GenomeNet

Database: UniProt
Entry: Q6QPH9_9ADEN
LinkDB: Q6QPH9_9ADEN
Original site: Q6QPH9_9ADEN 
ID   Q6QPH9_9ADEN            Unreviewed;       347 AA.
AC   Q6QPH9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   22-FEB-2023, entry version 35.
DE   RecName: Full=Core-capsid bridging protein {ECO:0000256|HAMAP-Rule:MF_04053};
DE   AltName: Full=Core protein V {ECO:0000256|HAMAP-Rule:MF_04053};
GN   Name=L2 {ECO:0000256|HAMAP-Rule:MF_04053};
OS   Simian adenovirus E22.
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus E.
OX   NCBI_TaxID=175569 {ECO:0000313|EMBL:AAS10366.1, ECO:0000313|Proteomes:UP000161138};
RN   [1] {ECO:0000313|EMBL:AAS10366.1, ECO:0000313|Proteomes:UP000161138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-591 {ECO:0000313|EMBL:AAS10366.1};
RX   PubMed=15207622; DOI=10.1016/j.virol.2004.03.047;
RA   Roy S., Gao G., Clawson D.S., Vandenberghe L.H., Farina S.F., Wilson J.M.;
RT   "Complete nucleotide sequences and genome organization of four chimpanzee
RT   adenoviruses.";
RL   Virology 324:361-372(2004).
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:0000256|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:0000256|HAMAP-Rule:MF_04053}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04053}. Host
CC       nucleus, host nucleolus {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_04053}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_04053}.
CC   -!- MISCELLANEOUS: This protein is only encoded by mastadenoviruses, and
CC       may therefore play a role in mammals tropism. {ECO:0000256|HAMAP-
CC       Rule:MF_04053}.
CC   -!- SIMILARITY: Belongs to the adenoviridae core-capsid bridging protein
CC       family. {ECO:0000256|ARBA:ARBA00008293, ECO:0000256|HAMAP-
CC       Rule:MF_04053}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY530876; AAS10366.1; -; Genomic_DNA.
DR   Proteomes; UP000161138; Genome.
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   2: Evidence at transcript level;
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_04053};
KW   Host nucleus {ECO:0000256|HAMAP-Rule:MF_04053};
KW   Late protein {ECO:0000256|HAMAP-Rule:MF_04053};
KW   Viral capsid assembly {ECO:0000256|HAMAP-Rule:MF_04053};
KW   Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04053};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04053}.
FT   REGION          227..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..313
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   347 AA;  39571 MW;  D4581AEB350E15BD CRC64;
     MSKRKFKEEM LQVIAPEIYG PAAVKEERKP RKLKRVKKDK KEEEDVDGLV EFVREFAPRR
     RVQWRGRKVK PVLRPGTTVV FTPGERSGSA SKRSYDEVYG DEDILEQAAE RLGEFAYGKR
     SRPAPLKEEA VSIPLDHGNP TPSLKPVTLQ QVLPGAAPRR GFKREGGEDL YPTMQLMVPK
     RQKLEDVLEH MKVDPEVQPE VKVRPIKQVA PGLGVQTVDI KIPTEPMETQ TEPVKPSTST
     MEVQTDPWMP APASTTRRRR KYGAASLLMP NYALHPSIIP TPGYRGTRFY RGYTSSRRRK
     TTTRRRRRRT RRSSTATSAA ALVRRVYRSG REPLTLPRAR YHPSIAI
//
DBGET integrated database retrieval system