ID A0A0M4MFL5_9ADEN Unreviewed; 937 AA.
AC A0A0M4MFL5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 adenovirus 13.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Simian mastadenovirus D.
OX NCBI_TaxID=38432 {ECO:0000313|EMBL:ALE30363.1, ECO:0000313|Proteomes:UP000099964};
RN [1] {ECO:0000313|EMBL:ALE30363.1, ECO:0000313|Proteomes:UP000099964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P-9 {ECO:0000313|EMBL:ALE30363.1};
RX PubMed=26370792; DOI=10.1007/s00705-015-2575-z;
RA Panto L., Podgorski I.I., Janoska M., Marko O., Harrach B.;
RT "Taxonomy proposal for Old World monkey adenoviruses: characterisation of
RT several non-human, non-ape primate adenovirus lineages.";
RL Arch. Virol. 160:3165-3177(2015).
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}.
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; KP329563; ALE30363.1; -; Genomic_DNA.
DR RefSeq; YP_009174018.1; NC_028103.1.
DR GeneID; 26100536; -.
DR KEGG; vg:26100536; -.
DR OrthoDB; 198at10239; -.
DR Proteomes; UP000099964; Genome.
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..937
FT /note="Hexon protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
FT /id="PRO_5023290480"
FT DOMAIN 8..620
FT /note="Adenovirus Pll hexon N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01065"
FT DOMAIN 621..841
FT /note="Adenovirus Pll hexon C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03678"
FT SITE 762
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 925
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04051"
SQ SEQUENCE 937 AA; 105610 MW; 60D723EC98B5AEA6 CRC64;
MATPSMMPQW SYMHIAGQDA SEYLSPGLVQ FARATDTYFT LGNKFRNPTV APTHDVTTDR
SQRLTLRFVP VDREDTAYAY KARFTLSVGD NRVLDMASTY FDIRGVIDRG PSFKPYSGTA
YNALAPKGAP NNSQWHTVNE DNQNFLMHTY AQAPFESEFV ANNGNIGIQV GVSDTNTPIL
ADPTYQPEPQ DGEPQWQSLK AQEKLEHAGR ALKYTTPMKP CYGSYARPTN AQGGQGIIDE
QTGETDATEI TQNYFALSTA TTDFTPKVVL YTEDVYLQTP DTHLVYTPSA TEGSTQDMLG
QQAAPNRPNY IGFRDNFIGL MYYNSTGNMG VLAGQASQLN AVVDLQDRNT ELSYQLMLDA
LSDRTRYFSM WNQAVDSYDP DVRIIENHGV EDELPTYCFP LSGVGITQEY QGVEPTNPAA
ADITWKEDAT VFDPNYIATG NINAYEINLQ ASLWRSFLYS NVALYLPDKY KYTPANVTLP
TNTNTYKYMN GRVTSPSLVD IFVNVGARWS PDPMDNVNPF NHHRNAGLRY RSQLLGNGRI
VPFHIQVPQK FFAIKNLLLL PGSYTYEWSF RKDVNMILQS TLGNDLRTDG AAIRIESVNL
YANFFPMAHN TASTLEAMLR NDTNDQSFND YLSAANMLYP IPANATNVPI SIPSRNWAAF
RGWSFTRLKA KETPALGSGF DPYFVYSGSI PYLDGTFYLN HTFKRVSIMF DSSVSWPGND
RLLTPNEFEV KRVVDGEGYT VAQSNMTKDW FLIQMLSHYN IGYQGFYIPE GYKDRMYSFF
RNFQPMTRQA VDPVNYTNYK EITVAHQHNN SGFVGFMGPT MREGHPYPAN YPYPLIGDSA
VPTVTQKKFL CDRTMWRIPF SSNFMSMGAL TDLGQNMLYA NSAHALDMTF EVDPMDEPTL
LYVLFEVFDV VRVHQPHRGI IEAVYLRTPF SAGNATT
//
