CAPSH_ADE40
ID CAPSH_ADE40 Reviewed; 923 AA.
AC P11819;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 25-MAY-2022, entry version 123.
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 F serotype 40 (HAdV-40) (Human adenovirus 40).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX NCBI_TaxID=28284;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugan;
RX PubMed=8263936; DOI=10.1006/jmbi.1993.1687;
RA Davison A.J., Telford E.A., Watson M.S., McBride K., Mautner V.;
RT "The DNA sequence of adenovirus type 40.";
RL J. Mol. Biol. 234:1308-1316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Dugan;
RX PubMed=2481711; DOI=10.1099/0022-1317-70-12-3203;
RA Toogood C.I.A., Murali R., Burnett M., Hay R.T.;
RT "The adenovirus type 40 hexon: sequence, predicted structure and
RT relationship to other adenovirus hexons.";
RL J. Gen. Virol. 70:3203-3214(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 640-923.
RX PubMed=3279700; DOI=10.1016/0042-6822(88)90227-9;
RA Vos H.L., der Lee F.M., Reemst A.M.C.B., van Loon A.E., Sussenbach J.S.;
RT "The genes encoding the DNA binding protein and the 23K protease of
RT adenovirus types 40 and 41.";
RL Virology 163:1-10(1988).
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; L19443; AAC13967.1; -; Genomic_DNA.
DR EMBL; X51782; CAA36077.1; -; Genomic_DNA.
DR EMBL; M19540; AAA52194.1; -; Genomic_DNA.
DR PIR; A33611; HXAD40.
DR RefSeq; NP_040862.1; NC_001454.1.
DR SMR; P11819; -.
DR DNASU; 2715932; -.
DR GeneID; 2715932; -.
DR KEGG; vg:2715932; -.
DR Proteomes; UP000151954; 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; 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; Reference proteome;
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..923
FT /note="Hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT /id="PRO_0000221824"
FT SITE 748
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 911
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT CONFLICT 163
FT /note="S -> L (in Ref. 2; CAA36077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 923 AA; 103953 MW; C6630EA788E00A29 CRC64;
MATPSMMPQW SYMHIAGQDA SEYLSPGLVQ FARATDTYFS LGNKFRNPTV APTHDVTTDR
SQRLTLRFVP VDREETAYSY KVRFTLAVGD NRVLDMASTY FDIRGVLDRG PSFKPYSGTA
YNSLAPKGAP NPSQWTNQNK TNSFGQAPYI GQKITNQGVQ VGSDSNNRDV FADKTYQPEP
QVGQTQWNIN PMQNAAGRIL KQTTPMQPCY GSYARPTNEK GGQAKLVKND DNQTTTTNVG
LNFFTTATET ANFSPKVVLY SEDVNLEAPD THLVFKPDVN GTSAELLLGQ QAAPNRPNYI
GFRDNFIGLM YYNSTGNMGV LAGQASQLNA VVDLQDRNTE LSYQLMLDAL GDRSRYFSMW
NQAVDSYDPD VRIIENHGVE DELPNYCFPL NGQGISNSYQ GVKTDNGTNW SQNNTDVSSN
NEISIGNVFA MEINLAANLW RSFLYSNVAL YLPDSYKITP DNITLPDNKN TYAYMNGRVA
VPSALDTYVN IGARWSPDPM DNVNPFNHHR NAGLRYRSML LGNGRYVPFH IQVPQKFFAI
KNLLLLPGSY TYEWNFRKDV NMILQSSLGN DLRVDGASVR FDSINLYANF FPMAHNTAST
LEAMLRNDTN DQSFNDYLCA ANMLYPIPAN ATSVPISIPS RNWAAFRGWS FTRLKTKETP
SLGSGFDPYF TYSGSVPYLD GTFYLNHTFK KVSVMFDSSV SWPGNDRLLT PNEFEIKRTV
DGEGYNVAQC NMTKDWFLIQ MLSHYNIGYQ GFHVPESYKD RMYSFFRNFQ PMSRQVVDTT
TYTEYQNVTL PFQHNNSGFV GYMGPAIREG QAYPANYPYP LIGQTAVPSL TQKKFLCDRT
MWRIPFSSNF MSMGALTDLG QNMLYANSAH ALDMTFEVDP MDEPTLLYVL FEVFDVVRIH
QPHRGVIEAV YLRTPFSAGN ATT
