Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hexon protein

Gene

L3

Organism
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei793 – 7931Involved in interaction with pre-protein VIBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cytoplasmic inwards viral transport, Host-virus interaction, Microtubular inwards viral transport, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Hexon protein
Short name:
CP-H
Alternative name(s):
Protein II
Gene namesi
ORF Names:L3
OrganismiHuman adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Taxonomic identifieri10515 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008167 Componenti: Genome

Subcellular locationi

  • Virion 1 Publication
  • Host nucleus 1 Publication

  • Note: Forms the capsid icosahedric shell. Present in 720 copies per virion, assembled in 240 trimers.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host nucleus, T=25 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved; by host2 Publications
Chaini2 – 968967Hexon proteinPRO_0000221813Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine; by host1 Publication
Modified residuei182 – 1821Phosphoserine; by host1 Publication
Modified residuei283 – 2831Phosphoserine; by host1 Publication
Modified residuei956 – 9561Phosphotyrosine; by host1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

PTM databases

iPTMnetiP03277.

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Homotrimer. 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 pre-protein VI; this interaction probably allows nuclear import of hexon trimers and possibly pre-capsid assembly. 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.6 Publications

Structurei

Secondary structure

1
968
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 126Combined sources
Beta strandi15 – 173Combined sources
Helixi20 – 234Combined sources
Helixi26 – 3510Combined sources
Turni36 – 383Combined sources
Helixi42 – 443Combined sources
Beta strandi54 – 574Combined sources
Beta strandi64 – 685Combined sources
Beta strandi71 – 755Combined sources
Beta strandi77 – 8812Combined sources
Helixi96 – 983Combined sources
Beta strandi99 – 10810Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi190 – 1923Combined sources
Turni209 – 2113Combined sources
Beta strandi220 – 2234Combined sources
Beta strandi228 – 2358Combined sources
Beta strandi274 – 2785Combined sources
Beta strandi296 – 3016Combined sources
Beta strandi310 – 3145Combined sources
Beta strandi316 – 3194Combined sources
Helixi325 – 3284Combined sources
Beta strandi330 – 3334Combined sources
Beta strandi339 – 3413Combined sources
Helixi343 – 3453Combined sources
Helixi354 – 3563Combined sources
Beta strandi359 – 3624Combined sources
Turni363 – 3653Combined sources
Beta strandi367 – 3693Combined sources
Helixi378 – 38912Combined sources
Helixi397 – 3993Combined sources
Helixi408 – 4114Combined sources
Beta strandi412 – 4143Combined sources
Beta strandi424 – 4263Combined sources
Beta strandi436 – 4383Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi476 – 4783Combined sources
Helixi480 – 49213Combined sources
Helixi494 – 4963Combined sources
Helixi499 – 5013Combined sources
Beta strandi506 – 5083Combined sources
Helixi517 – 5226Combined sources
Helixi527 – 5304Combined sources
Turni532 – 5376Combined sources
Helixi543 – 5464Combined sources
Helixi557 – 56610Combined sources
Beta strandi568 – 57811Combined sources
Turni583 – 5875Combined sources
Beta strandi592 – 60211Combined sources
Helixi605 – 6084Combined sources
Beta strandi609 – 6135Combined sources
Turni617 – 6215Combined sources
Beta strandi623 – 63412Combined sources
Helixi640 – 65011Combined sources
Helixi653 – 6553Combined sources
Beta strandi657 – 6604Combined sources
Beta strandi665 – 6728Combined sources
Beta strandi678 – 6869Combined sources
Beta strandi693 – 7008Combined sources
Helixi701 – 7033Combined sources
Beta strandi708 – 7103Combined sources
Helixi722 – 7254Combined sources
Helixi731 – 7333Combined sources
Beta strandi734 – 7418Combined sources
Turni742 – 7443Combined sources
Beta strandi745 – 7484Combined sources
Beta strandi753 – 7553Combined sources
Beta strandi758 – 7603Combined sources
Helixi765 – 7706Combined sources
Beta strandi775 – 7784Combined sources
Helixi779 – 79012Combined sources
Turni802 – 8043Combined sources
Helixi810 – 8134Combined sources
Beta strandi815 – 8228Combined sources
Turni824 – 8263Combined sources
Helixi835 – 8373Combined sources
Turni842 – 8443Combined sources
Beta strandi847 – 8515Combined sources
Beta strandi866 – 8683Combined sources
Beta strandi874 – 8818Combined sources
Beta strandi887 – 8904Combined sources
Helixi904 – 9063Combined sources
Helixi908 – 9103Combined sources
Beta strandi915 – 9239Combined sources
Beta strandi930 – 9378Combined sources
Beta strandi939 – 9457Combined sources
Beta strandi953 – 9619Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P2ZX-ray2.20A2-968[»]
ProteinModelPortaliP03277.
SMRiP03277. Positions 6-963.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03277.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi134 – 16229Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the adenoviridae hexon protein family.Curated

Family and domain databases

Gene3Di2.70.9.10. 2 hits.
3.90.249.10. 3 hits.
InterProiIPR016108. Adenovirus_Pll_hexon_C.
IPR016107. Adenovirus_Pll_hexon_N.
IPR016110. Adenovirus_Pll_hexon_sub3.
IPR016111. Hexon_subdom4.
IPR016112. VP_dsDNA_II.
[Graphical view]
PfamiPF01065. Adeno_hexon. 1 hit.
PF03678. Adeno_hexon_C. 1 hit.
[Graphical view]
SUPFAMiSSF49749. SSF49749. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P03277-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPSMMPQW SYMHISGQDA SEYLSPGLVQ FARATETYFS LNNKFRNPTV
60 70 80 90 100
APTHDVTTDR SQRLTLRFIP VDREDTAYSY KARFTLAVGD NRVLDMASTY
110 120 130 140 150
FDIRGVLDRG PTFKPYSGTA YNALAPKGAP NSCEWEQTED SGRAVAEDEE
160 170 180 190 200
EEDEDEEEEE EEQNARDQAT KKTHVYAQAP LSGETITKSG LQIGSDNAET
210 220 230 240 250
QAKPVYADPS YQPEPQIGES QWNEADANAA GGRVLKKTTP MKPCYGSYAR
260 270 280 290 300
PTNPFGGQSV LVPDEKGVPL PKVDLQFFSN TTSLNDRQGN ATKPKVVLYS
310 320 330 340 350
EDVNMETPDT HLSYKPGKGD ENSKAMLGQQ SMPNRPNYIA FRDNFIGLMY
360 370 380 390 400
YNSTGNMGVL AGQASQLNAV VDLQDRNTEL SYQLLLDSIG DRTRYFSMWN
410 420 430 440 450
QAVDSYDPDV RIIENHGTED ELPNYCFPLG GIGVTDTYQA IKANGNGSGD
460 470 480 490 500
NGDTTWTKDE TFATRNEIGV GNNFAMEINL NANLWRNFLY SNIALYLPDK
510 520 530 540 550
LKYNPTNVEI SDNPNTYDYM NKRVVAPGLV DCYINLGARW SLDYMDNVNP
560 570 580 590 600
FNHHRNAGLR YRSMLLGNGR YVPFHIQVPQ KFFAIKNLLL LPGSYTYEWN
610 620 630 640 650
FRKDVNMVLQ SSLGNDLRVD GASIKFDSIC LYATFFPMAH NTASTLEAML
660 670 680 690 700
RNDTNDQSFN DYLSAANMLY PIPANATNVP ISIPSRNWAA FRGWAFTRLK
710 720 730 740 750
TKETPSLGSG YDPYYTYSGS IPYLDGTFYL NHTFKKVAIT FDSSVSWPGN
760 770 780 790 800
DRLLTPNEFE IKRSVDGEGY NVAQCNMTKD WFLVQMLANY NIGYQGFYIP
810 820 830 840 850
ESYKDRMYSF FRNFQPMSRQ VVDDTKYKEY QQVGILHQHN NSGFVGYLAP
860 870 880 890 900
TMREGQAYPA NVPYPLIGKT AVDSITQKKF LCDRTLWRIP FSSNFMSMGA
910 920 930 940 950
LTDLGQNLLY ANSAHALDMT FEVDPMDEPT LLYVLFEVFD VVRVHQPHRG
960
VIETVYLRTP FSAGNATT
Length:968
Mass (Da):109,153
Last modified:January 23, 2007 - v3
Checksum:i78C1C61BEFB38452
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01917 Genomic DNA. Translation: AAA92215.1.
PIRiA94597. HXAD2.
RefSeqiAP_000175.1. AC_000007.1.
NP_040525.1. NC_001405.1.

Genome annotation databases

GeneIDi2652998.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01917 Genomic DNA. Translation: AAA92215.1.
PIRiA94597. HXAD2.
RefSeqiAP_000175.1. AC_000007.1.
NP_040525.1. NC_001405.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P2ZX-ray2.20A2-968[»]
ProteinModelPortaliP03277.
SMRiP03277. Positions 6-963.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP03277.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2652998.

Miscellaneous databases

EvolutionaryTraceiP03277.

Family and domain databases

Gene3Di2.70.9.10. 2 hits.
3.90.249.10. 3 hits.
InterProiIPR016108. Adenovirus_Pll_hexon_C.
IPR016107. Adenovirus_Pll_hexon_N.
IPR016110. Adenovirus_Pll_hexon_sub3.
IPR016111. Hexon_subdom4.
IPR016112. VP_dsDNA_II.
[Graphical view]
PfamiPF01065. Adeno_hexon. 1 hit.
PF03678. Adeno_hexon_C. 1 hit.
[Graphical view]
SUPFAMiSSF49749. SSF49749. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "The gene for the adenovirus 2 hexon polypeptide."
    Akusjaervi G., Alestroem P., Pettersson M., Lager M., Joernvall H., Pettersson U.
    J. Biol. Chem. 259:13976-13979(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The adenovirus hexon protein. The primary structure of the polypeptide and its correlation with the hexon gene."
    Joernvall H., Akusjaervi G., Alestroem P., von Bahr-Lindstroem H., Pettersson U., Appella E., Fowler A.V., Philipson L.
    J. Biol. Chem. 256:6181-6186(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-455 AND 457-968.
  3. Cited for: PROTEIN SEQUENCE OF 173-188; 273-287 AND 950-958, PHOSPHORYLATION AT SER-182; SER-283 AND TYR-956.
  4. "The sequence of the 3' non-coding region of the hexon mRNA discloses a novel adenovirus gene."
    Akusjaervi G., Zabielski J., Perricaudet M., Pettersson U.
    Nucleic Acids Res. 9:1-17(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 923-967.
  5. "Assembly of adenovirus major capsid protein is mediated by a nonvirion protein."
    Cepko C.L., Sharp P.A.
    Cell 31:407-415(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHUTOFF PROTEIN.
  6. "An acetylated N-terminus of adenovirus type 2 hexon protein."
    Joernvall H., Ohlsson H., Philipson L.
    Biochem. Biophys. Res. Commun. 56:304-310(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT ALA-2.
  7. "Adenovirus protein-protein interactions: molecular parameters governing the binding of protein VI to hexon and the activation of the adenovirus 23K protease."
    Matthews D.A., Russell W.C.
    J. Gen. Virol. 76:1959-1969(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRE-PROTEIN VI.
  8. "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.
  9. "The 100K-chaperone protein from adenovirus serotype 2 (Subgroup C) assists in trimerization and nuclear localization of hexons from subgroups C and B adenoviruses."
    Hong S.S., Szolajska E., Schoehn G., Franqueville L., Myhre S., Lindholm L., Ruigrok R.W., Boulanger P., Chroboczek J.
    J. Mol. Biol. 352:125-138(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE SHUTOFF PROTEIN.
  10. "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.
    Strain: Human adenovirus C serotype 5.
  11. "Latest insights on adenovirus structure and assembly."
    San Martin C.
    Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  12. "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 CAPSID VERTEX PROTEIN AND HEXON-LINKING PROTEIN.
    Strain: Human adenovirus C serotype 5.
  13. "The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9-A resolution."
    Athappilly F.K., Murali R., Rux J.J., Cai Z., Burnett R.M.
    J. Mol. Biol. 242:430-455(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

Entry informationi

Entry nameiCAPSH_ADE02
AccessioniPrimary (citable) accession number: P03277
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 107 of the entry and version 3 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, Direct protein sequencing, Reference 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.