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}.
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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
//