ID   CORE5_ADEM1             Reviewed;         228 AA.
AC   O10442;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Core-capsid bridging protein {ECO:0000255|HAMAP-Rule:MF_04053};
DE   AltName: Full=Core protein V {ECO:0000255|HAMAP-Rule:MF_04053};
GN   Name=L2 {ECO:0000255|HAMAP-Rule:MF_04053};
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: Associates loosely with the viral DNA to form an outer shell
CC       around the nucleoprotein-DNA complex and links it with the capsid by
CC       binding the endosome lysis protein. Dissociates from the viral genome
CC       during entry. Might be involved in nuclear capsid assembly of the viral
CC       particles through its association with NPM1/nucleophosmin.
CC       {ECO:0000255|HAMAP-Rule:MF_04053}.
CC   -!- SUBUNIT: Monomer. Homodimer. Exists in equilibrium between monomers and
CC       dimers in solution. Interacts with the histone-like nucleoprotein; this
CC       interactions bridge the virus core to the capsid. Interacts with core
CC       protein X; this interactions bridge the virus core to the capsid.
CC       Interacts with the endosome lysis protein VI; this interactions bridge
CC       the virus core to the capsid. Interacts with the peripentonal hexons.
CC       Interacts with host NPM1; this interaction might play a role in virus
CC       assembly. {ECO:0000255|HAMAP-Rule:MF_04053}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04053}. Host
CC       nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04053}. Note=Located
CC       inside the capsid (core). Present in 157 copies per virion. Localizes
CC       in the nucleoli during infection, then translocates from the nucleoli
CC       to the nucleoplasm as the infection progresses and is finally
CC       incorporated into the viral particles. {ECO:0000255|HAMAP-
CC       Rule:MF_04053}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000255|HAMAP-Rule:MF_04053}.
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_04053}.
CC   -!- MISCELLANEOUS: This protein is only encoded by mastadenoviruses, and
CC       may therefore play a role in mammals tropism. {ECO:0000255|HAMAP-
CC       Rule:MF_04053}.
CC   -!- SIMILARITY: Belongs to the adenoviridae core-capsid bridging protein
CC       family. {ECO:0000255|HAMAP-Rule:MF_04053, ECO:0000305}.
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DR   EMBL; U95843; AAB53757.1; -; Genomic_DNA.
DR   GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04053; ADV_CORE5; 1.
DR   InterPro; IPR005608; Adeno_V.
PE   3: Inferred from homology;
KW   DNA-binding; Host nucleus; Late protein; Viral capsid assembly;
KW   Viral release from host cell; Virion.
FT   CHAIN           1..228
FT                   /note="Core-capsid bridging protein"
FT                   /id="PRO_0000221910"
FT   REGION          146..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..169
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   228 AA;  25572 MW;  660FD493F3F2F08E CRC64;
     MEDSRVYLDR SNATPSYIPV TPQIPVPGLG HRRVKREHVQ VDEEPTVQIL IKRPKVEDEE
     VPIPIFPPLP PARDPVAAVA AAGGQIVRRR RRRVPGTAMG VDTVDVVLPV GVRYHPSIEA
     ARPPAVPPPR AVPPVGVRYH PSIEVARPPA ARISPPRRRR RRRRSPRPRA TAAYRSSAEV
     VERRRRVAQT VPVVRYHPSI QVEPAVHPPL APRLPVQMAY TRYHPTIH