CAPSH_ADE05
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 03-AUG-2022, entry version 146.
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.
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}.
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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 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 SMR; P04133; -.
DR IntAct; P04133; 2.
DR PRIDE; P04133; -.
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; 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; 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 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
