CAPSH_ADE03
ID CAPSH_ADE03 Reviewed; 944 AA.
AC P36849;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 23-FEB-2022, entry version 98.
DE RecName: Full=Hexon protein {ECO:0000255|HAMAP-Rule:MF_04051};
DE Short=CP-H {ECO:0000255|HAMAP-Rule:MF_04051};
DE AltName: Full=Protein II {ECO:0000255|HAMAP-Rule:MF_04051};
GN Name=L3 {ECO:0000255|HAMAP-Rule:MF_04051};
OS Human adenovirus B serotype 3 (HAdV-3) (Human adenovirus 3).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX NCBI_TaxID=45659;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate GB;
RX PubMed=7676636; DOI=10.1006/viro.1995.1474;
RA Pring-Akerblom P., Trijssenaar J., Adrian T.;
RT "Sequence characterization and comparison of human adenovirus subgenus B
RT and E hexons.";
RL Virology 212:232-236(1995).
RN [2]
RP SEQUENCE REVISION.
RA Pring-Akerblom P.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-Rule:MF_04051}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04051}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04051}. Note=Forms the capsid
CC icosahedric shell. Present in 720 copies per virion, assembled in 240
CC trimers. {ECO:0000255|HAMAP-Rule:MF_04051}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04051}.
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:0000255|HAMAP-Rule:MF_04051}.
CC -!- SIMILARITY: Belongs to the adenoviridae hexon protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04051, ECO:0000305}.
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DR EMBL; X76549; CAA54051.1; -; Genomic_DNA.
DR PIR; S39298; S39298.
DR SMR; P36849; -.
DR PRIDE; P36849; -.
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; 3.90.249.10; -; 2.
DR Gene3D; 3.90.39.10; -; 1.
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; SSF49749; 2.
PE 3: Inferred from homology;
KW Acetylation; Capsid protein; Cytoplasmic inwards viral transport;
KW Host nucleus; Host-virus interaction; Late protein;
KW Microtubular inwards viral transport; Phosphoprotein;
KW T=25 icosahedral capsid protein; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT CHAIN 2..944
FT /note="Hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT /id="PRO_0000221814"
FT REGION 193..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 769
FT /note="Involved in interaction with pre-protein VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT MOD_RES 2
FT /note="N-acetylalanine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT MOD_RES 932
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
SQ SEQUENCE 944 AA; 106088 MW; B779C679417F49D9 CRC64;
MATPSMMPQW AYMHIAGQDA SGYLSPGLVQ FARATDTYFS MGNKFRNPTV APTHDVTTDR
SQRLMLRFVP VDREDNTYSY KVRYTLAVGD NRVLDMASTF FDIRGVLDRG PSFKPYSGTA
YNSLAPKGAP NTSQWIVTTN GDNAVTTTTN TFGIASMKGG NITKEGLQIG KDITTTEGEE
KPIYADKTYQ PEPQVGEESW TDTDGTNEKF GGRALKPATN MKPCYGSFAR PTNIKGGQAK
NRKVKPTTEG GVETEEPDID MEFFDGRDAV AGALAPEIVL YTENVNLETP DSHVVYKPET
SNNSHANLGQ QAMPNRPNYI GFRDNFVGLM YYNSTGNMGV LAGQASQLNA VVDLQDRNTE
LSYQLLLDSL GDRTRYFSMW NQAVDSYDPD VRIIENHGIE DELPNYCFPL NGIGPGHTYQ
GIKVKTDDTN GWEKDANVAP ANEITIGNNL AMEINIQANL WRSFLYSNVA LYLPDVYKYT
PPNITLPTNT NTYEYMNGRV VSPSLVDSYI NIGARWSLDP MDNVNPFNHH RNAGLRYRSM
LLGNGRYVPF HIQVPQKFFA VKNLLLLPGS YTYEWNFRKD VNMVLQSSLG NDLRTDGATI
SFTSINLYAT FFPMAHNTAS TLEAMLRNDT NDQSFNDYLS AANMLYPIPA NATNIPISIP
SRNWAAFRGW SFTRLKTKET PSLGSGFDPY FVYSGSIPYL DGTFYLNHTF KKVAIMFDSS
VSWPGNDRLL SPNEFEIKRT VDGEGYNVAQ CNMTKDWFLV QMLANYNIGY QGFYIPEGYK
DRMYSFFRNF QPMSRQVVDE VNYTDYKAVT LPYQHNNSGF VGYLAPTMRQ GEPYPANYPY
PLIGTTAVKS VTQKKFLCDR TMWRIPFSSN FMSMGALTDL GQNMLYANSA HALDMTFEVD
PMDEPTLLYL LFEVFDVVRV HQPHRGVIEA VYLRTPFSAG NATT
