ID Q8B661_ADET1 Unreviewed; 911 AA.
AC Q8B661;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=L3 {ECO:0000256|HAMAP-Rule:MF_04051};
OS Tree shrew adenovirus serotype 1 (TSAdV-1) (Tupaia adenovirus 1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Tree shrew mastadenovirus A.
OX NCBI_TaxID=47680 {ECO:0000313|EMBL:AAN84889.1, ECO:0000313|Proteomes:UP000152383};
OH NCBI_TaxID=9393; Tupaiidae (tree shrews).
RN [1] {ECO:0000313|EMBL:AAN84889.1, ECO:0000313|Proteomes:UP000152383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6156536; DOI=10.1016/0042-6822(80)90371-2;
RA Darai G., Matz B., Flugel R.M., Grafe A., Gelderblom H., Delius H.;
RT "An adenovirus from Tupaia (tree shrew): growth of the virus,
RT characterization of viral DNA, and transforming ability.";
RL Virology 104:122-138(1980).
RN [2] {ECO:0000313|EMBL:AAN84889.1, ECO:0000313|Proteomes:UP000152383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12634391; DOI=10.1128/JVI.77.7.4345-4356.2003;
RA Schondorf E., Bahr U., Handermann M., Darai G.;
RT "Characterization of the complete genome of the Tupaia (tree shrew)
RT adenovirus.";
RL J. Virol. 77:4345-4356(2003).
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}.
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DR EMBL; AF258784; AAN84889.1; -; Genomic_DNA.
DR RefSeq; YP_068069.1; AC_000190.1.
DR OrthoDB; 198at10239; -.
DR Proteomes; UP000152383; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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; 2.70.9.10; Adenovirus Type 2 Hexon, domain 4; 2.
DR Gene3D; 3.90.39.10; Hexon Major Viral Coat Protein, domain 2; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000152383};
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..911
FT /note="Hexon protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
FT /id="PRO_5023539324"
FT DOMAIN 8..593
FT /note="Adenovirus Pll hexon N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01065"
FT DOMAIN 594..816
FT /note="Adenovirus Pll hexon C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03678"
FT SITE 735
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 899
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
SQ SEQUENCE 911 AA; 101246 MW; F5E488C36E3ACEDB CRC64;
MATPSMLPQW SFMHIAGQDA SEYLSPGLVQ FARATESYFN IGNKFRNPTV APTHDVTTER
SQRLQLRFVP VDKEDTQYTY KTRFQLAVGD NRVLDMGSTY FDIRGTLDRG PSFKPYSGTA
YNSLAPKSAT NNAQYTSGGK TATYAQASFI SEIVEVGGQY GIKVGEDNTG ADILADPNYQ
PEPTVGGEGW TVELGTIDSA GGRVLSATTP KAPCYGSYAA PTNNNGGQTT GQVNVKFFKE
GQGAGNPTVA LYSETVDMQS PDTHLVYATE PGALPDGLGQ QSAPNRPNYI GFRDNFIGLM
YYNSNGNLGV LAGQASQLNA VVDLQDRNTE LSYQLMLDSL VDRSRYFSMW NQAVDSYDPD
VRVLENNGVE DELPNYCFPL SGVGLTELYT GVARNGGNWA ADNDAAASQI AVGNVHAMEI
NIAANLWRGF LYSNVALYLP DEYKYTPINV TLPENTNTYA YMNGRVPANN LVDSFVNVGA
RWSPDVMDNV NPFNHHRNAG LRYRSQLLGN GRYCRFHIQV PQKFFAIKNL LLLPGTYTYE
WSFRKDVNMI LQSTLGNDLR VDGASINIES VNLYASFFPM SHNTASTLEA MLRNDTNDQC
FTDYLSAANM LYPIAANATN VPISIPSRNW AAFRGWSFTR LKQKETPALG SPYDPYFTYS
GSIPYLDGTF YLNHTFRRVA IQFDSSVSWP GNDRLLTPNE FEIKRAVDGE GYSTAQSTIT
KDWFLTQMLA NYNIGYQGYY LPDGYKDRLY SFLRNFQPMC RQVVDEANYA NYKAVSITHQ
HNNSGFTGFA SAAVPREGHP YPANWPYPLI GDTAVPSVTQ RKFLCDRTLW RIPFSSNFMS
MGTLSDLGQN LLYANSAHAL DMIFEVDPMP EPTLLYVLFE VFDVARVHQP HRGVIEVVYL
RTPFSAGNAT T
//
