CAPSP_ADEM1
ID CAPSP_ADEM1 Reviewed; 489 AA.
AC O10439;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 Murine adenovirus A serotype 1 (MAdV-1) (Murine adenovirus 1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Murine mastadenovirus A.
OX NCBI_TaxID=10530;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Meissner J.D., Hirsch G.N., Larue E.A., Fulcher R.A., Spindler K.R.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
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; U95843; AAB53754.1; -; Genomic_DNA.
DR SMR; O10439; -.
DR PRIDE; O10439; -.
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..489
FT /note="Penton protein"
FT /id="PRO_0000221881"
SQ SEQUENCE 489 AA; 55383 MW; 066AE3DC6C0E68D0 CRC64;
MSRYGNAPPP YEEVVSVATP SYVQQPWVPP RYFAPTEGRN SIVYDQFPTC YDTTKLFLVD
NKSADITDLN MQNDHSHFAT TVVQNSEFTP REASTQHITL DNRSRWGAKL KTLIQTNLPS
VTDYMYTNSL RVKLMESYDE ATGTATYEWH DITLPEGNFD SGRIIDLLNN AIWELYLTYG
RQNGVREDQI GIKFDTRNFR LGFDPLTNLI MPGHYTYEYF HPDIVLMKGC AVDFSKTRLN
NVLGWRKRYP YQPGFVITYD DLVGGDIPPL LDLAAYLKKP REGAGGPIIR ALQKDSKGRS
YHVQYTDLGE VTGYRSLYLA YNYTSDVTHL RKSTVRSWLV LTAPDITGGA QQLYWSLPDM
ALAPTTFRPS GQTPATFPVV STEPLPIAAR TIFNAQPGYA QIVNQNTSQT MVYNRFPENA
ILMRPPQPFM VQVPENVTTV TDHGTLPLQN TLSGVQRVAV TDSRRRTCPY VYKCAATLEP
HIMSSRTLQ