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Protein

Pre-hexon-linking protein IIIa

Gene

L1

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

Functioni

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 3.3 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Viral genome packaging, Virus exit from host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-hexon-linking protein IIIa
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]
Proteomesi
  • UP000004992 Componenti: Genome

Subcellular locationi

Hexon-linking protein IIIa :

GO - Cellular componenti

  • host cell nucleus Source: UniProtKB-SubCell
  • viral capsid Source: CACAO
  • viral capsid, decoration Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Capsid decoration protein, Capsid protein, Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 585585Pre-hexon-linking protein IIIaPRO_0000221835Add
BLAST
Chaini1 – 570570Hexon-linking protein IIIaPRO_0000421130Add
BLAST
Propeptidei571 – 58515By similarityPRO_0000421129Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei570 – 5712Cleavage; by viral proteaseBy 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 hexon proteins; this interaction tethers the peripentonal hexons to hexons situated in the facet (PubMed:20798312, PubMed:25071205). Interacts with the penton protein (via N-terminus) (PubMed:20798312). Interacts with packaging protein 3; this interaction is required to promote correct genome packaging (PubMed:21632753).3 Publications

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYNelectron microscopy-N1-585[»]
4CWUX-ray3.80O1-585[»]
ProteinModelPortaliP12537.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12537.

Family & Domainsi

Region

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

« Hide

        10         20         30         40         50
MMQDATDPAV RAALQSQPSG LNSTDDWRQV MDRIMSLTAR NPDAFRQQPQ
60 70 80 90 100
ANRLSAILEA VVPARANPTH EKVLAIVNAL AENRAIRPDE AGLVYDALLQ
110 120 130 140 150
RVARYNSGNV QTNLDRLVGD VREAVAQRER AQQQGNLGSM VALNAFLSTQ
160 170 180 190 200
PANVPRGQED YTNFVSALRL MVTETPQSEV YQSGPDYFFQ TSRQGLQTVN
210 220 230 240 250
LSQAFKNLQG LWGVRAPTGD RATVSSLLTP NSRLLLLLIA PFTDSGSVSR
260 270 280 290 300
DTYLGHLLTL YREAIGQAHV DEHTFQEITS VSRALGQEDT GSLEATLNYL
310 320 330 340 350
LTNRRQKIPS LHSLNSEEER ILRYVQQSVS LNLMRDGVTP SVALDMTARN
360 370 380 390 400
MEPGMYASNR PFINRLMDYL HRAAAVNPEY FTNAILNPHW LPPPGFYTGG
410 420 430 440 450
FEVPEGNDGF LWDDIDDSVF SPQPQTLLEL QQREQAEAAL RKESFRRPSS
460 470 480 490 500
LSDLGAAAPR SDASSPFPSL IGSLTSTRTT RPRLLGEEEY LNNSLLQPQR
510 520 530 540 550
EKNLPPAFPN NGIESLVDKM SRWKTYAQEH RDVPGPRPPT RRQRHDRQRG
560 570 580
LVWEDDDSAD DSSVLDLGGS GNPFAHLRPR LGRMF
Length:585
Mass (Da):65,253
Last modified:March 1, 1992 - v2
Checksum:i430113688C473F1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. Translation: AAA96407.1.
M22141 Genomic DNA. Translation: AAA42518.1.
PIRiB39449. SXADH5.
RefSeqiAP_000205.1. AC_000008.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYNelectron microscopy-N1-585[»]
4CWUX-ray3.80O1-585[»]
ProteinModelPortaliP12537.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP12537.

Family and domain databases

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

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 THE HEXON PROTEIN, INTERACTION WITH THE PENTON PROTEIN.
  8. "Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection."
    Reddy V.S., Nemerow G.R.
    Proc. Natl. Acad. Sci. U.S.A. 111:11715-11720(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS), INTERACTION WITH THE HEXON PROTEIN, FUNCTION, SUBCELLULAR LOCATION.

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: June 8, 2016
This is version 56 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.

Caution

An interaction between hexon-linking protein IIIa and hexon-linking protein VIII as been described in PubMed:20798312. However, the subcellular location of hexon-linking protein IIIa was incorrectly assigned to the capsid interior.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.