALQSQPSGLNST | ||||||
Region | 1-106 | Peripentonal hexon-tethering domain | ||||
Sequence: MMQDATDPAVRAALQSQPSGLNSTDDWRQVMDRIMSLTARNPDAFRQQPQANRLSAILEAVVPARANPTHEKVLAIVNALAENRAIRPDEAGLVYDALLQRVARYN | ||||||
Compositional bias | 10-24 | Polar residues | ||||
Sequence: VRAALQSQPSGLNST | ||||||
Region | 138-251 | Binding to hexon-linking protein | ||||
Sequence: GSMVALNAFLSTQPANVPRGQEDYTNFVSALRLMVTETPQSEVYQSGPDYFFQTSRQGLQTVNLSQAFKNLQGLWGVRAPTGDRATVSSLLTPNSRLLLLLIAPFTDSGSVSRD | ||||||
Region | 439-479 | Disordered | ||||
Sequence: ALRKESFRRPSSLSDLGAAAPRSDASSPFPSLIGSLTSTRT | ||||||
Compositional bias | 528-556 | Basic and acidic residues | ||||
Sequence: QEHRDVPGPRPPTRRQRHDRQRGLVWEDD | ||||||
Region | 528-573 | Disordered | ||||
Sequence: QEHRDVPGPRPPTRRQRHDRQRGLVWEDDDSADDSSVLDLGGSGNP |
Sequence similarities
Belongs to the adenoviridae hexon-linking protein IIIa family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length585
- Mass (Da)65,262
- Last updated2019-04-10 v1
- Checksum5543798B79E6B61D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 10-24 | Polar residues | ||||
Sequence: VRAALQSQPSGLNST | ||||||
Compositional bias | 528-556 | Basic and acidic residues | ||||
Sequence: QEHRDVPGPRPPTRRQRHDRQRGLVWEDD |