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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)DescriptionActionsGraphical viewLength
Sitei793Involved in interaction with pre-protein VIBy similarity1

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by host2 Publications
ChainiPRO_00002218132 – 968Hexon proteinAdd BLAST967

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine; by host1 Publication1
Modified residuei182Phosphoserine; by host1 Publication1
Modified residuei283Phosphoserine; by host1 Publication1
Modified residuei956Phosphotyrosine; by host1 Publication1

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

1968
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 12Combined sources6
Beta strandi15 – 17Combined sources3
Helixi20 – 23Combined sources4
Helixi26 – 35Combined sources10
Turni36 – 38Combined sources3
Helixi42 – 44Combined sources3
Beta strandi54 – 57Combined sources4
Beta strandi64 – 68Combined sources5
Beta strandi71 – 75Combined sources5
Beta strandi77 – 88Combined sources12
Helixi96 – 98Combined sources3
Beta strandi99 – 108Combined sources10
Beta strandi116 – 118Combined sources3
Beta strandi132 – 135Combined sources4
Beta strandi174 – 176Combined sources3
Beta strandi190 – 192Combined sources3
Turni209 – 211Combined sources3
Beta strandi220 – 223Combined sources4
Beta strandi228 – 235Combined sources8
Beta strandi274 – 278Combined sources5
Beta strandi296 – 301Combined sources6
Beta strandi310 – 314Combined sources5
Beta strandi316 – 319Combined sources4
Helixi325 – 328Combined sources4
Beta strandi330 – 333Combined sources4
Beta strandi339 – 341Combined sources3
Helixi343 – 345Combined sources3
Helixi354 – 356Combined sources3
Beta strandi359 – 362Combined sources4
Turni363 – 365Combined sources3
Beta strandi367 – 369Combined sources3
Helixi378 – 389Combined sources12
Helixi397 – 399Combined sources3
Helixi408 – 411Combined sources4
Beta strandi412 – 414Combined sources3
Beta strandi424 – 426Combined sources3
Beta strandi436 – 438Combined sources3
Beta strandi466 – 468Combined sources3
Beta strandi476 – 478Combined sources3
Helixi480 – 492Combined sources13
Helixi494 – 496Combined sources3
Helixi499 – 501Combined sources3
Beta strandi506 – 508Combined sources3
Helixi517 – 522Combined sources6
Helixi527 – 530Combined sources4
Turni532 – 537Combined sources6
Helixi543 – 546Combined sources4
Helixi557 – 566Combined sources10
Beta strandi568 – 578Combined sources11
Turni583 – 587Combined sources5
Beta strandi592 – 602Combined sources11
Helixi605 – 608Combined sources4
Beta strandi609 – 613Combined sources5
Turni617 – 621Combined sources5
Beta strandi623 – 634Combined sources12
Helixi640 – 650Combined sources11
Helixi653 – 655Combined sources3
Beta strandi657 – 660Combined sources4
Beta strandi665 – 672Combined sources8
Beta strandi678 – 686Combined sources9
Beta strandi693 – 700Combined sources8
Helixi701 – 703Combined sources3
Beta strandi708 – 710Combined sources3
Helixi722 – 725Combined sources4
Helixi731 – 733Combined sources3
Beta strandi734 – 741Combined sources8
Turni742 – 744Combined sources3
Beta strandi745 – 748Combined sources4
Beta strandi753 – 755Combined sources3
Beta strandi758 – 760Combined sources3
Helixi765 – 770Combined sources6
Beta strandi775 – 778Combined sources4
Helixi779 – 790Combined sources12
Turni802 – 804Combined sources3
Helixi810 – 813Combined sources4
Beta strandi815 – 822Combined sources8
Turni824 – 826Combined sources3
Helixi835 – 837Combined sources3
Turni842 – 844Combined sources3
Beta strandi847 – 851Combined sources5
Beta strandi866 – 868Combined sources3
Beta strandi874 – 881Combined sources8
Beta strandi887 – 890Combined sources4
Helixi904 – 906Combined sources3
Helixi908 – 910Combined sources3
Beta strandi915 – 923Combined sources9
Beta strandi930 – 937Combined sources8
Beta strandi939 – 945Combined sources7
Beta strandi953 – 961Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP03277.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi134 – 162Glu-rich (acidic)Add BLAST29

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. 2 hits.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P2ZX-ray2.20A2-968[»]
ProteinModelPortaliP03277.
SMRiP03277.
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. 2 hits.
PF03678. Adeno_hexon_C. 1 hit.
[Graphical view]
SUPFAMiSSF49749. SSF49749. 2 hits.
ProtoNetiSearch...

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: November 30, 2016
This is version 112 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.