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P04133 (CAPSH_ADE05) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. 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:
Hexon protein

Short name=CP-H
Alternative name(s):
Protein II
Gene names
ORF Names:L3
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 length952 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein By similarity. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus.

Subunit structure

Homotrimer By similarity. Interacts with the capsid vertex protein; this interaction binds the peripentonal hexons to the neighboring penton base. Interacts with the hexon-linking protein; this interaction tethers the hexons surrounding the penton to those situated in the central plate of the facet. Interacts with the hexon-interlacing protein; this interaction lashes the hexons together. Interacts with host dyneins DYNC1LI1 and DYNC1I2; this interaction might be involved in intracellular microtubule-dependent transport of incoming viral capsid. Interacts with the shutoff protein; this interaction allows folding and formation of hexons trimers By similarity. Interacts with pre-protein VI; this interaction probably allows nuclear import of hexon trimers and possibly pre-capsid assembly. Ref.4 Ref.5

Subcellular location

Virion By similarity. Host nucleus By similarity. Note: Forms the capsid icosahedric shell. Present in 720 copies per virion, assembled in 240 trimers By similarity.

Induction

Expressed in the late phase of the viral replicative cycle.

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 By similarity.

Sequence similarities

Belongs to the adenoviridae hexon protein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 952951Hexon protein
PRO_0000221816

Regions

Compositional bias134 – 15926Asp/Glu-rich (acidic)

Sites

Site7771Involved in interaction with pre-protein VI By similarity

Amino acid modifications

Modified residue21N-acetylalanine; by host By similarity
Modified residue1751Phosphoserine; by host By similarity
Modified residue9401Phosphotyrosine; by host By similarity

Experimental info

Sequence conflict2731T → A no nucleotide entry Ref.3
Sequence conflict9301R → Q no nucleotide entry Ref.3

Secondary structure

..................................................................................................................................................................................... 952
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04133 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 822CCDE26E970C5A

FASTA952108,007
        10         20         30         40         50         60 
MATPSMMPQW SYMHISGQDA SEYLSPGLVQ FARATETYFS LNNKFRNPTV APTHDVTTDR 

        70         80         90        100        110        120 
SQRLTLRFIP VDREDTAYSY KARFTLAVGD NRVLDMASTY FDIRGVLDRG PTFKPYSGTA 

       130        140        150        160        170        180 
YNALAPKGAP NPCEWDEAAT ALEINLEEED DDNEDEVDEQ AEQQKTHVFG QAPYSGINIT 

       190        200        210        220        230        240 
KEGIQIGVEG QTPKYADKTF QPEPQIGESQ WYETEINHAA GRVLKKTTPM KPCYGSYAKP 

       250        260        270        280        290        300 
TNENGGQGIL VKQQNGKLES QVEMQFFSTT EATAGNGDNL TPKVVLYSED VDIETPDTHI 

       310        320        330        340        350        360 
SYMPTIKEGN SRELMGQQSM PNRPNYIAFR DNFIGLMYYN STGNMGVLAG QASQLNAVVD 

       370        380        390        400        410        420 
LQDRNTELSY QLLLDSIGDR TRYFSMWNQA VDSYDPDVRI IENHGTEDEL PNYCFPLGGV 

       430        440        450        460        470        480 
INTETLTKVK PKTGQENGWE KDATEFSDKN EIRVGNNFAM EINLNANLWR NFLYSNIALY 

       490        500        510        520        530        540 
LPDKLKYSPS NVKISDNPNT YDYMNKRVVA PGLVDCYINL GARWSLDYMD NVNPFNHHRN 

       550        560        570        580        590        600 
AGLRYRSMLL GNGRYVPFHI QVPQKFFAIK NLLLLPGSYT YEWNFRKDVN MVLQSSLGND 

       610        620        630        640        650        660 
LRVDGASIKF DSICLYATFF PMAHNTASTL EAMLRNDTND QSFNDYLSAA NMLYPIPANA 

       670        680        690        700        710        720 
TNVPISIPSR NWAAFRGWAF TRLKTKETPS LGSGYDPYYT YSGSIPYLDG TFYLNHTFKK 

       730        740        750        760        770        780 
VAITFDSSVS WPGNDRLLTP NEFEIKRSVD GEGYNVAQCN MTKDWFLVQM LANYNIGYQG 

       790        800        810        820        830        840 
FYIPESYKDR MYSFFRNFQP MSRQVVDDTK YKDYQQVGIL HQHNNSGFVG YLAPTMREGQ 

       850        860        870        880        890        900 
AYPANFPYPL IGKTAVDSIT QKKFLCDRTL WRIPFSSNFM SMGALTDLGQ NLLYANSAHA 

       910        920        930        940        950 
LDMTFEVDPM DEPTLLYVLF EVFDVVRVHR PHRGVIETVY LRTPFSAGNA TT 

« Hide

References

[1]"Adenovirus hexon. Sequence comparison of subgroup C serotypes 2 and 5."
Kinloch R., MacKay N., Mautner V.
J. Biol. Chem. 259:6431-6436(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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].
[3]"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].
[4]"Switch from capsid protein import to adenovirus assembly by cleavage of nuclear transport signals."
Wodrich H., Guan T., Cingolani G., Von Seggern D., Nemerow G., Gerace L.
EMBO J. 22:6245-6255(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRE-PROTEIN VI.
Strain: Ad5 ts147 mutant and Human adenovirus C serotype 5.
[5]"Adenovirus transport via direct interaction of cytoplasmic dynein with the viral capsid hexon subunit."
Bremner K.H., Scherer J., Yi J., Vershinin M., Gross S.P., Vallee R.B.
Cell Host Microbe 6:523-535(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN DYNEINS DYNC1LI1 AND DYNC1I2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73260 Genomic DNA. No translation available.
X02997 Genomic DNA. Translation: CAA26753.1.
PIRHXAD5. A03849.
RefSeqAP_000211.1. AC_000008.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P30X-ray2.50A2-952[»]
1VSZX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L1-952[»]
2BVIelectron microscopy10.00F/G/H/I/J/K/L/M/N/O/P/Q2-952[»]
3IYNelectron microscopy-A/B/C/D/E/F/G/H/I/J/K/L1-952[»]
3TG7X-ray1.57A2-952[»]
ProteinModelPortalP04133.
SMRP04133. Positions 6-947.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP04133. 2 interactions.
MINTMINT-6597435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.70.9.10. 2 hits.
3.90.249.10. 3 hits.
InterProIPR016108. Adenovirus_Pll_hexon_C.
IPR016107. Adenovirus_Pll_hexon_N.
IPR016110. Adenovirus_Pll_hexon_sub3.
IPR016111. Hexon_subdom4.
IPR016112. VP_dsDNA_II.
[Graphical view]
PfamPF01065. Adeno_hexon. 1 hit.
PF03678. Adeno_hexon_C. 1 hit.
[Graphical view]
SUPFAMSSF49749. SSF49749. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP04133.

Entry information

Entry nameCAPSH_ADE05
AccessionPrimary (citable) accession number: P04133
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 99 of the entry and version 3 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