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P04133

- CAPSH_ADE05

UniProt

P04133 - CAPSH_ADE05

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Protein

Hexon protein

Gene

L3

Organism
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei777 – 7771Involved in interaction with pre-protein VIBy similarity

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. microtubule-dependent intracellular transport of viral material towards nucleus Source: UniProtKB-KW
  2. viral entry into host cell Source: UniProtKB-KW
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]
ProteomesiUP000004992: 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

  1. host cell nucleus Source: UniProtKB-KW
  2. intracellular Source: GOC
  3. T=25 icosahedral viral capsid Source: UniProtKB-KW
  4. 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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 952951Hexon proteinPRO_0000221816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine; by hostBy similarity
Modified residuei175 – 1751Phosphoserine; by hostBy similarity
Modified residuei940 – 9401Phosphotyrosine; by hostBy similarity

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 interactions.
MINTiMINT-6597435.

Structurei

Secondary structure

1
952
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 124Combined 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 strandi100 – 1089Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi183 – 1875Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi192 – 1954Combined sources
Turni198 – 2003Combined sources
Beta strandi209 – 2124Combined sources
Beta strandi217 – 2248Combined sources
Beta strandi226 – 2283Combined sources
Turni243 – 2453Combined sources
Turni254 – 2563Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi283 – 2897Combined sources
Beta strandi298 – 3025Combined sources
Beta strandi306 – 3094Combined sources
Helixi312 – 3165Combined sources
Beta strandi318 – 3214Combined sources
Beta strandi327 – 3293Combined sources
Helixi331 – 3333Combined sources
Helixi342 – 3443Combined sources
Beta strandi347 – 3504Combined sources
Turni351 – 3533Combined sources
Helixi366 – 37712Combined sources
Helixi385 – 3873Combined sources
Helixi396 – 3994Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi415 – 4173Combined sources
Beta strandi424 – 4263Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi444 – 4463Combined sources
Beta strandi450 – 4523Combined sources
Helixi464 – 47613Combined sources
Helixi478 – 4803Combined sources
Helixi483 – 4853Combined sources
Helixi501 – 5066Combined sources
Helixi511 – 5144Combined sources
Turni516 – 5216Combined sources
Helixi527 – 5304Combined sources
Beta strandi536 – 5405Combined sources
Helixi541 – 55010Combined sources
Beta strandi552 – 56312Combined sources
Turni567 – 5715Combined sources
Beta strandi576 – 58611Combined sources
Helixi589 – 5924Combined sources
Beta strandi593 – 5975Combined sources
Turni601 – 6055Combined sources
Beta strandi607 – 61812Combined sources
Helixi624 – 63411Combined sources
Helixi637 – 6393Combined sources
Beta strandi641 – 6444Combined sources
Beta strandi649 – 6568Combined sources
Beta strandi662 – 6709Combined sources
Beta strandi677 – 6848Combined sources
Helixi685 – 6873Combined sources
Beta strandi692 – 6943Combined sources
Helixi706 – 7094Combined sources
Helixi715 – 7173Combined sources
Beta strandi718 – 7258Combined sources
Turni726 – 7283Combined sources
Beta strandi729 – 7324Combined sources
Beta strandi737 – 7393Combined sources
Beta strandi742 – 7443Combined sources
Helixi749 – 7546Combined sources
Beta strandi759 – 7624Combined sources
Helixi763 – 77412Combined sources
Beta strandi777 – 7793Combined sources
Helixi786 – 7883Combined sources
Helixi794 – 7974Combined sources
Beta strandi798 – 8069Combined sources
Turni808 – 8103Combined sources
Turni819 – 8213Combined sources
Turni826 – 8283Combined sources
Beta strandi831 – 8355Combined sources
Beta strandi858 – 8669Combined sources
Beta strandi871 – 8766Combined sources
Beta strandi882 – 8854Combined sources
Helixi888 – 8903Combined sources
Helixi892 – 8965Combined sources
Beta strandi899 – 9079Combined sources
Beta strandi914 – 9218Combined sources
Beta strandi923 – 9297Combined sources
Turni932 – 9343Combined sources
Beta strandi937 – 9459Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4CWUX-ray3.80A/B/C/D/E/F/G/H/I/J/K/L1-952[»]
ProteinModelPortaliP04133.
SMRiP04133. Positions 6-947.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04133.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi134 – 15926Asp/Glu-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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2731T → A no nucleotide entry (PubMed:23142869)Curated
Sequence conflicti930 – 9301R → Q no nucleotide entry (PubMed:23142869)Curated

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 .
PIRi A03849. HXAD5.
RefSeqi AP_000211.1. AC_000008.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P30 X-ray 2.50 A 2-952 [» ]
1VSZ X-ray 3.50 A/B/C/D/E/F/G/H/I/J/K/L 1-952 [» ]
2BVI electron microscopy 10.00 F/G/H/I/J/K/L/M/N/O/P/Q 2-952 [» ]
3IYN electron microscopy - A/B/C/D/E/F/G/H/I/J/K/L 1-952 [» ]
3TG7 X-ray 1.57 A 2-952 [» ]
4CWU X-ray 3.80 A/B/C/D/E/F/G/H/I/J/K/L 1-952 [» ]
ProteinModelPortali P04133.
SMRi P04133. Positions 6-947.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P04133. 2 interactions.
MINTi MINT-6597435.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P04133.

Family and domain databases

Gene3Di 2.70.9.10. 2 hits.
3.90.249.10. 3 hits.
InterProi IPR016108. Adenovirus_Pll_hexon_C.
IPR016107. Adenovirus_Pll_hexon_N.
IPR016110. Adenovirus_Pll_hexon_sub3.
IPR016111. Hexon_subdom4.
IPR016112. VP_dsDNA_II.
[Graphical view ]
Pfami PF01065. Adeno_hexon. 1 hit.
PF03678. Adeno_hexon_C. 1 hit.
[Graphical view ]
SUPFAMi SSF49749. SSF49749. 2 hits.
ProtoNeti Search...

Publicationsi

  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.

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 26, 2014
This is version 102 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

External Data

Dasty 3