CAPSP_ADE05
ID CAPSP_ADE05 Reviewed; 571 AA.
AC P12538;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 94.
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 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=3224820; DOI=10.1016/0378-1119(88)90389-7;
RA Neumann R., Chroboczek J., Jacrot B.;
RT "Determination of the nucleotide sequence for the penton-base gene of human
RT adenovirus type 5.";
RL Gene 69:153-157(1988).
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] OF 131-571.
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 FUNCTION, AND INTERACTION WITH HOST ITGAV-ITGB5 HETERODIMER.
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 [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (10.0 ANGSTROMS) OF 49-571.
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 [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL PARTICLE,
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAPSID VERTEX PROTEIN.
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).
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:20615244, ECO:0000269|PubMed:20798312}.
CC -!- SUBUNIT: Interacts (via the cell attachment site RGD) with host
CC heterodimer ITGAV-ITGB5; this interaction promotes virus
CC internalization. Interacts with host WWP1 and WWP2. Interacts with the
CC fiber protein (via N-terminal tail region). Interacts with the capsid
CC vertex protein; this interaction binds the penton base to neighboring
CC peripentonal hexons. {ECO:0000255|HAMAP-Rule:MF_04052,
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}.
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DR EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M22141; AAA42519.1; -; Genomic_DNA.
DR PIR; JT0337; XZADH5.
DR RefSeq; AP_000206.1; AC_000008.1.
DR PDB; 3IZO; EM; -; A/B/C/D/E=1-571.
DR PDB; 6B1T; EM; 3.20 A; M=1-571.
DR PDB; 6CGV; X-ray; 3.80 A; N=1-571.
DR PDB; 7S78; EM; 3.72 A; N=1-571.
DR PDBsum; 3IZO; -.
DR PDBsum; 6B1T; -.
DR PDBsum; 6CGV; -.
DR PDBsum; 7S78; -.
DR SMR; P12538; -.
DR PRIDE; P12538; -.
DR EvolutionaryTrace; P12538; -.
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: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; Host nucleus;
KW Host-virus interaction; Late protein; 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_0000221873"
FT REGION 297..325
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 305..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6CGV"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:6CGV"
FT TURN 103..107
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:6CGV"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:6CGV"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:6CGV"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:6CGV"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:6CGV"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 485..489
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:6CGV"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:6CGV"
SQ SEQUENCE 571 AA; 63293 MW; 89D77207F2786802 CRC64;
MRRAAMYEEG PPPSYESVVS AAPVAAALGS PFDAPLDPPF VPPRYLRPTG GRNSIRYSEL
APLFDTTRVY LVDNKSTDVA SLNYQNDHSN FLTTVIQNND YSPGEASTQT INLDDRSHWG
GDLKTILHTN MPNVNEFMFT NKFKARVMVS RLPTKDNQVE LKYEWVEFTL PEGNYSETMT
IDLMNNAIVE HYLKVGRQNG VLESDIGVKF DTRNFRLGFD PVTGLVMPGV YTNEAFHPDI
ILLPGCGVDF THSRLSNLLG IRKRQPFQEG FRITYDDLEG GNIPALLDVD AYQASLKDDT
EQGGGGAGGS NSSGSGAEEN SNAAAAAMQP VEDMNDHAIR GDTFATRAEE KRAEAEAAAE
AAAPAAQPEV EKPQKKPVIK PLTEDSKKRS YNLISNDSTF TQYRSWYLAY NYGDPQTGIR
SWTLLCTPDV TCGSEQVYWS LPDMMQDPVT FRSTRQISNF PVVGAELLPV HSKSFYNDQA
VYSQLIRQFT SLTHVFNRFP ENQILARPPA PTITTVSENV PALTDHGTLP LRNSIGGVQR
VTITDARRRT CPYVYKALGI VSPRVLSSRT F
