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Protein

Hexon protein

Gene

L3

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

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei777Involved 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 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

  • 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).By similarity

GO - Cellular componenti

  • host cell nucleus Source: UniProtKB-SubCell
  • T=25 icosahedral viral capsid Source: UniProtKB-KW
  • viral capsid Source: CACAO
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 hostBy similarity
ChainiPRO_00002218162 – 952Hexon proteinAdd BLAST951

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine; by hostBy similarity1
Modified residuei175Phosphoserine; by hostBy similarity1
Modified residuei940Phosphotyrosine; by hostBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

IntActiP04133. 2 interactors.
MINTiMINT-6597435.

Structurei

Secondary structure

1952
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 12Combined sources4
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 strandi100 – 108Combined sources9
Beta strandi116 – 118Combined sources3
Beta strandi132 – 135Combined sources4
Beta strandi167 – 169Combined sources3
Beta strandi183 – 187Combined sources5
Beta strandi192 – 195Combined sources4
Turni198 – 200Combined sources3
Beta strandi209 – 212Combined sources4
Beta strandi217 – 224Combined sources8
Beta strandi263 – 267Combined sources5
Beta strandi283 – 289Combined sources7
Beta strandi298 – 302Combined sources5
Helixi312 – 316Combined sources5
Beta strandi318 – 321Combined sources4
Beta strandi327 – 329Combined sources3
Helixi331 – 333Combined sources3
Helixi342 – 344Combined sources3
Beta strandi347 – 350Combined sources4
Turni351 – 353Combined sources3
Helixi366 – 377Combined sources12
Helixi385 – 387Combined sources3
Helixi396 – 399Combined sources4
Beta strandi400 – 402Combined sources3
Beta strandi424 – 426Combined sources3
Beta strandi444 – 446Combined sources3
Beta strandi450 – 452Combined sources3
Helixi464 – 476Combined sources13
Helixi478 – 480Combined sources3
Helixi483 – 485Combined sources3
Helixi501 – 506Combined sources6
Helixi511 – 514Combined sources4
Turni516 – 521Combined sources6
Helixi527 – 530Combined sources4
Helixi541 – 550Combined sources10
Beta strandi552 – 563Combined sources12
Turni567 – 571Combined sources5
Beta strandi576 – 586Combined sources11
Helixi589 – 592Combined sources4
Beta strandi593 – 597Combined sources5
Turni601 – 605Combined sources5
Beta strandi607 – 618Combined sources12
Helixi624 – 634Combined sources11
Helixi637 – 639Combined sources3
Beta strandi641 – 644Combined sources4
Beta strandi649 – 656Combined sources8
Beta strandi662 – 670Combined sources9
Beta strandi677 – 684Combined sources8
Helixi685 – 687Combined sources3
Beta strandi692 – 694Combined sources3
Helixi706 – 709Combined sources4
Helixi715 – 717Combined sources3
Beta strandi718 – 725Combined sources8
Turni726 – 728Combined sources3
Beta strandi729 – 732Combined sources4
Beta strandi737 – 739Combined sources3
Beta strandi742 – 744Combined sources3
Helixi749 – 754Combined sources6
Beta strandi759 – 762Combined sources4
Helixi763 – 774Combined sources12
Beta strandi777 – 779Combined sources3
Helixi786 – 788Combined sources3
Helixi794 – 797Combined sources4
Beta strandi798 – 806Combined sources9
Turni808 – 810Combined sources3
Turni819 – 821Combined sources3
Turni826 – 828Combined sources3
Beta strandi831 – 835Combined sources5
Beta strandi858 – 866Combined sources9
Beta strandi871 – 876Combined sources6
Helixi888 – 890Combined sources3
Helixi892 – 896Combined sources5
Beta strandi899 – 907Combined sources9
Beta strandi914 – 921Combined sources8
Beta strandi923 – 929Combined sources7
Beta strandi937 – 945Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P30X-ray2.50A2-952[»]
3IYNelectron microscopy-A/B/C/D/E/F/G/H/I/J/K/L1-952[»]
3TG7X-ray1.57A2-952[»]
4CWUX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L1-952[»]
4V4Uelectron microscopy10.00F/G/H/I/J/K/L/M/N/O/P/Q2-952[»]
ProteinModelPortaliP04133.
SMRiP04133.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04133.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi134 – 159Asp/Glu-rich (acidic)Add BLAST26

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.

P04133-1 [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 NPCEWDEAAT ALEINLEEED
160 170 180 190 200
DDNEDEVDEQ AEQQKTHVFG QAPYSGINIT KEGIQIGVEG QTPKYADKTF
210 220 230 240 250
QPEPQIGESQ WYETEINHAA GRVLKKTTPM KPCYGSYAKP TNENGGQGIL
260 270 280 290 300
VKQQNGKLES QVEMQFFSTT EATAGNGDNL TPKVVLYSED VDIETPDTHI
310 320 330 340 350
SYMPTIKEGN SRELMGQQSM PNRPNYIAFR DNFIGLMYYN STGNMGVLAG
360 370 380 390 400
QASQLNAVVD LQDRNTELSY QLLLDSIGDR TRYFSMWNQA VDSYDPDVRI
410 420 430 440 450
IENHGTEDEL PNYCFPLGGV INTETLTKVK PKTGQENGWE KDATEFSDKN
460 470 480 490 500
EIRVGNNFAM EINLNANLWR NFLYSNIALY LPDKLKYSPS NVKISDNPNT
510 520 530 540 550
YDYMNKRVVA PGLVDCYINL GARWSLDYMD NVNPFNHHRN AGLRYRSMLL
560 570 580 590 600
GNGRYVPFHI QVPQKFFAIK NLLLLPGSYT YEWNFRKDVN MVLQSSLGND
610 620 630 640 650
LRVDGASIKF DSICLYATFF PMAHNTASTL EAMLRNDTND QSFNDYLSAA
660 670 680 690 700
NMLYPIPANA TNVPISIPSR NWAAFRGWAF TRLKTKETPS LGSGYDPYYT
710 720 730 740 750
YSGSIPYLDG TFYLNHTFKK VAITFDSSVS WPGNDRLLTP NEFEIKRSVD
760 770 780 790 800
GEGYNVAQCN MTKDWFLVQM LANYNIGYQG FYIPESYKDR MYSFFRNFQP
810 820 830 840 850
MSRQVVDDTK YKDYQQVGIL HQHNNSGFVG YLAPTMREGQ AYPANFPYPL
860 870 880 890 900
IGKTAVDSIT QKKFLCDRTL WRIPFSSNFM SMGALTDLGQ NLLYANSAHA
910 920 930 940 950
LDMTFEVDPM DEPTLLYVLF EVFDVVRVHR PHRGVIETVY LRTPFSAGNA

TT
Length:952
Mass (Da):108,007
Last modified:January 23, 2007 - v3
Checksum:i822CCDE26E970C5A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti273T → A no nucleotide entry (PubMed:23142869).Curated1
Sequence conflicti930R → Q no nucleotide entry (PubMed:23142869).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. No translation available.
X02997 Genomic DNA. Translation: CAA26753.1.
PIRiA03849. HXAD5.
RefSeqiAP_000211.1. AC_000008.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. No translation available.
X02997 Genomic DNA. Translation: CAA26753.1.
PIRiA03849. HXAD5.
RefSeqiAP_000211.1. AC_000008.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P30X-ray2.50A2-952[»]
3IYNelectron microscopy-A/B/C/D/E/F/G/H/I/J/K/L1-952[»]
3TG7X-ray1.57A2-952[»]
4CWUX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L1-952[»]
4V4Uelectron microscopy10.00F/G/H/I/J/K/L/M/N/O/P/Q2-952[»]
ProteinModelPortaliP04133.
SMRiP04133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04133. 2 interactors.
MINTiMINT-6597435.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP04133.

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...

Entry informationi

Entry nameiCAPSH_ADE05
AccessioniPrimary (citable) accession number: P04133
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 115 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 (By similarity).By similarity

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.