ID CAPSH_ADE05 Reviewed; 952 AA. AC P04133; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 152. 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 C serotype 5 (HAdV-5) (Human adenovirus 5). OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes; OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus C. OX NCBI_TaxID=28285; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6202684; DOI=10.1016/s0021-9258(20)82161-9; RA Kinloch R., MacKay N., Mautner V.; RT "Adenovirus hexon. Sequence comparison of subgroup C serotypes 2 and 5."; RL J. Biol. Chem. 259:6431-6436(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z; RA Chroboczek J., Bieber F., Jacrot B.; RT "The sequence of the genome of adenovirus type 5 and its comparison with RT the genome of adenovirus type 2."; RL Virology 186:280-285(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=23142869; DOI=10.1038/nmeth.2227; RA Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.; RT "De novo derivation of proteomes from transcriptomes for transcript and RT protein identification."; RL Nat. Methods 9:1207-1211(2012). RN [4] RP INTERACTION WITH PRE-PROTEIN VI. RC STRAIN=Ad5 ts147 mutant, and Human adenovirus C serotype 5; RX PubMed=14633984; DOI=10.1093/emboj/cdg614; RA Wodrich H., Guan T., Cingolani G., Von Seggern D., Nemerow G., Gerace L.; RT "Switch from capsid protein import to adenovirus assembly by cleavage of RT nuclear transport signals."; RL EMBO J. 22:6245-6255(2003). RN [5] RP INTERACTION WITH HUMAN DYNEINS DYNC1LI1 AND DYNC1I2. RX PubMed=20006841; DOI=10.1016/j.chom.2009.11.006; RA Bremner K.H., Scherer J., Yi J., Vershinin M., Gross S.P., Vallee R.B.; RT "Adenovirus transport via direct interaction of cytoplasmic dynein with the RT viral capsid hexon subunit."; RL Cell Host Microbe 6:523-535(2009). RN [6] RP INTERACTION WITH HUMAN NUP214. RX PubMed=25410864; DOI=10.1128/jvi.02639-14; RA Cassany A., Ragues J., Guan T., Begu D., Wodrich H., Kann M., Nemerow G.R., RA Gerace L.; RT "Nuclear import of adenovirus DNA involves direct interaction of hexon with RT an N-terminal domain of the nucleoporin Nup214."; RL J. Virol. 89:1719-1730(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: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. Interacts with host NUP214 (via N- CC terminus); this interaction might be essential for the release of the CC virus genome to the nucleus (PubMed:25410864). {ECO:0000255|HAMAP- CC Rule:MF_04051, ECO:0000269|PubMed:14633984, CC ECO:0000269|PubMed:20006841, ECO:0000269|PubMed:25410864}. 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; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X02997; CAA26753.1; -; Genomic_DNA. DR PIR; A03849; HXAD5. DR RefSeq; AP_000211.1; AC_000008.1. DR PDB; 1P30; X-ray; 2.50 A; A=2-952. DR PDB; 3TG7; X-ray; 1.57 A; A=2-952. DR PDB; 4V4U; EM; 10.00 A; F/G/H/I/J/K/L/M/N/O/P/Q=2-952. DR PDB; 5LDN; X-ray; 2.70 A; A=8-146, A=164-947. DR PDB; 5OGI; X-ray; 2.80 A; A=1-952. DR PDB; 6B1T; EM; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-952. DR PDB; 6CGV; X-ray; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L=4-952. DR PDB; 6EQC; EM; 7.40 A; A/B/C=1-952. DR PDB; 7S78; EM; 3.72 A; A/B/C/D/E/F/G/H/I/J/K/L=1-952. DR PDB; 8Q7C; EM; 2.90 A; A/B/C=1-952. DR PDBsum; 1P30; -. DR PDBsum; 3TG7; -. DR PDBsum; 4V4U; -. DR PDBsum; 5LDN; -. DR PDBsum; 5OGI; -. DR PDBsum; 6B1T; -. DR PDBsum; 6CGV; -. DR PDBsum; 6EQC; -. DR PDBsum; 7S78; -. DR PDBsum; 8Q7C; -. DR EMDB; EMD-18212; -. DR SMR; P04133; -. DR IntAct; P04133; 3. DR ABCD; P04133; 2 sequenced antibodies. DR EvolutionaryTrace; P04133; -. DR Proteomes; UP000004992; 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:0019028; C:viral capsid; IDA:CACAO. 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; 2.170.9.10; Adenovirus Type 2 Hexon, domain 1; 1. 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 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; 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 1: Evidence at protein level; KW 3D-structure; Acetylation; Capsid protein; KW Cytoplasmic inwards viral transport; Host nucleus; Host-virus interaction; KW Late protein; 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..952 FT /note="Hexon protein" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051" FT /id="PRO_0000221816" FT REGION 149..172 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 777 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 175 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051" FT MOD_RES 940 FT /note="Phosphotyrosine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051" FT CONFLICT 273 FT /note="T -> A (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 930 FT /note="R -> Q (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT HELIX 9..12 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 15..17 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 20..23 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 26..35 FT /evidence="ECO:0007829|PDB:3TG7" FT TURN 36..38 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 54..57 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 64..68 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 77..88 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 100..108 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:5OGI" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 183..187 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 192..195 FT /evidence="ECO:0007829|PDB:1P30" FT TURN 198..200 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 209..212 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 217..224 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:5OGI" FT TURN 253..256 FT /evidence="ECO:0007829|PDB:5LDN" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:5OGI" FT STRAND 263..267 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:5LDN" FT STRAND 283..289 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 298..302 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 312..316 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 318..321 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:3TG7" FT TURN 334..336 FT /evidence="ECO:0007829|PDB:5LDN" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 347..350 FT /evidence="ECO:0007829|PDB:3TG7" FT TURN 351..353 FT /evidence="ECO:0007829|PDB:1P30" FT HELIX 366..377 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 385..387 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 396..399 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 400..402 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:5LDN" FT STRAND 424..426 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 429..431 FT /evidence="ECO:0007829|PDB:5LDN" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:5LDN" FT STRAND 439..441 FT /evidence="ECO:0007829|PDB:5LDN" FT STRAND 444..446 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 450..452 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:5LDN" FT HELIX 464..476 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 478..480 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 483..485 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 501..506 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 511..514 FT /evidence="ECO:0007829|PDB:3TG7" FT TURN 516..521 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 527..530 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 541..550 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 552..563 FT /evidence="ECO:0007829|PDB:3TG7" FT TURN 567..571 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 576..586 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 589..592 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 593..597 FT /evidence="ECO:0007829|PDB:3TG7" FT TURN 601..605 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 607..618 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 624..634 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 637..639 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 641..644 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 649..656 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 662..670 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 677..684 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 685..687 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 692..694 FT /evidence="ECO:0007829|PDB:1P30" FT HELIX 706..709 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 715..717 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 718..725 FT /evidence="ECO:0007829|PDB:3TG7" FT TURN 726..728 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 729..732 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 737..739 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 742..744 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 749..754 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 759..762 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 763..774 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 777..779 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 786..788 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 794..797 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 798..806 FT /evidence="ECO:0007829|PDB:3TG7" FT TURN 808..810 FT /evidence="ECO:0007829|PDB:3TG7" FT TURN 819..821 FT /evidence="ECO:0007829|PDB:3TG7" FT TURN 826..828 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 831..835 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 858..866 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 871..876 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 888..890 FT /evidence="ECO:0007829|PDB:3TG7" FT HELIX 892..896 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 899..907 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 914..921 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 923..929 FT /evidence="ECO:0007829|PDB:3TG7" FT STRAND 937..945 FT /evidence="ECO:0007829|PDB:3TG7" SQ SEQUENCE 952 AA; 108007 MW; 822CCDE26E970C5A CRC64; MATPSMMPQW SYMHISGQDA SEYLSPGLVQ FARATETYFS LNNKFRNPTV APTHDVTTDR SQRLTLRFIP VDREDTAYSY KARFTLAVGD NRVLDMASTY FDIRGVLDRG PTFKPYSGTA YNALAPKGAP NPCEWDEAAT ALEINLEEED DDNEDEVDEQ AEQQKTHVFG QAPYSGINIT KEGIQIGVEG QTPKYADKTF QPEPQIGESQ WYETEINHAA GRVLKKTTPM KPCYGSYAKP TNENGGQGIL VKQQNGKLES QVEMQFFSTT EATAGNGDNL TPKVVLYSED VDIETPDTHI SYMPTIKEGN SRELMGQQSM PNRPNYIAFR DNFIGLMYYN STGNMGVLAG QASQLNAVVD LQDRNTELSY QLLLDSIGDR TRYFSMWNQA VDSYDPDVRI IENHGTEDEL PNYCFPLGGV INTETLTKVK PKTGQENGWE KDATEFSDKN EIRVGNNFAM EINLNANLWR NFLYSNIALY LPDKLKYSPS NVKISDNPNT YDYMNKRVVA PGLVDCYINL GARWSLDYMD NVNPFNHHRN AGLRYRSMLL GNGRYVPFHI QVPQKFFAIK NLLLLPGSYT YEWNFRKDVN MVLQSSLGND LRVDGASIKF DSICLYATFF PMAHNTASTL EAMLRNDTND QSFNDYLSAA NMLYPIPANA TNVPISIPSR NWAAFRGWAF TRLKTKETPS LGSGYDPYYT YSGSIPYLDG TFYLNHTFKK VAITFDSSVS WPGNDRLLTP NEFEIKRSVD GEGYNVAQCN MTKDWFLVQM LANYNIGYQG FYIPESYKDR MYSFFRNFQP MSRQVVDDTK YKDYQQVGIL HQHNNSGFVG YLAPTMREGQ AYPANFPYPL IGKTAVDSIT QKKFLCDRTL WRIPFSSNFM SMGALTDLGQ NLLYANSAHA LDMTFEVDPM DEPTLLYVLF EVFDVVRVHR PHRGVIETVY LRTPFSAGNA TT //