Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P42671 (CAPSH_ADEG1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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
OrganismFowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian adenovirus gal1 (strain Phelps)) [Reference proteome]
Taxonomic identifier10553 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageAdenoviridaeAviadenovirusFowl adenovirus A
Virus hostGalliformes [TaxID: 8976]

Protein attributes

Sequence length942 AA.
Sequence statusComplete.
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. 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 By similarity.

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. Interacts with pre-protein VI; this interaction probably allows nuclear import of hexon trimers and possibly pre-capsid assembly By similarity.

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

Chain1 – 942942Hexon protein
PRO_0000221826

Amino acid modifications

Modified residue9311Phosphotyrosine; by host By similarity

Secondary structure

..................................................................................................................................................... 942
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42671 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 7F4CE8D3F17D051B

FASTA942106,709
        10         20         30         40         50         60 
MTALTPDLTT ATPRLQYFHI AGPGTREYLS EDLQQFISAT GSYFDLKNKF RQTVVAPTRN 

        70         80         90        100        110        120 
VTTEKAQRLQ IRFYPIQTDD TPNSYRVRYS VNVGDSWVLD MGATYFDIKG VLDRGPSFKP 

       130        140        150        160        170        180 
YGGTAYNPLA PREAIFNTWV ESTGPQTNVV GQMTNVYTNQ TRNDKTATLQ QVNSISGVVP 

       190        200        210        220        230        240 
NVNLGPGLSQ LASRADVDNI GVVGRFAKVD SAGVKQAYGA YVKPVKDDGS QSLNQTAYWL 

       250        260        270        280        290        300 
MDNGGTNYLG ALAVEDYTQT LSYPDTVLVT PPTAYQQVNS GTMRACRPNY IGFRDNFINL 

       310        320        330        340        350        360 
LYHDSGVCSG TLNSERSGMN VVVELQDRNT ELSYQYMLAD MMSRHHYFAL WNQAVDQYDH 

       370        380        390        400        410        420 
DVRVFNNDGY EEGVPTYAFL PDGHGAGEDN GPDLSNVKIY TNGQQDKGNV VAGTVSTQLN 

       430        440        450        460        470        480 
FGTIPSYEID IAAATRRNFI MSNIADYLPD KYKFSIRGFD PVTDNIDPTT YFYMNRRVPL 

       490        500        510        520        530        540 
TNVVDLFTNI GARWSVDQMD NVNPFNHHRN WGLKYRSQLL GNSRYCRFHI QVPQKYFAIK 

       550        560        570        580        590        600 
NLLLLPGTYT YEWVLRKDPN MILQSSLGND LRADGAQIVY TEVNLMANFM PMDHNTSNQL 

       610        620        630        640        650        660 
ELMLRNATND QTFADYLGAK NALYNVPAGS TLLTINIPAR TWEGMRGWSF TRLKASETPQ 

       670        680        690        700        710        720 
LGAQYDVGFK YSGSIPYSDG TFYLSHTFRS MSVLFDTSIN WPGNDRLLTP NLFEIKRPVA 

       730        740        750        760        770        780 
TDSEGFTMSQ CDMTKDWFLV QMATNYNYVY NGYRFWPDRH YFHYDFLRNF DPMSRQGPNF 

       790        800        810        820        830        840 
LDTTLYDLVS STPVVNDTGS QPSQDNVRNN SGFIAPRSWP VWTAQQGEAW PANWPYPLIG 

       850        860        870        880        890        900 
NDAISSNQTV NYKKFLCDNY LWTVPFSSDF MYMGELTDLG QNPMYTNNSH SMVINFELDP 

       910        920        930        940 
MDENTYVYML YGVFDTVRVN QPERNVLAMA YFRTPFATGN AV 

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence and genomic organization of the avian adenovirus CELO."
Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.
J. Virol. 70:2939-2949(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Organization of the avian adenovirus genome and the structure of its endopeptidase."
Cai F., Weber J.M.
Virology 196:358-362(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 913-942.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U46933 Genomic DNA. Translation: AAC54912.1.
L13161 Genomic DNA. Translation: AAA51401.1.
RefSeqNP_043886.1. NC_001720.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2INYX-ray3.90A1-942[»]
ProteinModelPortalP42671.
SMRP42671. Positions 2-942.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1476562.

Phylogenomic databases

ProtClustDBCLSP2513880.

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

EvolutionaryTraceP42671.

Entry information

Entry nameCAPSH_ADEG1
AccessionPrimary (citable) accession number: P42671
Secondary accession number(s): Q64758
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: February 19, 2014
This is version 73 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