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P12537

- CAP3_ADE05

UniProt

P12537 - CAP3_ADE05

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Protein

Pre-capsid vertex protein

Gene
L1
Organism
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 3.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei15 – 162Cleavage; by viral protease By similarity

GO - Biological processi

  1. viral release from host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Viral genome packaging, Virus exit from host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-capsid vertex protein
Alternative name(s):
Capsid vertex-specific component IIIa
Short name:
CVSC
Protein IIIa
pIIIa
Cleaved into the following chain:
Gene namesi
ORF Names:L1
OrganismiHuman adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Taxonomic identifieri28285 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000004992: Genome

Subcellular locationi

Chain Pre-capsid vertex protein : Host nucleus Inferred 2 Publications
Chain 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.2 Publications

GO - Cellular componenti

  1. host cell nucleus Source: UniProtKB-SubCell
  2. viral capsid Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 585585Pre-capsid vertex proteinPRO_0000221835Add
BLAST
Propeptidei1 – 1515 By similarityPRO_0000421129Add
BLAST
Chaini16 – 585570Capsid vertex protein By similarityPRO_0000421130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei225 – 2251Phosphoserine; by host By similarity
Modified residuei274 – 2741Phosphothreonine; by host By similarity
Modified residuei310 – 3101Phosphoserine; by host By similarity
Modified residuei444 – 4441Phosphoserine; by host By similarity
Modified residuei449 – 4491Phosphoserine; by host By similarity
Modified residuei450 – 4501Phosphoserine; by host By similarity
Modified residuei452 – 4521Phosphoserine; by host By similarity
Modified residuei469 – 4691Phosphoserine; by host By similarity
Modified residuei473 – 4731Phosphoserine; by host By similarity
Modified residuei490 – 4901Phosphotyrosine; by host By similarity
Modified residuei494 – 4941Phosphoserine; by host By similarity
Modified residuei515 – 5151Phosphoserine; by host By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

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).2 Publications

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYNelectron microscopy-N1-585[»]
ProteinModelPortaliP12537.

Miscellaneous databases

EvolutionaryTraceiP12537.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 106106Peripentonal hexon-tethering domain By similarityAdd
BLAST
Regioni138 – 251114Binding to hexon-linking protein By similarityAdd
BLAST

Sequence similaritiesi

Family and domain databases

InterProiIPR003479. Hex_IIIa.
[Graphical view]
PfamiPF02455. Hex_IIIa. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12537-1 [UniParc]FASTAAdd to Basket

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MMQDATDPAV RAALQSQPSG LNSTDDWRQV MDRIMSLTAR NPDAFRQQPQ    50
ANRLSAILEA VVPARANPTH EKVLAIVNAL AENRAIRPDE AGLVYDALLQ 100
RVARYNSGNV QTNLDRLVGD VREAVAQRER AQQQGNLGSM VALNAFLSTQ 150
PANVPRGQED YTNFVSALRL MVTETPQSEV YQSGPDYFFQ TSRQGLQTVN 200
LSQAFKNLQG LWGVRAPTGD RATVSSLLTP NSRLLLLLIA PFTDSGSVSR 250
DTYLGHLLTL YREAIGQAHV DEHTFQEITS VSRALGQEDT GSLEATLNYL 300
LTNRRQKIPS LHSLNSEEER ILRYVQQSVS LNLMRDGVTP SVALDMTARN 350
MEPGMYASNR PFINRLMDYL HRAAAVNPEY FTNAILNPHW LPPPGFYTGG 400
FEVPEGNDGF LWDDIDDSVF SPQPQTLLEL QQREQAEAAL RKESFRRPSS 450
LSDLGAAAPR SDASSPFPSL IGSLTSTRTT RPRLLGEEEY LNNSLLQPQR 500
EKNLPPAFPN NGIESLVDKM SRWKTYAQEH RDVPGPRPPT RRQRHDRQRG 550
LVWEDDDSAD DSSVLDLGGS GNPFAHLRPR LGRMF 585
Length:585
Mass (Da):65,253
Last modified:March 1, 1992 - v2
Checksum:i430113688C473F1D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73260 Genomic DNA. Translation: AAA96407.1.
M22141 Genomic DNA. Translation: AAA42518.1.
PIRiB39449. SXADH5.
RefSeqiAP_000205.1. AC_000008.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73260 Genomic DNA. Translation: AAA96407.1 .
M22141 Genomic DNA. Translation: AAA42518.1 .
PIRi B39449. SXADH5.
RefSeqi AP_000205.1. AC_000008.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IYN electron microscopy - N 1-585 [» ]
ProteinModelPortali P12537.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P12537.

Family and domain databases

InterProi IPR003479. Hex_IIIa.
[Graphical view ]
Pfami PF02455. Hex_IIIa. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCAP3_ADE05
AccessioniPrimary (citable) accession number: P12537
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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