ID   CAPSP_ADEGX             Reviewed;         525 AA.
AC   P32538;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   23-FEB-2022, entry version 57.
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 C serotype 10 (strain SA2) (FAdV-10) (Fowl adenovirus 10).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus C.
OX   NCBI_TaxID=10547;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1316685; DOI=10.1016/0042-6822(92)90546-2;
RA   Sheppard M., Trist H.;
RT   "Characterization of the avian adenovirus penton base.";
RL   Virology 188:881-886(1992).
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; M87008; AAA42517.1; -; Genomic_DNA.
DR   PIR; A42546; XZAD10.
DR   SMR; P32538; -.
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   T=25 icosahedral capsid protein; Viral attachment to host cell;
KW   Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW   Virus entry into host cell.
FT   CHAIN           1..525
FT                   /note="Penton protein"
FT                   /id="PRO_0000221880"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  57406 MW;  474F1CB37541A6FA CRC64;
     MWGLQPPTSI PPPPPPTELT PSTYPAMVNG YPPPAASAQS CSSSGGQSEL YMPLQRVMAP
     TGGRNSIKYR DYTPCRNTTK LFYVDNKASD IDTYNKDANH SNFRTTVIHN QDLDADTAAT
     ESIQLDNRSC WGGDLKTAVR TNCPNVSSFF QSNSVRVRMM WKRDPPTSTA PPSAVGSGYS
     VPGAQYKWYD LTVPEGNYAL CELIDLLNEG IVQLYLSEGR QNNVQKSDIG VKFDTRNFGL
     LRDPVTGLVT PGTYVYKGYH PDIVLLPGCA IDFTYSRLSL LLGIGKREPY SKGFVITYED
     LQGGDIPALL DLDSVDVNDA DGEVIELDNA APLLHDSAGV SYNVIYDQVT GKPVTAYRSW
     MLAYNVPNSQ ANQTTLLTVP DMAGGIGAMY TSLPDTFIAP TGFKEDNTTN LCPVVGMNLF
     PTYNKIYYQA ASTYVQRLEN SCQSATAAFN RFPENEILKQ APPMNVSSVC DNQPAVVQQG
     VLPVKSSLPG LQRVLITDDQ RRPIPYVYKS IATVQPTVLS SATLQ