UniProtKB - P03277 (CAPSH_ADE02)
Hexon protein
L3
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.
UniRule annotation1 PublicationMiscellaneous
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 793 | Involved in interaction with pre-protein VIUniRule annotation | 1 |
GO - Molecular functioni
- structural molecule activity Source: UniProtKB-UniRule
GO - Biological processi
- microtubule-dependent intracellular transport of viral material towards nucleus Source: UniProtKB-UniRule
- viral entry into host cell Source: UniProtKB-UniRule
Keywordsi
Biological process | Cytoplasmic inwards viral transport, Host-virus interaction, Microtubular inwards viral transport, Virus entry into host cell |
Names & Taxonomyi
Protein namesi | Recommended name: Hexon proteinUniRule annotationShort name: CP-HUniRule annotation Alternative name(s): Protein IIUniRule annotation |
Gene namesi | Name:L3UniRule annotation |
Organismi | Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) |
Taxonomic identifieri | 10515 [NCBI] |
Taxonomic lineagei | Viruses › Varidnaviria › Bamfordvirae › Preplasmiviricota › Tectiliviricetes › Rowavirales › Adenoviridae › Mastadenovirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
- Virion UniRule annotation1 Publication
- Host nucleus UniRule annotation1 Publication Note: Forms the capsid icosahedric shell. Present in 720 copies per virion, assembled in 240 trimers.UniRule annotation
Keywords - Cellular componenti
Capsid protein, Host nucleus, T=25 icosahedral capsid protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostUniRule annotation2 Publications | |||
ChainiPRO_0000221813 | 2 – 968 | Hexon proteinUniRule annotationAdd BLAST | 967 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanine; by hostUniRule annotation1 Publication | 1 | |
Modified residuei | 182 | Phosphoserine; by hostUniRule annotation1 Publication | 1 | |
Modified residuei | 283 | Phosphoserine; by hostUniRule annotation1 Publication | 1 | |
Modified residuei | 956 | Phosphotyrosine; by host1 Publication | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinPTM databases
iPTMneti | P03277 |
Expressioni
Inductioni
Keywords - Developmental stagei
Late proteinInteractioni
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.
Interacts with host NUP214 (via N-terminus); this interaction might be essential for the release of the virus genome to the nucleus (By similarity).
UniRule annotationBy similarity6 PublicationsStructurei
Secondary structure
3D structure databases
SMRi | P03277 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03277 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 125 – 188 | DisorderedSequence analysisAdd BLAST | 64 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 143 – 163 | Acidic residuesSequence analysisAdd BLAST | 21 |
Sequence similaritiesi
Family and domain databases
Gene3Di | 3.90.39.10, 1 hit |
HAMAPi | MF_04051, ADV_CAPSH, 1 hit |
InterProi | View protein in InterPro IPR016108, Adenovirus_Pll_hexon_C IPR016107, Adenovirus_Pll_hexon_N IPR044942, Adenovirus_Pll_hexon_sub2 IPR037542, ADV_hexon IPR016112, VP_dsDNA_II |
Pfami | View protein in Pfam PF01065, Adeno_hexon, 2 hits PF03678, Adeno_hexon_C, 1 hit |
SUPFAMi | SSF49749, SSF49749, 2 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J01917 Genomic DNA Translation: AAA92215.1 |
PIRi | A94597, HXAD2 |
RefSeqi | AP_000175.1, AC_000007.1 NP_040525.1, NC_001405.1 |
Genome annotation databases
GeneIDi | 2652998 |
KEGGi | vg:2652998 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J01917 Genomic DNA Translation: AAA92215.1 |
PIRi | A94597, HXAD2 |
RefSeqi | AP_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 entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1P2Z | X-ray | 2.20 | A | 2-968 | [»] | |
SMRi | P03277 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB04272, Citric acid |
PTM databases
iPTMneti | P03277 |
Genome annotation databases
GeneIDi | 2652998 |
KEGGi | vg:2652998 |
Miscellaneous databases
EvolutionaryTracei | P03277 |
Family and domain databases
Gene3Di | 3.90.39.10, 1 hit |
HAMAPi | MF_04051, ADV_CAPSH, 1 hit |
InterProi | View protein in InterPro IPR016108, Adenovirus_Pll_hexon_C IPR016107, Adenovirus_Pll_hexon_N IPR044942, Adenovirus_Pll_hexon_sub2 IPR037542, ADV_hexon IPR016112, VP_dsDNA_II |
Pfami | View protein in Pfam PF01065, Adeno_hexon, 2 hits PF03678, Adeno_hexon_C, 1 hit |
SUPFAMi | SSF49749, SSF49749, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | CAPSH_ADE02 | |
Accessioni | P03277Primary (citable) accession number: P03277 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 134 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families