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P12537 (CAP3_ADE05) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pre-capsid vertex protein
Alternative name(s):
Capsid vertex-specific component IIIa
Short name=CVSC
Protein IIIa
pIIIa

Cleaved into the following chain:

  1. Capsid vertex protein
Gene names
ORF Names:L1
OrganismHuman adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5) [Complete proteome]
Taxonomic identifier28285 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Pre-capsid vertex protein: Host nucleus Probable Ref.4 Ref.7.

Capsid vertex protein: Virion. Note: Located inside the virion, arranged in a ring underneath the penton base and peripentonal hexons. Present in around 60 copies per virion. Ref.4 Ref.7

Induction

Expressed in the late phase of the viral replicative cycle.

Post-translational modification

Cleaved near the N-terminus by the viral protease during virion maturation to form the mature protein By similarity.

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.

Sequence similarities

Belongs to the adenoviridae capsid vertex protein family.

Ontologies

Keywords
   Biological processViral genome packaging
Virus exit from host cell
   Cellular componentCapsid protein
Host nucleus
Virion
   Developmental stageLate protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processviral release from host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

viral capsid

Inferred from direct assay PubMed 19782383. Source: CACAO

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 585585Pre-capsid vertex protein
PRO_0000221835
Propeptide1 – 1515 By similarity
PRO_0000421129
Chain16 – 585570Capsid vertex protein By similarity
PRO_0000421130

Regions

Region1 – 106106Peripentonal hexon-tethering domain By similarity
Region138 – 251114Binding to hexon-linking protein By similarity

Sites

Site15 – 162Cleavage; by viral protease By similarity

Amino acid modifications

Modified residue2251Phosphoserine; by host By similarity
Modified residue2741Phosphothreonine; by host By similarity
Modified residue3101Phosphoserine; by host By similarity
Modified residue4441Phosphoserine; by host By similarity
Modified residue4491Phosphoserine; by host By similarity
Modified residue4501Phosphoserine; by host By similarity
Modified residue4521Phosphoserine; by host By similarity
Modified residue4691Phosphoserine; by host By similarity
Modified residue4731Phosphoserine; by host By similarity
Modified residue4901Phosphotyrosine; by host By similarity
Modified residue4941Phosphoserine; by host By similarity
Modified residue5151Phosphoserine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P12537 [UniParc].

Last modified March 1, 1992. Version 2.
Checksum: 430113688C473F1D

FASTA58565,253
        10         20         30         40         50         60 
MMQDATDPAV RAALQSQPSG LNSTDDWRQV MDRIMSLTAR NPDAFRQQPQ ANRLSAILEA 

        70         80         90        100        110        120 
VVPARANPTH EKVLAIVNAL AENRAIRPDE AGLVYDALLQ RVARYNSGNV QTNLDRLVGD 

       130        140        150        160        170        180 
VREAVAQRER AQQQGNLGSM VALNAFLSTQ PANVPRGQED YTNFVSALRL MVTETPQSEV 

       190        200        210        220        230        240 
YQSGPDYFFQ TSRQGLQTVN LSQAFKNLQG LWGVRAPTGD RATVSSLLTP NSRLLLLLIA 

       250        260        270        280        290        300 
PFTDSGSVSR DTYLGHLLTL YREAIGQAHV DEHTFQEITS VSRALGQEDT GSLEATLNYL 

       310        320        330        340        350        360 
LTNRRQKIPS LHSLNSEEER ILRYVQQSVS LNLMRDGVTP SVALDMTARN MEPGMYASNR 

       370        380        390        400        410        420 
PFINRLMDYL HRAAAVNPEY FTNAILNPHW LPPPGFYTGG FEVPEGNDGF LWDDIDDSVF 

       430        440        450        460        470        480 
SPQPQTLLEL QQREQAEAAL RKESFRRPSS LSDLGAAAPR SDASSPFPSL IGSLTSTRTT 

       490        500        510        520        530        540 
RPRLLGEEEY LNNSLLQPQR EKNLPPAFPN NGIESLVDKM SRWKTYAQEH RDVPGPRPPT 

       550        560        570        580 
RRQRHDRQRG LVWEDDDSAD DSSVLDLGGS GNPFAHLRPR LGRMF 

« Hide

References

[1]"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].
[2]"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].
[3]"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.
[4]"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.
[5]"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.
[6]"Latest insights on adenovirus structure and assembly."
San Martin C.
Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[7]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73260 Genomic DNA. Translation: AAA96407.1.
M22141 Genomic DNA. Translation: AAA42518.1.
PIRSXADH5. B39449.
RefSeqAP_000205.1. AC_000008.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYNelectron microscopy-N1-585[»]
ProteinModelPortalP12537.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR003479. Hex_IIIa.
[Graphical view]
PfamPF02455. Hex_IIIa. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12537.

Entry information

Entry nameCAP3_ADE05
AccessionPrimary (citable) accession number: P12537
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: March 1, 1992
Last modified: February 19, 2014
This is version 50 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references