CAPSP_ADEG1
ID CAPSP_ADEG1 Reviewed; 515 AA.
AC Q64755;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 68.
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 Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian
OS adenovirus gal1 (strain Phelps)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus A.
OX NCBI_TaxID=10553;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8634026; DOI=10.1007/bf01718405;
RA Akopian T.A., Lazareva S.E., Tikhomirov E.E., Karpov V.A., Naroditsky B.S.;
RT "Genes for fowl adenovirus CELO penton base and core polypeptides.";
RL Arch. Virol. 141:357-365(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8627769; DOI=10.1128/jvi.70.5.2939-2949.1996;
RA Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.;
RT "The complete DNA sequence and genomic organization of the avian adenovirus
RT CELO.";
RL J. Virol. 70:2939-2949(1996).
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, and in
CC endocytosis of virions. As the virus enters the host cell, penton
CC proteins are shed concomitant with virion acidification in the
CC endosome. {ECO:0000255|HAMAP-Rule:MF_04052}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_04052}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04052}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04052}. Note=Located at each vertex
CC of the 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 -!- 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; U46933; AAC54908.1; -; Genomic_DNA.
DR RefSeq; NP_043882.1; NC_001720.1.
DR SMR; Q64755; -.
DR GeneID; 1476561; -.
DR KEGG; vg:1476561; -.
DR Proteomes; UP000001594; 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:0075509; P:endocytosis involved in viral entry into 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 3: Inferred from homology;
KW Capsid protein; Host nucleus; Host-virus interaction; Late protein;
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..515
FT /note="Penton protein"
FT /id="PRO_0000221879"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 56722 MW; 90C389ACD686C6AC CRC64;
MYRSLRPPTS IPPPPPSGPS PYPAMINGYP PDVPVGSPAN GDAELFVPLQ RVMPPTGGRN
SIRYRNYAPC QNTTKFFYVD NKLSDLDTYN EDANHSNFRT TVIHNQDLDP STAATETIQL
DNRSCWGGEL KTAVKTNCPN ISSFFQSDTV RVRLMSKRDP GGTDPDAGVN NPPGAEYKWY
DLRIPEGNYA LNEIIDLLNE GIVQLYLQEG RQNNVLKSDI GVKFDTRYLD LLKDPVTGLV
TPGTYVYKGY HPDIILLPGC AVDFTFSRLS LLLGIAKREP YSKGFTITYE DLQGGNVPAL
LDLSSVQVDD QDEDVIVVAD ARPLLKDSKG VSYNVITTGV TQPQTAYRSW LLAYHTLDSP
ARNKTLLTVP DMAGGIGAMY TSMPDTFTAP AGFKEDNTTN LCPVVAMNLF PSFNKVFYQG
ASAYVQRLEN ATQSATAAFN RFPENEILKQ APPMNVSSVC DNQPAVVQQG VLPLKNSLSG
LQRVLITDDR RRPIPYVYKT IATVQPRVLS SSTLQ