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Database: UniProt
Entry: CORE5_ADECC
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Original site: CORE5_ADECC 
ID   CORE5_ADECC             Reviewed;         421 AA.
AC   Q65952;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 51.
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   Canine adenovirus serotype 1 (strain CLL) (CAdV-1) (Canine adenovirus 1
OS   (strain CLL)).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX   NCBI_TaxID=69150;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Campbell J.B., Zhao Y.;
RT   "DNA sequence and genomic organization of canine adenovirus type 1.";
RL   Submitted (AUG-1996) 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; U55001; AAB05440.1; -; 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.
DR   Pfam; PF03910; Adeno_PV; 1.
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..421
FT                   /note="Core-capsid bridging protein"
FT                   /id="PRO_0000221908"
SQ   SEQUENCE   421 AA;  47538 MW;  C84536291CDDEEF9 CRC64;
     MAAISRAIKQ ELLEDLKPEM YLPPKSTRRR AKVKTEEKVD VKTLVKSKSK KRRAAKNELE
     ENVEFVRRFA PRRPYQWRGR QVRALPRPGI PVVFTPGQRS GVASKRSYDE VYADEDVLDQ
     SGNMINEFAY GKRVKMLTHK NPTPSQVPIT PQEPIARPGE AGLLPTVQVL APRDSKHETM
     LPVTKSEGGD VKVENKGFEQ ITPQLGVQTV DIKVPVKRKS EVEDEILKRA KMEPFETTVK
     MEYSEQPQVE VFDTGVEPSS FFEVRSQARP IAVARKRRVP TVEVMEVQQS DHTAPTASAA
     PVANVIVGPH LSRRPSRWGP ANAIYPDYVY HPSISAKKTM GPRPTGRVSR WGPANSIFPE
     VRLHPSMVSA VTRAAPRKST KSRRRRRVRT RRAFVLPAGT KTGVMLPQNI RYHPSILFRR
     A
//
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