CAPSH_ADE41
ID CAPSH_ADE41 Reviewed; 925 AA.
AC P11820; Q64880;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 25-MAY-2022, entry version 106.
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 41 (HAdV-41) (Human adenovirus 41).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX NCBI_TaxID=10524;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3411299; DOI=10.1099/0022-1317-69-9-2291;
RA Toogood C.I.A., Hay R.T.;
RT "DNA sequence of the adenovirus type 41 hexon gene and predicted structure
RT of the protein.";
RL J. Gen. Virol. 69:2291-2301(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tak;
RA Toogood C.I.A., Murali R., Burnett M., Hay R.T.;
RL Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-756 AND 814-925.
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}.
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; D13781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M19541; AAA42460.1; -; Genomic_DNA.
DR EMBL; X51783; CAA36079.1; -; Genomic_DNA.
DR EMBL; M21163; AAA42461.1; -; Genomic_DNA.
DR PIR; A31040; HXAD41.
DR PDB; 6YBA; EM; 4.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-925.
DR PDB; 6Z7N; EM; 3.77 A; A/B/C/D/E/F/G/H/I/J/K/L=1-925.
DR PDBsum; 6YBA; -.
DR PDBsum; 6Z7N; -.
DR SMR; P11820; -.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Capsid protein;
KW Cytoplasmic inwards viral transport; Host nucleus; Host-virus interaction;
KW Late protein; 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..925
FT /note="Hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT /id="PRO_0000221825"
FT SITE 750
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 913
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
SQ SEQUENCE 925 AA; 103976 MW; 0A5EC704C82057BC CRC64;
MATPSMMPQW SYMHIAGQDA SEYLSPGLVQ FARATDTYFS LGNKFRNPTV APTHDVTTDR
SQRLTLRFVP VDREDTAYSY KVRFTLAVGD NRVLDMASTY FDIRGVLDRG PSFKPYSGTA
YNSLAPKTAP NPCEWKDNNK IKVRGQAPFI GTNINKDNGI QIGTDTTNQP IYADKTYQPE
PQVGQTQWNS EVGAAQKVAG RVLKDTTPML PCYGSYAKPT NEKGGQASLI TNGTDQTLTS
DVNLQFFALP STPNEPKAVL YAENVSIEAP DTHLVYKPDV AQGTISSADL LTQQAAPNRP
NYIGFRDNFI GLMYYNSTGN MGVLAGQASQ LNAVVDLQDR NTELSYQLML DALGDRSRYF
SMWNQAVDSY DPDVRIIENH GVEDELPNYC FPLGGSAATD TYSGIKANGQ TWTADDNYAD
RGAEIESGNI FAMEINLAAN LWRSFLYSNV ALYLPDSYKI TPDNITLPEN KNTYAYMNGR
VAVPSALDTY VNIGARWSPD PMDNVNPFNH HRNAGLRYRS MLLGNGRYVP FHIQVPQKFF
AIKNLLLLPG SYTYEWNFRK DVNMILQSSL GNDLRVDGAS VRFDSINLYA NFFPMAHNTA
STLEAMLRND TNDQSFNDYL CAANMLYPIP SNATSVPISI PSRNWAAFRG WSFTRLKTKE
TPSLGSGFDP YFTYSGSVPY LDGTFYLNHT FKKVSIMFDS SVSWPGNDRL LTPNEFEIKR
TVDGEGYNVA QCNMTKDWFL IQMLSHYNIG YQGFYVPESY KDRMYSFFRN FQPMSRQVVN
TTTYKEYQNV TLPFQHNNSG FVGYMGPTMR EGQAYPANYP YPLIGQTAVP SLTQKKFLCD
RTMWRIPFSS NFMSMGALTD LGQNMLYANS AHALDMTFEV DPMDEPTLLY VLFEVFDVVR
IHQPHRGVIE AVYLRTPFSA GNATT
