CAPSH_ADE02
ID CAPSH_ADE02 Reviewed; 968 AA.
AC P03277;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 135.
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 2 (HAdV-2) (Human adenovirus 2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=10515;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6501284; DOI=10.1016/s0021-9258(18)89840-4;
RA Akusjaervi G., Alestroem P., Pettersson M., Lager M., Joernvall H.,
RA Pettersson U.;
RT "The gene for the adenovirus 2 hexon polypeptide.";
RL J. Biol. Chem. 259:13976-13979(1984).
RN [2]
RP PROTEIN SEQUENCE OF 2-455 AND 457-968.
RX PubMed=6263909; DOI=10.1016/s0021-9258(19)69145-3;
RA Joernvall H., Akusjaervi G., Alestroem P., von Bahr-Lindstroem H.,
RA Pettersson U., Appella E., Fowler A.V., Philipson L.;
RT "The adenovirus hexon protein. The primary structure of the polypeptide and
RT its correlation with the hexon gene.";
RL J. Biol. Chem. 256:6181-6186(1981).
RN [3]
RP PROTEIN SEQUENCE OF 173-188; 273-287 AND 950-958, AND PHOSPHORYLATION AT
RP SER-182; SER-283 AND TYR-956.
RX PubMed=22939182; DOI=10.1016/j.virol.2012.08.012;
RA Bergstrom Lind S., Artemenko K.A., Elfineh L., Zhao Y., Bergquist J.,
RA Pettersson U.;
RT "The phosphoproteome of the adenovirus type 2 virion.";
RL Virology 433:253-261(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 923-967.
RX PubMed=6259616; DOI=10.1093/nar/9.1.1;
RA Akusjaervi G., Zabielski J., Perricaudet M., Pettersson U.;
RT "The sequence of the 3' non-coding region of the hexon mRNA discloses a
RT novel adenovirus gene.";
RL Nucleic Acids Res. 9:1-17(1981).
RN [5]
RP INTERACTION WITH SHUTOFF PROTEIN.
RX PubMed=7159928; DOI=10.1016/0092-8674(82)90134-9;
RA Cepko C.L., Sharp P.A.;
RT "Assembly of adenovirus major capsid protein is mediated by a nonvirion
RT protein.";
RL Cell 31:407-415(1982).
RN [6]
RP ACETYLATION AT ALA-2.
RX PubMed=4823869; DOI=10.1016/0006-291x(74)90842-0;
RA Joernvall H., Ohlsson H., Philipson L.;
RT "An acetylated N-terminus of adenovirus type 2 hexon protein.";
RL Biochem. Biophys. Res. Commun. 56:304-310(1974).
RN [7]
RP INTERACTION WITH PRE-PROTEIN VI.
RX PubMed=7636476; DOI=10.1099/0022-1317-76-8-1959;
RA Matthews D.A., Russell W.C.;
RT "Adenovirus protein-protein interactions: molecular parameters governing
RT the binding of protein VI to hexon and the activation of the adenovirus 23K
RT protease.";
RL J. Gen. Virol. 76:1959-1969(1995).
RN [8]
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 [9]
RP INTERACTION WITH THE SHUTOFF PROTEIN.
RX PubMed=16081097; DOI=10.1016/j.jmb.2005.06.070;
RA Hong S.S., Szolajska E., Schoehn G., Franqueville L., Myhre S.,
RA Lindholm L., Ruigrok R.W., Boulanger P., Chroboczek J.;
RT "The 100K-chaperone protein from adenovirus serotype 2 (Subgroup C) assists
RT in trimerization and nuclear localization of hexons from subgroups C and B
RT adenoviruses.";
RL J. Mol. Biol. 352:125-138(2005).
RN [10]
RP INTERACTION WITH HUMAN DYNEINS DYNC1LI1 AND DYNC1I2.
RC STRAIN=Human adenovirus C serotype 5;
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 [11]
RP REVIEW.
RX PubMed=22754652; DOI=10.3390/v4050847;
RA San Martin C.;
RT "Latest insights on adenovirus structure and assembly.";
RL Viruses 4:847-877(2012).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL PARTICLE,
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAPSID VERTEX PROTEIN
RP AND HEXON-LINKING PROTEIN.
RC STRAIN=Human adenovirus C serotype 5;
RX PubMed=20798312; DOI=10.1126/science.1187433;
RA Liu H., Jin L., Koh S.B., Atanasov I., Schein S., Wu L., Zhou Z.H.;
RT "Atomic structure of human adenovirus by cryo-EM reveals interactions among
RT protein networks.";
RL Science 329:1038-1043(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=7932702; DOI=10.1006/jmbi.1994.1593;
RA Athappilly F.K., Murali R., Rux J.J., Cai Z., Burnett R.M.;
RT "The refined crystal structure of hexon, the major coat protein of
RT adenovirus type 2, at 2.9-A resolution.";
RL J. Mol. Biol. 242:430-455(1994).
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 ECO:0000269|PubMed:20798312}.
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 pre-protein VI; this interaction probably allows nuclear import of
CC hexon trimers and possibly pre-capsid assembly. Interacts with host
CC dyneins DYNC1LI1 and DYNC1I2; this interaction might be involved in
CC intracellular microtubule-dependent transport of incoming viral capsid.
CC Interacts with the shutoff protein; this interaction allows folding and
CC formation of hexons trimers. Interacts with host NUP214 (via N-
CC terminus); this interaction might be essential for the release of the
CC virus genome to the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:P04133, ECO:0000255|HAMAP-Rule:MF_04051,
CC ECO:0000269|PubMed:14633984, ECO:0000269|PubMed:16081097,
CC ECO:0000269|PubMed:20006841, ECO:0000269|PubMed:20798312,
CC ECO:0000269|PubMed:7159928, ECO:0000269|PubMed:7636476}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04051,
CC ECO:0000269|PubMed:20798312}. Host nucleus {ECO:0000255|HAMAP-
CC Rule:MF_04051, ECO:0000269|PubMed:20798312}. 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; J01917; AAA92215.1; -; Genomic_DNA.
DR PIR; A94597; HXAD2.
DR RefSeq; AP_000175.1; AC_000007.1.
DR RefSeq; NP_040525.1; NC_001405.1.
DR PDB; 1P2Z; X-ray; 2.20 A; A=2-968.
DR PDBsum; 1P2Z; -.
DR SMR; P03277; -.
DR DrugBank; DB04272; Citric acid.
DR iPTMnet; P03277; -.
DR GeneID; 2652998; -.
DR KEGG; vg:2652998; -.
DR EvolutionaryTrace; P03277; -.
DR Proteomes; UP000008167; 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; 3.90.39.10; -; 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; 2.
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; Direct protein sequencing;
KW Host nucleus; Host-virus interaction; Late protein;
KW Microtubular inwards viral transport; Phosphoprotein; Reference proteome;
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 ECO:0000269|PubMed:4823869, ECO:0000269|PubMed:6263909"
FT CHAIN 2..968
FT /note="Hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT /id="PRO_0000221813"
FT REGION 125..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 793
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 ECO:0000269|PubMed:4823869"
FT MOD_RES 182
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 283
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 956
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000269|PubMed:22939182"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:1P2Z"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 77..88
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1P2Z"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:1P2Z"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 480..492
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 517..522
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 527..530
FT /evidence="ECO:0007829|PDB:1P2Z"
FT TURN 532..537
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 543..546
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 557..566
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 568..578
FT /evidence="ECO:0007829|PDB:1P2Z"
FT TURN 583..587
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 592..602
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 605..608
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 609..613
FT /evidence="ECO:0007829|PDB:1P2Z"
FT TURN 617..621
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 623..634
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 640..650
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 653..655
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 657..660
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 665..672
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 678..686
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 693..700
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 701..703
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 708..710
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 722..725
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 734..741
FT /evidence="ECO:0007829|PDB:1P2Z"
FT TURN 742..744
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 765..770
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 775..778
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 779..790
FT /evidence="ECO:0007829|PDB:1P2Z"
FT TURN 802..804
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 810..813
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 815..822
FT /evidence="ECO:0007829|PDB:1P2Z"
FT TURN 824..826
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 835..837
FT /evidence="ECO:0007829|PDB:1P2Z"
FT TURN 842..844
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 847..851
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 866..868
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 874..881
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 904..906
FT /evidence="ECO:0007829|PDB:1P2Z"
FT HELIX 908..910
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 915..923
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 930..937
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 939..945
FT /evidence="ECO:0007829|PDB:1P2Z"
FT STRAND 953..961
FT /evidence="ECO:0007829|PDB:1P2Z"
SQ SEQUENCE 968 AA; 109153 MW; 78C1C61BEFB38452 CRC64;
MATPSMMPQW SYMHISGQDA SEYLSPGLVQ FARATETYFS LNNKFRNPTV APTHDVTTDR
SQRLTLRFIP VDREDTAYSY KARFTLAVGD NRVLDMASTY FDIRGVLDRG PTFKPYSGTA
YNALAPKGAP NSCEWEQTED SGRAVAEDEE EEDEDEEEEE EEQNARDQAT KKTHVYAQAP
LSGETITKSG LQIGSDNAET QAKPVYADPS YQPEPQIGES QWNEADANAA GGRVLKKTTP
MKPCYGSYAR PTNPFGGQSV LVPDEKGVPL PKVDLQFFSN TTSLNDRQGN ATKPKVVLYS
EDVNMETPDT HLSYKPGKGD ENSKAMLGQQ SMPNRPNYIA FRDNFIGLMY YNSTGNMGVL
AGQASQLNAV VDLQDRNTEL SYQLLLDSIG DRTRYFSMWN QAVDSYDPDV RIIENHGTED
ELPNYCFPLG GIGVTDTYQA IKANGNGSGD NGDTTWTKDE TFATRNEIGV GNNFAMEINL
NANLWRNFLY SNIALYLPDK LKYNPTNVEI SDNPNTYDYM NKRVVAPGLV DCYINLGARW
SLDYMDNVNP FNHHRNAGLR YRSMLLGNGR YVPFHIQVPQ KFFAIKNLLL LPGSYTYEWN
FRKDVNMVLQ SSLGNDLRVD GASIKFDSIC LYATFFPMAH NTASTLEAML RNDTNDQSFN
DYLSAANMLY PIPANATNVP ISIPSRNWAA FRGWAFTRLK TKETPSLGSG YDPYYTYSGS
IPYLDGTFYL NHTFKKVAIT FDSSVSWPGN DRLLTPNEFE IKRSVDGEGY NVAQCNMTKD
WFLVQMLANY NIGYQGFYIP ESYKDRMYSF FRNFQPMSRQ VVDDTKYKEY QQVGILHQHN
NSGFVGYLAP TMREGQAYPA NVPYPLIGKT AVDSITQKKF LCDRTLWRIP FSSNFMSMGA
LTDLGQNLLY ANSAHALDMT FEVDPMDEPT LLYVLFEVFD VVRVHQPHRG VIETVYLRTP
FSAGNATT
