ID M9Z2K7_9ADEN Unreviewed; 927 AA.
AC M9Z2K7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Hexon protein {ECO:0000256|ARBA:ARBA00019716, ECO:0000256|HAMAP-Rule:MF_04051};
DE Short=CP-H {ECO:0000256|HAMAP-Rule:MF_04051, ECO:0000256|RuleBase:RU361265};
DE AltName: Full=Protein II {ECO:0000256|ARBA:ARBA00032254, ECO:0000256|HAMAP-Rule:MF_04051};
GN Name=L3 {ECO:0000256|HAMAP-Rule:MF_04051};
OS Simian mastadenovirus C.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=1962300 {ECO:0000313|EMBL:AGK27138.1, ECO:0000313|Proteomes:UP000120020};
RN [1] {ECO:0000313|Proteomes:UP000120020, ECO:0000313|Proteomes:UP000142830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BaAdV-2 {ECO:0000313|EMBL:AGK27138.1}, and BaAdV-4
RC {ECO:0000313|EMBL:AGK27210.1};
RX PubMed=23592261; DOI=10.1128/mBio.00084-13;
RA Chiu C.Y., Yagi S., Lu X., Yu G., Chen E.C., Liu M., Dick E.J.Jr.,
RA Carey K.D., Erdman D.D., Leland M.M., Patterson J.L.;
RT "A novel adenovirus species associated with an acute respiratory outbreak
RT in a baboon colony and evidence of coincident human infection.";
RL MBio 4:e00084-e00084(2013).
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:0000256|ARBA:ARBA00024662,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_04051}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147,
CC ECO:0000256|HAMAP-Rule:MF_04051}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Virion {ECO:0000256|HAMAP-
CC Rule:MF_04051}. Note=Forms the capsid icosahedric shell. Present in 720
CC copies per virion, assembled in 240 trimers. {ECO:0000256|HAMAP-
CC Rule:MF_04051}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000256|HAMAP-Rule:MF_04051, ECO:0000256|RuleBase:RU361265}.
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:0000256|HAMAP-Rule:MF_04051}.
CC -!- SIMILARITY: Belongs to the adenoviridae hexon protein family.
CC {ECO:0000256|ARBA:ARBA00008659, ECO:0000256|HAMAP-Rule:MF_04051,
CC ECO:0000256|RuleBase:RU361265}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04051}.
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DR EMBL; KC693022; AGK27138.1; -; Genomic_DNA.
DR EMBL; KC693024; AGK27210.1; -; Genomic_DNA.
DR OrthoDB; 198at10239; -.
DR Proteomes; UP000120020; Genome.
DR Proteomes; UP000142830; 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; 2.70.9.10; Adenovirus Type 2 Hexon, domain 4; 2.
DR Gene3D; 3.90.39.10; Hexon Major Viral Coat Protein, domain 2; 1.
DR Gene3D; 3.90.249.10; Hexon Major Viral Coat Protein, domain 3; 2.
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; Group II dsDNA viruses VP; 2.
PE 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|HAMAP-Rule:MF_04051};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561, ECO:0000256|HAMAP-
KW Rule:MF_04051};
KW Cytoplasmic inwards viral transport {ECO:0000256|ARBA:ARBA00023120,
KW ECO:0000256|HAMAP-Rule:MF_04051};
KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04051,
KW ECO:0000256|RuleBase:RU361265};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW Rule:MF_04051};
KW Late protein {ECO:0000256|HAMAP-Rule:MF_04051,
KW ECO:0000256|RuleBase:RU361265};
KW Microtubular inwards viral transport {ECO:0000256|ARBA:ARBA00022952,
KW ECO:0000256|HAMAP-Rule:MF_04051};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_04051};
KW T=25 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00023275,
KW ECO:0000256|HAMAP-Rule:MF_04051};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04051};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296,
KW ECO:0000256|HAMAP-Rule:MF_04051}.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
FT CHAIN 2..927
FT /note="Hexon protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
FT /id="PRO_5039765249"
FT DOMAIN 8..610
FT /note="Adenovirus Pll hexon N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01065"
FT DOMAIN 611..832
FT /note="Adenovirus Pll hexon C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03678"
FT REGION 124..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 752
FT /note="Involved in interaction with pre-protein VI"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
FT MOD_RES 2
FT /note="N-acetylalanine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
FT MOD_RES 915
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
SQ SEQUENCE 927 AA; 103821 MW; E3AA9738CC3495FA CRC64;
MATPSMMPQW SYMHIAGQDA SEYLSPGLVQ FARATDTYFS LGNKFRNPTV APTHDVTTDR
SQRLTLRFVP VDREDTAYSY KVRYTLAVGD NRVLDMASTY FDIRGVLDRG PSFKPYSGTA
YNSLAPKGAP NPSQWTTTNG GNKTNSFGQA PFIGESLTKD GIQVGVDTGN PGTAVYADKL
YQPEPQVGLS KWNQNPSENA AGRILKPSTP MQPCYGSYAY PTNTNGGQVK TSATDATGAN
NVTLNFFNNA ADNGNNNPKV VLYSEDVNLE APDTHLVFKP DANNATSAET LLGQQAAPNR
PNYIGFRDNF IGLMYYNSTG NMGVLAGQAS QLNAVVDLQD RNTELSYQLM LDALGDRSRY
FSMWNQAVDS YDPDVRIIEN HGVEDELPNY CFPLNGQGIS NTYKGVKTNN GGAAWTQDTD
VVTTNEISIG NVFAMEINLA ANLWRSFLYS NVALYLPDSY KYTPDNIELP QNKNSYGYIN
GRVTAPNAID TYVNIGARWS PDPMDNVNPF NHHRNAGLRY RSMLLGNGRY VPFHIQVPQK
FFAIKNLLLL PGSYTYEWNF RKDVNMILQS TLGNDLRVDG ASIRFDSINL YANFFPMAHN
TASTLEAMLR NDTNDQSFND YLCAANMLYP IPSNATSVPI SIPSRNWAAF RGWSFTRLKT
KETPSLGSGF DPYFVYSGSI PYLDGTFYLN HTFKKVSIMF DSSVSWPGND RLLTPNEFEI
KRSVDGEGYN VAQSNMTKDW FLIQMLSHYN IGYQGFYVPE SYKDRMYSFF RNFQPMSRQV
VDTVNYANYK EVKMPFQHNN SGFVGYMGPT MREGQAYPAN YPYPLIGETA VPSVTQKKFL
CDRVMWRIPF SSNFMSMGAL TDLGQNMLYA NSAHALDMTF EVDPMDEPTL LYVLFEVFDV
VRIHQPHRGV IEAVYLRTPF SAGNATT
//
