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Penton protein (CP-P) (Penton base protein) (Protein III)

 CAPSP_ADE02             Reviewed;         571 AA.
P03276;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
23-MAY-2018, entry version 98.
RecName: Full=Penton protein {ECO:0000255|HAMAP-Rule:MF_04052};
Short=CP-P {ECO:0000255|HAMAP-Rule:MF_04052};
AltName: Full=Penton base protein {ECO:0000255|HAMAP-Rule:MF_04052};
AltName: Full=Protein III {ECO:0000255|HAMAP-Rule:MF_04052};
Name=L2 {ECO:0000255|HAMAP-Rule:MF_04052};
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus.
NCBI_TaxID=10515;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6334081;
Roberts R.J., O'Neill K.E., Yen C.E.;
"DNA sequences from the adenovirus 2 genome.";
J. Biol. Chem. 259:13968-13975(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 295-571.
PubMed=6094534;
Alestroem P., Akusjaervi G., Lager M., Yeh-kai L., Pettersson U.;
"Genes encoding the core proteins of adenovirus type 2.";
J. Biol. Chem. 259:13980-13985(1984).
[3]
PROTEIN SEQUENCE OF 453-473, AND PHOSPHORYLATION AT SER-455.
PubMed=22939182; DOI=10.1016/j.virol.2012.08.012;
Bergstrom Lind S., Artemenko K.A., Elfineh L., Zhao Y., Bergquist J.,
Pettersson U.;
"The phosphoproteome of the adenovirus type 2 virion.";
Virology 433:253-261(2012).
[4]
INTERACTION WITH THE FIBER PROTEIN.
PubMed=10553913; DOI=10.1038/44880;
van Raaij M.J., Mitraki A., Lavigne G., Cusack S.;
"A triple beta-spiral in the adenovirus fibre shaft reveals a new
structural motif for a fibrous protein.";
Nature 401:935-938(1999).
[5]
INTERACTION WITH WWP1 AND WWP2.
PubMed=12450395; DOI=10.1021/bi020125b;
Galinier R., Gout E., Lortat-Jacob H., Wood J., Chroboczek J.;
"Adenovirus protein involved in virus internalization recruits
ubiquitin-protein ligases.";
Biochemistry 41:14299-14305(2002).
[6]
FUNCTION.
PubMed=12221069; DOI=10.1083/jcb.200112067;
Meier O., Boucke K., Hammer S.V., Keller S., Stidwill R.P., Hemmi S.,
Greber U.F.;
"Adenovirus triggers macropinocytosis and endosomal leakage together
with its clathrin-mediated uptake.";
J. Cell Biol. 158:1119-1131(2002).
[7]
FUNCTION, AND INTERACTION WITH HOST ITGAV-ITGB5 HETERODIMER.
STRAIN=Human adenovirus C serotype 5;
PubMed=20615244; DOI=10.1186/1743-422X-7-148;
Lyle C., McCormick F.;
"Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-
negative cells.";
Virol. J. 7:148-148(2010).
[8]
REVIEW.
PubMed=22754652; DOI=10.3390/v4050847;
San Martin C.;
"Latest insights on adenovirus structure and assembly.";
Viruses 4:847-877(2012).
[9]
STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL
PARTICLE, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAPSID
VERTEX PROTEIN.
STRAIN=Human adenovirus C serotype 5;
PubMed=20798312; DOI=10.1126/science.1187433;
Liu H., Jin L., Koh S.B., Atanasov I., Schein S., Wu L., Zhou Z.H.;
"Atomic structure of human adenovirus by cryo-EM reveals interactions
among protein networks.";
Science 329:1038-1043(2010).
[10]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 49-571.
PubMed=15629723; DOI=10.1016/j.molcel.2004.11.041;
Zubieta C., Schoehn G., Chroboczek J., Cusack S.;
"The structure of the human adenovirus 2 penton.";
Mol. Cell 17:121-135(2005).
[11]
STRUCTURE BY ELECTRON MICROSCOPY (10.0 ANGSTROMS) OF 49-571.
STRAIN=Human adenovirus C serotype 5;
PubMed=15861131; DOI=10.1038/sj.emboj.7600653;
Fabry C.M., Rosa-Calatrava M., Conway J.F., Zubieta C., Cusack S.,
Ruigrok R.W., Schoehn G.;
"A quasi-atomic model of human adenovirus type 5 capsid.";
EMBO J. 24:1645-1654(2005).
[12]
X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 49-571.
PubMed=16939624; DOI=10.1111/j.1742-4658.2006.05430.x;
Zubieta C., Blanchoin L., Cusack S.;
"Structural and biochemical characterization of a human adenovirus
2/12 penton base chimera.";
FEBS J. 273:4336-4345(2006).
-!- FUNCTION: Major capsid protein that self-associates to form penton
base pentamers, each in the shape of a pentagon, situated at the
12 vertices of the pseudo T=25 capsid. Involved in virus secondary
attachment to host cell after initial attachment by the fiber
protein. Binds host integrin heterodimer ITGAV-ITGB5 (alphaV-
beta5) thereby triggering clathrin-mediated endocytosis of
virions. Mediates initial virus attachment to CXADR-negative
cells. Binding to integrins ITGAV-ITGB5 also seems to induce
macropinocytosis uptake of the virus. As the virus enters the host
cell, penton proteins are shed concomitant with virion
acidification in the endosome. {ECO:0000255|HAMAP-Rule:MF_04052,
ECO:0000269|PubMed:12221069, ECO:0000269|PubMed:20615244,
ECO:0000269|PubMed:20798312}.
-!- SUBUNIT: Interacts with the fiber protein (via N-terminal tail
region). Interacts with the capsid vertex protein; this
interaction binds the penton base to neighboring peripentonal
hexons. Interacts (via the cell attachment site RGD) with host
heterodimer ITGAV-ITGB5; this interaction promotes virus
internalization. Interacts with host WWP1 and WWP2.
{ECO:0000255|HAMAP-Rule:MF_04052, ECO:0000269|PubMed:10553913,
ECO:0000269|PubMed:12450395, ECO:0000269|PubMed:20615244,
ECO:0000269|PubMed:20798312}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04052,
ECO:0000269|PubMed:20798312}. Host nucleus {ECO:0000255|HAMAP-
Rule:MF_04052}. Note=Located at each vertex of the virion. Present
in 60 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04052}.
-!- INDUCTION: Expressed in the late phase of the viral replicative
cycle. {ECO:0000255|HAMAP-Rule:MF_04052}.
-!- DOMAIN: The cell attachment RGD motif is exposed at the virion
surface and is involved in binding to the integrin heterodimer
ITGAV-ITGB5. {ECO:0000255|HAMAP-Rule:MF_04052}.
-!- MISCELLANEOUS: All late proteins expressed from the major late
promoter are produced by alternative splicing and alternative
polyadenylation of the same gene giving rise to non-overlapping
ORFs. A leader sequence is present in the N-terminus of all these
mRNAs and is recognized by the viral shutoff protein to provide
expression although conventional translation via ribosome scanning
from the cap has been shut off in the host cell.
{ECO:0000255|HAMAP-Rule:MF_04052}.
-!- SIMILARITY: Belongs to the adenoviridae penton family.
{ECO:0000255|HAMAP-Rule:MF_04052}.
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1x9p";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with an ad2 N-terminal fiber peptide;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1x9t";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; J01917; AAA92211.1; -; Genomic_DNA.
PIR; A03847; XZAD32.
RefSeq; AP_000170.1; AC_000007.1.
RefSeq; NP_040521.1; NC_001405.1.
PDB; 1X9P; X-ray; 3.30 A; A=49-571.
PDB; 1X9T; X-ray; 3.50 A; A=49-571.
PDB; 2C6S; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=49-571.
PDB; 2C9F; EM; 16.50 A; A/B/C/D/E=49-571.
PDB; 2C9G; EM; 9.30 A; A/B/C/D/E=49-571.
PDB; 4V4U; EM; 10.00 A; A/B/C/D/E=49-571.
PDBsum; 1X9P; -.
PDBsum; 1X9T; -.
PDBsum; 2C6S; -.
PDBsum; 2C9F; -.
PDBsum; 2C9G; -.
PDBsum; 4V4U; -.
ProteinModelPortal; P03276; -.
SMR; P03276; -.
ELM; P03276; -.
iPTMnet; P03276; -.
PRIDE; P03276; -.
GeneID; 2652996; -.
KEGG; vg:2652996; -.
OrthoDB; VOG09000071; -.
EvolutionaryTrace; P03276; -.
Proteomes; UP000008167; Genome.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0039623; C:T=25 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
HAMAP; MF_04052; ADV_CAPSP; 1.
InterPro; IPR002605; Adeno_Penton_B.
Pfam; PF01686; Adeno_Penton_B; 1.
1: Evidence at protein level;
3D-structure; Capsid protein;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Direct protein sequencing; Host nucleus; Host-virus interaction;
Late protein; Phosphoprotein; Reference proteome;
T=25 icosahedral capsid protein; Viral attachment to host cell;
Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 571 Penton protein.
/FTId=PRO_0000221872.
REGION 336 348 Disordered. {ECO:0000255|HAMAP-
Rule:MF_04052}.
MOTIF 340 342 Cell attachment site. {ECO:0000255|HAMAP-
Rule:MF_04052}.
MOD_RES 455 455 Phosphoserine; by host.
{ECO:0000269|PubMed:22939182}.
TURN 50 52 {ECO:0000244|PDB:1X9P}.
STRAND 55 57 {ECO:0000244|PDB:1X9T}.
STRAND 58 60 {ECO:0000244|PDB:1X9P}.
STRAND 69 73 {ECO:0000244|PDB:1X9P}.
HELIX 76 81 {ECO:0000244|PDB:1X9P}.
STRAND 82 85 {ECO:0000244|PDB:1X9P}.
STRAND 90 94 {ECO:0000244|PDB:1X9P}.
STRAND 99 101 {ECO:0000244|PDB:1X9T}.
HELIX 103 106 {ECO:0000244|PDB:1X9P}.
STRAND 110 113 {ECO:0000244|PDB:1X9P}.
STRAND 117 129 {ECO:0000244|PDB:1X9P}.
TURN 136 139 {ECO:0000244|PDB:1X9P}.
STRAND 141 152 {ECO:0000244|PDB:1X9P}.
STRAND 155 158 {ECO:0000244|PDB:1X9P}.
STRAND 160 169 {ECO:0000244|PDB:1X9P}.
HELIX 177 194 {ECO:0000244|PDB:1X9P}.
TURN 195 200 {ECO:0000244|PDB:1X9P}.
HELIX 203 205 {ECO:0000244|PDB:1X9P}.
STRAND 209 213 {ECO:0000244|PDB:1X9T}.
STRAND 217 220 {ECO:0000244|PDB:1X9P}.
TURN 221 224 {ECO:0000244|PDB:1X9P}.
STRAND 235 242 {ECO:0000244|PDB:1X9T}.
STRAND 247 249 {ECO:0000244|PDB:1X9P}.
HELIX 255 259 {ECO:0000244|PDB:1X9P}.
STRAND 261 265 {ECO:0000244|PDB:1X9P}.
STRAND 267 269 {ECO:0000244|PDB:1X9P}.
STRAND 272 274 {ECO:0000244|PDB:1X9P}.
HELIX 275 277 {ECO:0000244|PDB:1X9P}.
STRAND 282 284 {ECO:0000244|PDB:1X9P}.
HELIX 289 294 {ECO:0000244|PDB:1X9P}.
TURN 349 353 {ECO:0000244|PDB:1X9P}.
TURN 386 388 {ECO:0000244|PDB:1X9P}.
STRAND 393 397 {ECO:0000244|PDB:1X9P}.
STRAND 399 405 {ECO:0000244|PDB:1X9P}.
HELIX 406 412 {ECO:0000244|PDB:1X9P}.
TURN 415 417 {ECO:0000244|PDB:1X9P}.
HELIX 419 422 {ECO:0000244|PDB:1X9P}.
STRAND 423 425 {ECO:0000244|PDB:1X9P}.
STRAND 436 439 {ECO:0000244|PDB:1X9P}.
TURN 442 444 {ECO:0000244|PDB:1X9P}.
HELIX 457 459 {ECO:0000244|PDB:1X9P}.
STRAND 464 467 {ECO:0000244|PDB:1X9P}.
STRAND 469 475 {ECO:0000244|PDB:1X9P}.
HELIX 479 482 {ECO:0000244|PDB:1X9P}.
HELIX 483 485 {ECO:0000244|PDB:1X9P}.
STRAND 487 489 {ECO:0000244|PDB:1X9P}.
TURN 495 497 {ECO:0000244|PDB:1X9T}.
STRAND 503 506 {ECO:0000244|PDB:1X9P}.
STRAND 512 519 {ECO:0000244|PDB:1X9P}.
STRAND 522 531 {ECO:0000244|PDB:1X9P}.
STRAND 533 542 {ECO:0000244|PDB:1X9P}.
STRAND 554 568 {ECO:0000244|PDB:1X9P}.
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


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