CAPSH_ADE16
ID CAPSH_ADE16 Reviewed; 940 AA.
AC P36854;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 23-FEB-2022, entry version 91.
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 16 (HAdV-16) (Human adenovirus 16).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX NCBI_TaxID=31544;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate CH.79;
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).
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; X74662; CAA52726.1; -; Genomic_DNA.
DR PIR; S37216; S37216.
DR SMR; P36854; -.
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..940
FT /note="Hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT /id="PRO_0000221822"
FT SITE 765
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 928
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
SQ SEQUENCE 940 AA; 105501 MW; E5A3493E68236D15 CRC64;
MATPSMMPQW AYMHIAGQDA SEYLSPGLVQ FARATDTYFS MGNKFRNPTV APTHDVTTDR
SQRLMLRFVP VDREDNTYSY KVRYTLAVGD NRVLDMASTF FDIRGVLDRG PSFKPYSGTA
YNSLAPKGAP NTCQWKDSDS KMHTFGVAAM PGVTGKKIEA DGLPIGIDST SGTDTVIYAD
KTFQPEPQVG NASWVDANGT EEKYGGRALK DTTKMKPCYG SFAKPTNKEG GQANLKDSET
AATTPNYDID LAFFDNKNIA ANYDPDIVMY TENVDLQTPD THIVYKPGTE DTSSESNLGQ
QAMPNRPNYI GFRDNFIGLM YYNSTGNMGV LAGQASQLNA VVDLQDRNTE LSYQLLLDSL
GDRTRYFSMW NQAVDSYDPD VRIIENHGVE DELPNYCFPL NGVGFTDTYQ GVKVKTDAVA
GTSGTQWDKD DTTVSTANEI HGGNPFAMEI NIQANLWRSF LYSNVALYLP DSYKYTPSNV
TLPENKNTYD YMNGRVVPPS LVDTYVNIGA RWSLDAMDNV NPFNHHRNAG LRYRSMLLGN
GRYVPFHIQV PQKFFAVKNL LLLPGSYTYV WNFRKDVNMV LQSSLGNDLR VDGATISFTS
INLYATFFPM AHNTASTLEA MLRNDTNDQS FNDYLSAANM LYPIPANATN IPISIPSRNW
AAFRGWSFTR LKTKETPSLG SGFDPYFVYS GSIPYLDGTF YLNHTFKKVS IMFDSSVSWP
GNDRLLSPNE FEIKRTVDGE GYNVAQCNMT KDWFLVQMLA NYNIGYQGFY IPEGYKDRMY
SFFRNFQPMS RQVVDEVNYT DYKAVTLPYQ HNNSGFVGYL APTMRQGEPY PANYPYPLIG
TTAVKSVTQK KFLCDRTMWR IPFSSNFMSM GALTDLGQNL LYANSAHALD MTFEVDPMDE
PTLLSLVFEV FDVVRVHQPH RGVIEAVYLR TPFSAGNATT
