CORE5_ADE02
ID CORE5_ADE02 Reviewed; 369 AA.
AC P03267;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=10515;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6094534; DOI=10.1016/s0021-9258(18)89841-6;
RA Alestroem P., Akusjaervi G., Lager M., Yeh-kai L., Pettersson U.;
RT "Genes encoding the core proteins of adenovirus type 2.";
RL J. Biol. Chem. 259:13980-13985(1984).
RN [2]
RP PROTEIN SEQUENCE OF 75-89 AND 164-179, AND PHOSPHORYLATION AT THR-85 AND
RP SER-166.
RX PubMed=22939182; DOI=10.1016/j.virol.2012.08.012;
RA Bergstrom Lind S., Artemenko K.A., Elfineh L., Zhao Y., Bergquist J.,
RA Pettersson U.;
RT "The phosphoproteome of the adenovirus type 2 virion.";
RL Virology 433:253-261(2012).
RN [3]
RP INTERACTION WITH THE HISTONE-LIKE NUCLEOPROTEIN AND PROTEIN X.
RX PubMed=4020954; DOI=10.1128/jvi.55.2.379-386.1985;
RA Chatterjee P.K., Vayda M.E., Flint S.J.;
RT "Interactions among the three adenovirus core proteins.";
RL J. Virol. 55:379-386(1985).
RN [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH THE ENDOSOME LYSIS PROTEIN VI.
RX PubMed=9680130; DOI=10.1099/0022-1317-79-7-1671;
RA Matthews D.A., Russell W.C.;
RT "Adenovirus core protein V is delivered by the invading virus to the
RT nucleus of the infected cell and later in infection is associated with
RT nucleoli.";
RL J. Gen. Virol. 79:1671-1675(1998).
RN [5]
RP INTERACTION WITH HOST NPM1.
RX PubMed=17602943; DOI=10.1016/j.febslet.2007.06.024;
RA Samad M.A., Okuwaki M., Haruki H., Nagata K.;
RT "Physical and functional interaction between a nucleolar protein
RT nucleophosmin/B23 and adenovirus basic core proteins.";
RL FEBS Lett. 581:3283-3288(2007).
RN [6]
RP FUNCTION.
RX PubMed=21047958; DOI=10.1128/jvi.01571-10;
RA Puntener D., Engelke M.F., Ruzsics Z., Strunze S., Wilhelm C., Greber U.F.;
RT "Stepwise loss of fluorescent core protein V from human adenovirus during
RT entry into cells.";
RL J. Virol. 85:481-496(2011).
RN [7]
RP FUNCTION.
RX PubMed=22717133; DOI=10.1016/j.virol.2012.05.028;
RA Ugai H., Dobbins G.C., Wang M., Le L.P., Matthews D.A., Curiel D.T.;
RT "Adenoviral protein V promotes a process of viral assembly through
RT nucleophosmin 1.";
RL Virology 432:283-295(2012).
RN [8]
RP REVIEW.
RX PubMed=22754652; DOI=10.3390/v4050847;
RA San Martin C.;
RT "Latest insights on adenovirus structure and assembly.";
RL Viruses 4:847-877(2012).
RN [9]
RP REVIEW.
RX PubMed=22116065; DOI=10.1093/nar/gkr1076;
RA Giberson A.N., Davidson A.R., Parks R.J.;
RT "Chromatin structure of adenovirus DNA throughout infection.";
RL Nucleic Acids Res. 40:2369-2376(2012).
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, ECO:0000269|PubMed:21047958,
CC ECO:0000269|PubMed:22717133}.
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 ECO:0000269|PubMed:17602943, ECO:0000269|PubMed:4020954,
CC ECO:0000269|PubMed:9680130}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04053}. Host
CC nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04053,
CC ECO:0000269|PubMed:9680130}. Note=Located inside the capsid (core).
CC Present in 157 copies per virion. Localizes in the nucleoli during
CC infection, then translocates from the nucleoli to the nucleoplasm as
CC the infection progresses and is finally incorporated into the viral
CC particles. {ECO:0000255|HAMAP-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; J01917; AAA92213.1; -; Genomic_DNA.
DR PIR; A03837; FOADM2.
DR RefSeq; AP_000172.1; AC_000007.1.
DR RefSeq; NP_040523.1; NC_001405.1.
DR iPTMnet; P03267; -.
DR PRIDE; P03267; -.
DR GeneID; 2652996; -.
DR Proteomes; UP000008167; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Host nucleus; Late protein;
KW Phosphoprotein; Reference proteome; Viral capsid assembly;
KW Viral release from host cell; Virion.
FT CHAIN 1..369
FT /note="Core-capsid bridging protein"
FT /id="PRO_0000221903"
FT REGION 15..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..341
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000269|PubMed:22939182"
FT MOD_RES 166
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:22939182"
SQ SEQUENCE 369 AA; 41721 MW; 577C9E645EB5E7DE CRC64;
MSKRKIKEEM LQVIAPEIYG PPKKEEQDYK PRKLKRVKKK KKDDDDDELD DEVELLHATA
PRRRVQWKGR RVRRVLRPGT TVVFTPGERS TRTYKRVYDE VYGDEDLLEQ ANERLGEFAY
GKRHKDMLAL PLDEGNPTPS LKPVTLQQVL PTLAPSEEKR GLKRESGDLA PTVQLMVPKR
QRLEDVLEKM TVEPGLEPEV RVRPIKQVAP GLGVQTVDVQ IPTTSSTSIA TATEGMETQT
SPVASAVADA AVQAAAAAAS KTSTEVQTDP WMFRVSAPRR PRRSRKYGTA SALLPEYALH
PSIAPTPGYR GYTYRPRRRA TTRRRTTTGT RRRRRRRQPV LAPISVRRVA REGGRTLVLP
TARYHPSIV
