ID Q8B8T3_9ADEN Unreviewed; 948 AA.
AC Q8B8T3;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Hexon protein {ECO:0000256|ARBA:ARBA00019716, ECO:0000256|HAMAP-Rule:MF_04051};
DE Short=CP-H {ECO:0000256|HAMAP-Rule:MF_04051, ECO:0000256|RuleBase:RU361265};
DE AltName: Full=Protein II {ECO:0000256|ARBA:ARBA00032254, ECO:0000256|HAMAP-Rule:MF_04051};
GN Name=Hexon {ECO:0000313|EMBL:BAG48788.1};
GN Synonyms=L3 {ECO:0000256|HAMAP-Rule:MF_04051,
GN ECO:0000313|EMBL:AAP49209.1};
OS Human adenovirus 11.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX NCBI_TaxID=10541 {ECO:0000313|EMBL:AAN62515.1, ECO:0000313|Proteomes:UP000152074};
RN [1] {ECO:0000313|EMBL:AAP49209.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Slobitski {ECO:0000313|EMBL:AAP49209.1};
RA Mei Y.-F., Skog J., Lindman K., Wadell G.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAP49209.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Slobitski {ECO:0000313|EMBL:AAP49209.1};
RX PubMed=12867636; DOI=10.1099/vir.0.19178-0;
RA Mei Y.F., Skog J., Lindman K., Wadell G.;
RT "Comparative analysis of the genome organization of human adenovirus 11, a
RT member of the human adenovirus species B, and the commonly used human
RT adenovirus 5 vector, a member of species C.";
RL J. Gen. Virol. 84:2061-2071(2003).
RN [3] {ECO:0000313|EMBL:AAN62515.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ad11p Slobitski {ECO:0000313|EMBL:AAN62515.1};
RX PubMed=12726735; DOI=10.1016/S0042-6822(02)00085-5;
RA Stone D., Furthmann A., Sandig V., Lieber A.;
RT "The complete nucleotide sequence, genome organization, and origin of human
RT adenovirus type 11.";
RL Virology 309:152-165(2003).
RN [4] {ECO:0000313|EMBL:AAN62515.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ad11p Slobitski {ECO:0000313|EMBL:AAN62515.1};
RX PubMed=15795294; DOI=10.1128/JVI.79.8.5090-5104.2005;
RA Stone D., Ni S., Li Z.Y., Gaggar A., DiPaolo N., Feng Q., Sandig V.,
RA Lieber A.;
RT "Development and assessment of human adenovirus type 11 as a gene transfer
RT vector.";
RL J. Virol. 79:5090-5104(2005).
RN [5] {ECO:0000313|EMBL:BAG48788.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Slobitski {ECO:0000313|EMBL:BAG48788.1};
RX PubMed=18385435; DOI=10.1128/JCM.01835-07;
RA Ishiko H., Shimada Y., Konno T., Hayashi A., Ohguchi T., Tagawa Y.,
RA Aoki K., Ohno S., Yamazaki S.;
RT "Novel human adenovirus causing nosocomial epidemic keratoconjunctivitis.";
RL J. Clin. Microbiol. 46:2002-2008(2008).
CC -!- FUNCTION: Major capsid protein that self-associates to form 240 hexon
CC trimers, each in the shape of a hexagon, building most of the pseudo
CC T=25 capsid. Assembled into trimeric units with the help of the
CC chaperone shutoff protein. Transported by pre-protein VI to the nucleus
CC where it associates with other structural proteins to form an empty
CC capsid. Might be involved, through its interaction with host dyneins,
CC in the intracellular microtubule-dependent transport of incoming viral
CC capsid to the nucleus. {ECO:0000256|ARBA:ARBA00024662,
CC ECO:0000256|HAMAP-Rule:MF_04051}.
CC -!- SUBUNIT: Homotrimer. Interacts with the capsid vertex protein; this
CC interaction binds the peripentonal hexons to the neighboring penton
CC base. Interacts with the hexon-linking protein; this interaction
CC tethers the hexons surrounding the penton to those situated in the
CC central plate of the facet. Interacts with the hexon-interlacing
CC protein; this interaction lashes the hexons together. Interacts with
CC host dyneins DYNC1LI1 and DYNC1I2; this interaction might be involved
CC in intracellular microtubule-dependent transport of incoming viral
CC capsid. Interacts with the shutoff protein; this interaction allows
CC folding and formation of hexons trimers. Interacts with pre-protein VI;
CC this interaction probably allows nuclear import of hexon trimers and
CC possibly pre-capsid assembly. {ECO:0000256|HAMAP-Rule:MF_04051}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147,
CC ECO:0000256|HAMAP-Rule:MF_04051}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Virion {ECO:0000256|HAMAP-
CC Rule:MF_04051}. Note=Forms the capsid icosahedric shell. Present in 720
CC copies per virion, assembled in 240 trimers. {ECO:0000256|HAMAP-
CC Rule:MF_04051}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000256|HAMAP-Rule:MF_04051, ECO:0000256|RuleBase:RU361265}.
CC -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC are produced by alternative splicing and alternative polyadenylation of
CC the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC present in the N-terminus of all these mRNAs and is recognized by the
CC viral shutoff protein to provide expression although conventional
CC translation via ribosome scanning from the cap has been shut off in the
CC host cell. {ECO:0000256|HAMAP-Rule:MF_04051}.
CC -!- SIMILARITY: Belongs to the adenoviridae hexon protein family.
CC {ECO:0000256|ARBA:ARBA00008659, ECO:0000256|HAMAP-Rule:MF_04051,
CC ECO:0000256|RuleBase:RU361265}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04051}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY163756; AAN62515.1; -; Genomic_DNA.
DR EMBL; AF532578; AAP49209.1; -; Genomic_DNA.
DR EMBL; AB330092; BAG48788.1; -; Genomic_DNA.
DR Proteomes; UP000128793; Genome.
DR Proteomes; UP000152074; Genome.
DR GO; GO:0039623; C:T=25 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 2.170.9.10; Adenovirus Type 2 Hexon, domain 1; 1.
DR Gene3D; 2.70.9.10; Adenovirus Type 2 Hexon, domain 4; 1.
DR Gene3D; 3.90.39.10; Hexon Major Viral Coat Protein, domain 2; 2.
DR Gene3D; 3.90.249.10; Hexon Major Viral Coat Protein, domain 3; 2.
DR HAMAP; MF_04051; ADV_CAPSH; 1.
DR InterPro; IPR016108; Adenovirus_Pll_hexon_C.
DR InterPro; IPR016107; Adenovirus_Pll_hexon_N.
DR InterPro; IPR044942; Adenovirus_Pll_hexon_sub2.
DR InterPro; IPR016110; Adenovirus_Pll_hexon_sub3.
DR InterPro; IPR037542; ADV_hexon.
DR InterPro; IPR016112; VP_dsDNA_II.
DR Pfam; PF01065; Adeno_hexon; 1.
DR Pfam; PF03678; Adeno_hexon_C; 1.
DR SUPFAM; SSF49749; Group II dsDNA viruses VP; 2.
PE 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|HAMAP-Rule:MF_04051};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561, ECO:0000256|HAMAP-
KW Rule:MF_04051};
KW Cytoplasmic inwards viral transport {ECO:0000256|ARBA:ARBA00023120,
KW ECO:0000256|HAMAP-Rule:MF_04051};
KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04051,
KW ECO:0000256|RuleBase:RU361265};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW Rule:MF_04051};
KW Late protein {ECO:0000256|HAMAP-Rule:MF_04051,
KW ECO:0000256|RuleBase:RU361265};
KW Microtubular inwards viral transport {ECO:0000256|ARBA:ARBA00022952,
KW ECO:0000256|HAMAP-Rule:MF_04051};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_04051};
KW T=25 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00023275,
KW ECO:0000256|HAMAP-Rule:MF_04051};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04051};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296,
KW ECO:0000256|HAMAP-Rule:MF_04051}.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
FT CHAIN 2..948
FT /note="Hexon protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
FT /id="PRO_5035976815"
FT DOMAIN 8..631
FT /note="Adenovirus Pll hexon N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01065"
FT DOMAIN 632..854
FT /note="Adenovirus Pll hexon C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03678"
FT REGION 196..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 773
FT /note="Involved in interaction with pre-protein VI"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
FT MOD_RES 2
FT /note="N-acetylalanine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
FT MOD_RES 936
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
SQ SEQUENCE 948 AA; 106994 MW; E41D137918F5594E CRC64;
MATPSMLPQW AYMHIAGQDA SEYLSPGLVQ FARATDTYFN LGNKFRNPTV APTHDVTTDR
SQRLMLRFVP VDREDNTYSY KVRYTLAVGD NRVLDMASTF FDIRGVLDRG PSFKPYSGTA
YNSLAPKGAP NTSQWIAEGV KNTTGEEHVT EEETNTTTYT FGNAPVKAEA EITKEGLPVG
LEVSDEESKP IYADKTYQPE PQLGDETWTD LDGKTEKYGG RALKPDTKMK PCYGSFAKPT
NVKGGQAKQK TTEQPNQKVE YDIDMEFFDA ASQKTNLSPK IVMYAENVNL ETPDTHVVYK
PGTEDTSSEA NLGQQSMPNR PNYIGFRDNF IGLMYYNSTG NMGVLAGQAS QLNAVVDLQD
RNTELSYQLL LDSLGDRTRY FSMWNQAVDS YDPDVRVIEN HGVEDELPNY CFPLDGIGVP
TTSYKSIVPN GDNAPNWKEP EVNGTSEIGQ GNLFAMEINL QANLWRSFLY SNVALYLPDS
YKYTPSNVTL PENKNTYDYM NGRVVPPSLV DTYVNIGARW SLDAMDNVNP FNHHRNAGLR
YRSMLLGNGR YVPFHIQVPQ KFFAVKNLLL LPGSYTYEWN FRKDVNMVLQ SSLGNDLRVD
GASISFTSIN LYATFFPMAH NTASTLEAML RNDTNDQSFN DYLSAANMLY PIPANATNIP
ISIPSRNWAA FRGWSFTRLK TKETPSLGSG FDPYFVYSGS IPYLDGTFYL NHTFKKVSIM
FDSSVSWPGN DRLLSPNEFE IKRTVDGEGY NVAQCNMTKD WFLVQMLANY NIGYQGFYIP
EGYKDRMYSF FRNFQPMSRQ VVDEVNYKDF KAVAIPYQHN NSGFVGYMAP TMRQGQPYPA
NYPYPLIGTT AVNSVTQKKF LCDRTMWRIP FSSNFMSMGA LTDLGQNMLY ANSAHALDMT
FEVDPMDEPT LLYLLFEVFD VVRVHQPHRG IIEAVYLRTP FSAGNATT
//
