CAPSP_ADE02
ID CAPSP_ADE02 Reviewed; 571 AA.
AC P03276;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Penton protein {ECO:0000255|HAMAP-Rule:MF_04052};
DE Short=CP-P {ECO:0000255|HAMAP-Rule:MF_04052};
DE AltName: Full=Penton base protein {ECO:0000255|HAMAP-Rule:MF_04052};
DE AltName: Full=Protein III {ECO:0000255|HAMAP-Rule:MF_04052};
GN Name=L2 {ECO:0000255|HAMAP-Rule:MF_04052};
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=6334081; DOI=10.1016/s0021-9258(18)89839-8;
RA Roberts R.J., O'Neill K.E., Yen C.E.;
RT "DNA sequences from the adenovirus 2 genome.";
RL J. Biol. Chem. 259:13968-13975(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 295-571.
RX PubMed=6094534; DOI=10.1016/s0021-9258(18)89841-6;
RA Alestroem P., Akusjaervi G., Lager M., Yeh-kai L., Pettersson U.;
RT "Genes encoding the core proteins of adenovirus type 2.";
RL J. Biol. Chem. 259:13980-13985(1984).
RN [3]
RP PROTEIN SEQUENCE OF 453-473, AND PHOSPHORYLATION AT SER-455.
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 INTERACTION WITH THE FIBER PROTEIN.
RX PubMed=10553913; DOI=10.1038/44880;
RA van Raaij M.J., Mitraki A., Lavigne G., Cusack S.;
RT "A triple beta-spiral in the adenovirus fibre shaft reveals a new
RT structural motif for a fibrous protein.";
RL Nature 401:935-938(1999).
RN [5]
RP INTERACTION WITH WWP1 AND WWP2.
RX PubMed=12450395; DOI=10.1021/bi020125b;
RA Galinier R., Gout E., Lortat-Jacob H., Wood J., Chroboczek J.;
RT "Adenovirus protein involved in virus internalization recruits ubiquitin-
RT protein ligases.";
RL Biochemistry 41:14299-14305(2002).
RN [6]
RP FUNCTION.
RX PubMed=12221069; DOI=10.1083/jcb.200112067;
RA Meier O., Boucke K., Hammer S.V., Keller S., Stidwill R.P., Hemmi S.,
RA Greber U.F.;
RT "Adenovirus triggers macropinocytosis and endosomal leakage together with
RT its clathrin-mediated uptake.";
RL J. Cell Biol. 158:1119-1131(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH HOST ITGAV-ITGB5 HETERODIMER.
RC STRAIN=Human adenovirus C serotype 5;
RX PubMed=20615244; DOI=10.1186/1743-422x-7-148;
RA Lyle C., McCormick F.;
RT "Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-negative
RT cells.";
RL Virol. J. 7:148-148(2010).
RN [8]
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 [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL PARTICLE,
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAPSID VERTEX 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 [10]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 49-571.
RX PubMed=15629723; DOI=10.1016/j.molcel.2004.11.041;
RA Zubieta C., Schoehn G., Chroboczek J., Cusack S.;
RT "The structure of the human adenovirus 2 penton.";
RL Mol. Cell 17:121-135(2005).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (10.0 ANGSTROMS) OF 49-571.
RC STRAIN=Human adenovirus C serotype 5;
RX PubMed=15861131; DOI=10.1038/sj.emboj.7600653;
RA Fabry C.M., Rosa-Calatrava M., Conway J.F., Zubieta C., Cusack S.,
RA Ruigrok R.W., Schoehn G.;
RT "A quasi-atomic model of human adenovirus type 5 capsid.";
RL EMBO J. 24:1645-1654(2005).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 49-571.
RX PubMed=16939624; DOI=10.1111/j.1742-4658.2006.05430.x;
RA Zubieta C., Blanchoin L., Cusack S.;
RT "Structural and biochemical characterization of a human adenovirus 2/12
RT penton base chimera.";
RL FEBS J. 273:4336-4345(2006).
CC -!- FUNCTION: Major capsid protein that self-associates to form penton base
CC pentamers, each in the shape of a pentagon, situated at the 12 vertices
CC of the pseudo T=25 capsid. Involved in virus secondary attachment to
CC host cell after initial attachment by the fiber protein. Binds host
CC integrin heterodimer ITGAV-ITGB5 (alphaV-beta5) thereby triggering
CC clathrin-mediated endocytosis of virions. Mediates initial virus
CC attachment to CXADR-negative cells. Binding to integrins ITGAV-ITGB5
CC also seems to induce macropinocytosis uptake of the virus. As the virus
CC enters the host cell, penton proteins are shed concomitant with virion
CC acidification in the endosome. {ECO:0000255|HAMAP-Rule:MF_04052,
CC ECO:0000269|PubMed:12221069, ECO:0000269|PubMed:20615244,
CC ECO:0000269|PubMed:20798312}.
CC -!- SUBUNIT: Interacts with the fiber protein (via N-terminal tail region).
CC Interacts with the capsid vertex protein; this interaction binds the
CC penton base to neighboring peripentonal hexons. Interacts (via the cell
CC attachment site RGD) with host heterodimer ITGAV-ITGB5; this
CC interaction promotes virus internalization. Interacts with host WWP1
CC and WWP2. {ECO:0000255|HAMAP-Rule:MF_04052,
CC ECO:0000269|PubMed:10553913, ECO:0000269|PubMed:12450395,
CC ECO:0000269|PubMed:20615244, ECO:0000269|PubMed:20798312}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04052,
CC ECO:0000269|PubMed:20798312}. Host nucleus {ECO:0000255|HAMAP-
CC Rule:MF_04052}. Note=Located at each vertex of the virion. Present in
CC 60 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04052}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04052}.
CC -!- DOMAIN: The cell attachment RGD motif is exposed at the virion surface
CC and is involved in binding to the integrin heterodimer ITGAV-ITGB5.
CC {ECO:0000255|HAMAP-Rule:MF_04052}.
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_04052}.
CC -!- SIMILARITY: Belongs to the adenoviridae penton family.
CC {ECO:0000255|HAMAP-Rule:MF_04052}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1x9p";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure in complex with an ad2 N-terminal fiber peptide;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1x9t";
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DR EMBL; J01917; AAA92211.1; -; Genomic_DNA.
DR PIR; A03847; XZAD32.
DR RefSeq; AP_000170.1; AC_000007.1.
DR RefSeq; NP_040521.1; NC_001405.1.
DR PDB; 1X9P; X-ray; 3.30 A; A=49-571.
DR PDB; 1X9T; X-ray; 3.50 A; A=49-571.
DR PDB; 2C6S; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=49-571.
DR PDB; 2C9F; EM; 16.50 A; A/B/C/D/E=49-571.
DR PDB; 2C9G; EM; 9.30 A; A/B/C/D/E=49-571.
DR PDB; 4V4U; EM; 10.00 A; A/B/C/D/E=49-571.
DR PDBsum; 1X9P; -.
DR PDBsum; 1X9T; -.
DR PDBsum; 2C6S; -.
DR PDBsum; 2C9F; -.
DR PDBsum; 2C9G; -.
DR PDBsum; 4V4U; -.
DR SMR; P03276; -.
DR ELM; P03276; -.
DR DrugBank; DB02643; N-Dodecyl-N,N-Dimethyl-3-Ammonio-1-Propanesulfonate.
DR iPTMnet; P03276; -.
DR GeneID; 2652996; -.
DR KEGG; vg:2652996; -.
DR EvolutionaryTrace; P03276; -.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04052; ADV_CAPSP; 1.
DR InterPro; IPR002605; Adeno_Penton_B.
DR Pfam; PF01686; Adeno_Penton_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host; Direct protein sequencing;
KW Host nucleus; Host-virus interaction; Late protein; Phosphoprotein;
KW Reference proteome; T=25 icosahedral capsid protein;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Virion; Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1..571
FT /note="Penton protein"
FT /id="PRO_0000221872"
FT REGION 298..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 340..342
FT /note="Cell attachment site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04052"
FT COMPBIAS 306..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 455
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:22939182"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1X9T"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1X9T"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 117..129
FT /evidence="ECO:0007829|PDB:1X9P"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 177..194
FT /evidence="ECO:0007829|PDB:1X9P"
FT TURN 195..200
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1X9T"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1X9P"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:1X9T"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:1X9P"
FT TURN 349..353
FT /evidence="ECO:0007829|PDB:1X9P"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:1X9P"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:1X9P"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:1X9P"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:1X9P"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:1X9T"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 512..519
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 522..531
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 533..542
FT /evidence="ECO:0007829|PDB:1X9P"
FT STRAND 554..568
FT /evidence="ECO:0007829|PDB:1X9P"
SQ SEQUENCE 571 AA; 63255 MW; E9807342982B1BC7 CRC64;
MQRAAMYEEG PPPSYESVVS AAPVAAALGS PFDAPLDPPF VPPRYLRPTG GRNSIRYSEL
APLFDTTRVY LVDNKSTDVA SLNYQNDHSN FLTTVIQNND YSPGEASTQT INLDDRSHWG
GDLKTILHTN MPNVNEFMFT NKFKARVMVS RSLTKDKQVE LKYEWVEFTL PEGNYSETMT
IDLMNNAIVE HYLKVGRQNG VLESDIGVKF DTRNFRLGFD PVTGLVMPGV YTNEAFHPDI
ILLPGCGVDF THSRLSNLLG IRKRQPFQEG FRITYDDLEG GNIPALLDVD AYQASLKDDT
EQGGDGAGGG NNSGSGAEEN SNAAAAAMQP VEDMNDHAIR GDTFATRAEE KRAEAEAAAE
AAAPAAQPEV EKPQKKPVIK PLTEDSKKRS YNLISNDSTF TQYRSWYLAY NYGDPQTGIR
SWTLLCTPDV TCGSEQVYWS LPDMMQDPVT FRSTSQISNF PVVGAELLPV HSKSFYNDQA
VYSQLIRQFT SLTHVFNRFP ENQILARPPA PTITTVSENV PALTDHGTLP LRNSIGGVQR
VTITDARRRT CPYVYKALGI VSPRVLSSRT F
