CAPSH_ADEM1
ID CAPSH_ADEM1 Reviewed; 909 AA.
AC P48308; O11839;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 23-FEB-2022, entry version 98.
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 Murine adenovirus A serotype 1 (MAdV-1) (Murine adenovirus 1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Murine mastadenovirus A.
OX NCBI_TaxID=10530;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FL;
RX PubMed=7509368; DOI=10.1099/0022-1317-75-1-141;
RA Weber J.M., Cai F., Murali R., Burnett R.M.;
RT "Sequence and structural analysis of murine adenovirus type 1 hexon.";
RL J. Gen. Virol. 75:141-147(1994).
RN [2]
RP SEQUENCE REVISION TO 443.
RA Weber J.M.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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; M81889; AAB48187.1; -; Genomic_DNA.
DR SMR; P48308; -.
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; T=25 icosahedral capsid protein; Virion;
KW 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..909
FT /note="Hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT /id="PRO_0000221831"
FT SITE 733
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; 102369 MW; 7E1C17DF7F0E95A0 CRC64;
MTTPSMQPQW AFMHIAGQDA SQYLSPGVVQ FAAATDTYFS LGNKFRNPTV APTHDVTTDR
SQRLTLRIVP VDREDSQYTY KTRFQLSVGD NRVLDMASTY FDIRGRLDRG PSFKPYSGTA
YNSLAPRAAP NNLMFKTGAD SKTMTIAQAN IVGSTIDQDG LKINNVALNP NAGEPAVQEG
LENWMEELQI GADKKFASRV LKADQPVLPN YGSYAYPTNI NGTQTKDGTT VDKVYMCSKG
ANVQNPDVVL YSEEVNLQAP DTHLLDGPGA DNPKDRVAFC AAPNRPNYIG FRDNFIGLMY
YNSNGNQGVL AGQASQLNAV VDLQDRNTEL SYQFLLDSLY DRSRYFSLWN QAIDSYDPRV
RIIENDGVED DITSFAFDLR GIGDLPYKQV QTHNGNQQSA NTTDTCYIGK GNMAAMEINI
PANLWLGFLY ANVAQYMPDD FKVDPSNIQM PQDKTTYAYM NQRIAPAGLI ETYVNVGGRW
SVDFMDTVNP FNHHRNEGLK YRSQILGNGR FVDFHIQVPQ KFFAIKSLLL LPGSYTYEWS
FRKDVNMVLQ SSLGNDLRAD GARLEIHSVN LYASFFPMAH NTASTLEAML RNETNDQTFL
DYLSSATMMF PIPAGQTQVP VSIPARNWAA FRGWSFTRIK QQETPNIGSP YDPYFKYSGS
IPFLDATFYL THTFQRVSIM FDSSVSWPGN DRLLTPNEFE IKRHIDAEGL CVGQSNMTKD
WFLVQMLSNY NIGYQGFYLP ENNKDRTYSF VRNFEPLARQ VVDDAAAANY RDVPLSKRFN
NSGWRSAGPP IFAREGAPYP ANWPYPLCGE AAWAAKTQRK FLVDRYMYRI PFSSNFMSMG
ALTDLGQNLL YANSAHSLEM TFNVDPMQEA TFLYILFEVF DCVRIHQPHR GIIEAVYLRS
PFSAGNATT
