P12537 (CAP3_ADE05) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 50. History...
Names and origin
|Protein names||Recommended name:|
Pre-capsid vertex protein
Capsid vertex-specific component IIIa
Cleaved into the following chain:
|Organism||Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5) [Complete proteome]|
|Taxonomic identifier||28285 [NCBI]|
|Taxonomic lineage||Viruses › dsDNA viruses, no RNA stage › Adenoviridae › Mastadenovirus ›|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
|Sequence length||585 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Structural component of the virion that is likely to participate in vertex stabilization and genome packaging. Stabilizes vertices by tethering the penton bases to neighboring peripentonal hexons. Lashes peripentonal hexons to the neighboring hexons thanks to its interaction with hexon-linking protein. As the virus enters the host cell, capsid vertex proteins are shed concomitant with virion acidification in the endosome. During virus assembly, seems to play a role in packaging of viral DNA via its interaction with packaging protein 3. Ref.5 Ref.7
Interacts with penton and hexon proteins; this interaction binds the penton base to neighboring peripentonal hexons. Interacts with hexon-linking protein; this interaction tethers the peripentonal hexons to hexons situated in the facet. Interacts with packaging protein 3; this interaction is required to promote correct genome packaging. Interacts with adjacent capsid vertex proteins (self-interaction). Ref.5 Ref.7
Expressed in the late phase of the viral replicative cycle.
Cleaved near the N-terminus by the viral protease during virion maturation to form the mature protein By similarity.
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.
Belongs to the adenoviridae capsid vertex protein family.
|Biological process||Viral genome packaging|
Virus exit from host cell
|Cellular component||Host nucleus|
|Developmental stage||Late protein|
|Molecular function||Capsid protein|
|Gene Ontology (GO)|
|Biological_process||viral release from host cell|
Inferred from electronic annotation. Source: UniProtKB-KW
|Cellular_component||host cell nucleus|
Inferred from electronic annotation. Source: UniProtKB-SubCellviral capsid
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 585||585||Pre-capsid vertex protein||PRO_0000221835|
|Propeptide||1 – 15||15||By similarity||PRO_0000421129|
|Chain||16 – 585||570||Capsid vertex protein By similarity||PRO_0000421130|
|Region||1 – 106||106||Peripentonal hexon-tethering domain By similarity|
|Region||138 – 251||114||Binding to hexon-linking protein By similarity|
|Site||15 – 16||2||Cleavage; by viral protease By similarity|
Amino acid modifications
|Modified residue||225||1||Phosphoserine; by host By similarity|
|Modified residue||274||1||Phosphothreonine; by host By similarity|
|Modified residue||310||1||Phosphoserine; by host By similarity|
|Modified residue||444||1||Phosphoserine; by host By similarity|
|Modified residue||449||1||Phosphoserine; by host By similarity|
|Modified residue||450||1||Phosphoserine; by host By similarity|
|Modified residue||452||1||Phosphoserine; by host By similarity|
|Modified residue||469||1||Phosphoserine; by host By similarity|
|Modified residue||473||1||Phosphoserine; by host By similarity|
|Modified residue||490||1||Phosphotyrosine; by host By similarity|
|Modified residue||494||1||Phosphoserine; by host By similarity|
|Modified residue||515||1||Phosphoserine; by host By similarity|
|||"The sequence of the genome of adenovirus type 5 and its comparison with the genome of adenovirus type 2."|
Chroboczek J., Bieber F., Jacrot B.
Virology 186:280-285(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
|||"De novo derivation of proteomes from transcriptomes for transcript and protein identification."|
Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.
Nat. Methods 9:1207-1211(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
|||"Determination of the nucleotide sequence for the penton-base gene of human adenovirus type 5."|
Neumann R., Chroboczek J., Jacrot B.
Gene 69:153-157(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 469-585.
|||"Localization of the N-terminus of minor coat protein IIIa in the adenovirus capsid."|
San Martin C., Glasgow J.N., Borovjagin A., Beatty M.S., Kashentseva E.A., Curiel D.T., Marabini R., Dmitriev I.P.
J. Mol. Biol. 383:923-934(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
|||"Adenovirus structural protein IIIa is involved in the serotype specificity of viral DNA packaging."|
Ma H.C., Hearing P.
J. Virol. 85:7849-7855(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PACKAGING PROTEIN 3.
Strain: Human adenovirus D serotype 17.
|||"Latest insights on adenovirus structure and assembly."|
San Martin C.
Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
|||"Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks."|
Liu H., Jin L., Koh S.B., Atanasov I., Schein S., Wu L., Zhou Z.H.
Science 329:1038-1043(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL PARTICLE, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HEXON-LINKING PROTEIN; PENTON PROTEIN AND HEXON PROTEIN.
|M73260 Genomic DNA. Translation: AAA96407.1.|
M22141 Genomic DNA. Translation: AAA42518.1.
|PIR||SXADH5. B39449. |
|RefSeq||AP_000205.1. AC_000008.1. |
3D structure databases
Protocols and materials databases
Family and domain databases
|InterPro||IPR003479. Hex_IIIa. |
|Pfam||PF02455. Hex_IIIa. 1 hit. |
|Accession||Primary (citable) accession number: P12537|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|