CAPSH_ADEP3
ID CAPSH_ADEP3 Reviewed; 939 AA.
AC Q9YTR8;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 116.
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 Porcine adenovirus A serotype 3 (PAdV-3) (Porcine adenovirus 3).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Porcine mastadenovirus A.
OX NCBI_TaxID=35265;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=6618;
RX PubMed=9837805; DOI=10.1006/viro.1998.9418;
RA Reddy P.S., Idamakanti N., Song J.Y., Lee J.B., Hyun B.H., Park J.H.,
RA Cha S.H., Bae Y.T., Tikoo S.K., Babiuk L.A.;
RT "Nucleotide sequence and transcription map of porcine adenovirus type 3.";
RL Virology 251:414-426(1998).
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; AF083132; AAC99441.1; -; Genomic_DNA.
DR SMR; Q9YTR8; -.
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; -; 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; 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..939
FT /note="Hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT /id="PRO_0000221832"
FT SITE 762
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 927
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
SQ SEQUENCE 939 AA; 106087 MW; 3B3B98EAC7C794EE CRC64;
MATPSMMPQW SYMHISGQDA SEYLSPGLVQ FSQATETYFN LNNKFRNPTV APTHDVTTER
SQRLQLRFVP VDKEDTQYTY KTRFQLAVGD NRVLDMASTF FDIRGTLDRG PSFKPYSGTA
YNIMAPKSAP NNCQYLDPKG ETEAGKVNTI AQASFVGPID ETTGDIKITE EEDEETTIDP
LYEPQPQLGP SSWSDNIPSA TSGAGRVLKQ TTPRQPCYGS YASPTNIHGG QTKDDKVTPL
YFTNNPATEA EALEENGLKP NVTLYSEDVD LKAPDTHLVY AVNQTQEFAQ YGLGQQAAPN
RANYIGFRDN FIGLLYYNSN GNQGMLAGQA SQLNAVVDLQ DRNHRTSYQL FLDSLYDRSR
YFSLWNQAID SYDKDVRVLE NNGVEDEMPN FCFPIGAIET NMTFTQLKKS ENGGSRATTW
TKENGDDGGN GAEHYLGIGN LNAMEINLTA NLWRSFLYSN VALYLPDKYK FSPPNVPIDP
NTHSYDYINK RLPLNNLIDT FVNIGARWSP DVMDNVNPFN HHRNYGLRYR SQLLGNGRYC
KFHIQVPQKF FALKSLLLLP GATYTYEWSF RKDVNMILQS TLGNDLRADG AKINIESVNL
YASFFPMAHN TASTLEAMLR NDTNNQTFID FLSSANMLYP IPANVTNLPI SIPSRNWAAF
RGWSFTRLKH NETPALGSPF DPYFTYSGSI PYLDGTFYLG HTFRRISIQF DSSVAWPGND
RLLTPNEFEV KRTVDGEGYT VAQTNMTKDW FLVQMLAHYN IGYQGYHLPE GYRDRTYSFL
RNFEPMCRQV PDYANHKDEY LEVPTTNQFN SSGFVSAAFT AGMREGHPYP ANWPYPLIGE
DAVQTVTQRK FLCDRTLWRI PFSSNFMSMG TLTDLGQNLL YANSAHALDM TFEVDAMDEP
TLLYVLFEVF DVCGVHQPHR GVIEAVYLRT PFSAGNATT
