CAPSH_ADE12
ID CAPSH_ADE12 Reviewed; 919 AA.
AC P19900;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 23-FEB-2022, entry version 111.
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 Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus A.
OX NCBI_TaxID=28282;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8254750; DOI=10.1128/jvi.68.1.379-389.1994;
RA Sprengel J., Schmitz B., Heuss-Neitzel D., Zock C., Doerfler W.;
RT "Nucleotide sequence of human adenovirus type 12 DNA: comparative
RT functional analysis.";
RL J. Virol. 68:379-389(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 888-919.
RC STRAIN=Pereira 1131;
RX PubMed=3043380; DOI=10.1093/nar/16.14.7195;
RA Weber J.M., Houde A.;
RT "The primary structure of human adenovirus type 12 protease.";
RL Nucleic Acids Res. 16:7195-7195(1988).
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; X73487; CAA51891.1; -; Genomic_DNA.
DR EMBL; X07655; CAB37192.1; -; Genomic_DNA.
DR PIR; S01730; S01730.
DR PIR; S33942; S33942.
DR RefSeq; NP_040924.1; NC_001460.1.
DR SMR; P19900; -.
DR GeneID; 1460858; -.
DR KEGG; vg:1460858; -.
DR Proteomes; UP000004993; 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 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..919
FT /note="Hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT /id="PRO_0000221821"
FT SITE 744
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 907
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
SQ SEQUENCE 919 AA; 103040 MW; B37167885A516288 CRC64;
MATPSMMPQW SYMHIAGQDA SEYLSPGLVQ FARATDTYFT LGNKFRNPTV APTHDVTTDR
SQRLTLRFVP VDREDTTYSY KARFTLAVGD NRVLDMASSY FDIRGVLDRG PSFKPYSGTA
YNSLAPKGAP NASQWSDNAK LNTFAQAPYL SDTITAADGI KVGTDTAQAG AAVYANKTYQ
PEPQVGPSEW NTSIENVKAG GRALKQTTAM QPCYGSYARP TNEHGGQSKD DNIELKFFDS
ANNAANTAQV VFYTEDVNLE MPDTHLVFKP TVTNGTIASE SLLGQQAAPN RANYIAFRDN
FIGLMYYNST GNMGVLAGQA SQLNAVVDLQ DRNTELSYQL MLDALGDRTR YFSLWNSAVD
SYDPDVRVIE NHGVEDELPN YCFPLSAVGE IKNYKGIKPD NGGGGGWTAD NTVSEANHIG
IGNIAAMEIN LQANLWRSFL YSNVGLYLPD DLKYTPGNIK LPDNKNTYEY MNGRVTAPGL
VDTYVNIGAR WSPDVMDNVN PFNHHRNAGL RYRSMLLGNG RFVPFHIQVP QKFFAIRNLL
LLPGSYTYEW NFRKDVNMIL QSTLGNDLRV DGASVRFDNI ALYANFFPMA HNTASTLEAM
LRNDTNDQSF NDYLCAANML YPIPANATSV PISIPSRNWA AFRGWSFTRL KTKETPSLGS
GFDPYFVYSG TIPYLDGTFY LNHTFKKVSI MFDSSVSWPG NDRLLTPNEF EIKRSVDGEG
YNVAQCNMTK DWFLIQMLSH YNIGYQGFYI PESYKDRMYS FFRNFQPMSR QVVDTTEYKN
YKKVTVEFQH NNSGFVGYLG PTMREGQAYP ANYPYPLIGQ TAVESITQKK FLCDRVMWRI
PFSSNFMSMG ALTDLGQNML YANSAHALDM TFEVDPMDEP TLLYVLFEVF DVVRIHQPHR
GVIEAVYLRT PFSAGNATT
