CAPSH_ADES1
ID CAPSH_ADES1 Reviewed; 909 AA.
AC Q8JN67;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 23-FEB-2022, entry version 82.
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 Snake adenovirus serotype 1 (SnAdV-1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Atadenovirus.
OX NCBI_TaxID=189830;
OH NCBI_TaxID=94885; Pantherophis guttatus (Corn snake) (Elaphe guttata).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12237421; DOI=10.1099/0022-1317-83-10-2403;
RA Farkas S.L., Benko M., Elo P.T., Ursu K., Dan A., Ahne W., Harrach B.;
RT "Genetic analysis of an adenovirus isolated from corn snake (Elaphe
RT guttata) implies common origin with the members of the proposed new genus
RT Atadenovirus.";
RL J. Gen. Virol. 83:2403-2410(2002).
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; DQ106414; AAL92452.1; -; Genomic_DNA.
DR RefSeq; YP_001552255.1; NC_009989.1.
DR SMR; Q8JN67; -.
DR GeneID; 10973869; -.
DR KEGG; vg:10973869; -.
DR Proteomes; UP000136605; 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 Capsid protein; Cytoplasmic inwards viral transport; Host nucleus;
KW Host-virus interaction; Late protein; Microtubular inwards viral transport;
KW Phosphoprotein; Reference proteome; T=25 icosahedral capsid protein;
KW Virion; Virus entry into host cell.
FT CHAIN 1..909
FT /note="Hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT /id="PRO_0000221833"
FT SITE 726
FT /note="Involved in interaction with pre-protein VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT MOD_RES 897
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
SQ SEQUENCE 909 AA; 101939 MW; DABCEF38B6442DD3 CRC64;
MEPQREFFHI AGRSAKEYLS ENLVQFIQAT QNYFNIGEKF RDPYVAPSAG VTTDRSQKLQ
LRVVPMQIED NANYYKARFT LNVGDNRLVD LGSSYFDIKG TLDRGPSFKP YGGTAYNPLA
PKSAPVNSPF IVGNDTHVVA QLPQTYAAAN TGVTEAIQQQ VSNVQPNPQD GLPNYSGPEV
VDATTKAGLG RVVAEESEGQ QFPCLRAYAA PQTAAGDVST APIEKTYVNT TNVAGRVSGT
MATDVIDWQN PDAHFVDYVD DGRSTSAGNR PNYIGFRDNF IGIMYYNSGS NTGSLSSQTQ
QLNVVLDLND RNSELSYQYM LADLTSRWHY FALWNQAVDS YDRHVRIIEN DGYEEGPPNL
SFPIQGIQNP FSPSSVGTEM TVNTANQTAA ATANTVAHIG YGNIPAVEMN LPANLRRTFL
YANVAMYLPD TYKFTPPNID LPANHLSYGY MNGRLPLPNI IDTWTDIGAR WSLDVMDTVN
PFNHHRNTGL KYRSQLLGNG RHCNFHIQVP QKFFAIKNLL LLPGTYNYEW YFRKDPNMVL
QSTLGNDLRE DGAQITYNQV NLYVSFFPMN YDTQSELELM LRNATNDQNF SDYLGAVNNL
YQIPAGSNTV VVNIPDRSWG AFRGWSFTRL KVTETPRIGA TQDPNFEYSG TIPYLDGTFY
LSHTFQRCSI QWDSSVPWPG NDRLLVPNWF EIKDPPNQDP EGYNTMQSNL TKDFFFTQMA
ASYNQGYQGF SYPSCTKHYG FINNFEPMSR QVPVYDATHP NLMAAYLNNP ATMPIWNNCG
FQQKTSTNAL LERCGHAYVA NWPFPLTGRD ALPNQTTEKK FLVDNYLWQI PFSSNFLNMG
TLTDLGQNVM YANSSHSLNM QFTVDPMNEP TYLLLLFGVF DQVVVNQPTR SGISVAYLRL
PFASGSAAT
