CORE5_ADE05
ID CORE5_ADE05 Reviewed; 368 AA.
AC P24938;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 23-FEB-2022, entry version 75.
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 5 (HAdV-5) (Human adenovirus 5).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=28285;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA Chroboczek J., Bieber F., Jacrot B.;
RT "The sequence of the genome of adenovirus type 5 and its comparison with
RT the genome of adenovirus type 2.";
RL Virology 186:280-285(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=23142869; DOI=10.1038/nmeth.2227;
RA Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.;
RT "De novo derivation of proteomes from transcriptomes for transcript and
RT protein identification.";
RL Nat. Methods 9:1207-1211(2012).
RN [3]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=7175505; DOI=10.1099/0022-1317-63-1-69;
RA Russell W.C., Precious B.;
RT "Nucleic acid-binding properties of adenovirus structural polypeptides.";
RL J. Gen. Virol. 63:69-79(1982).
RN [4]
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 [5]
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).
RN [6]
RP INTERACTION WITH THE ENDOSOME LYSIS PROTEIN VI, DNA-BINDING, AND SUBUNIT.
RX PubMed=24899200; DOI=10.1128/jvi.00935-14;
RA Perez-Vargas J., Vaughan R.C., Houser C., Hastie K.M., Kao C.C.,
RA Nemerow G.R.;
RT "Isolation and characterization of the DNA and protein binding activities
RT of adenovirus core protein V.";
RL J. Virol. 88:9287-9296(2014).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH ENDOSOME LYSIS PROTEIN VI AND
RP HEXON-LINKING PROTEIN VIII, INTERACTION WITH THE HEXON PROTEIN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25071205; DOI=10.1073/pnas.1408462111;
RA Reddy V.S., Nemerow G.R.;
RT "Structures and organization of adenovirus cement proteins provide insights
RT into the role of capsid maturation in virus entry and infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11715-11720(2014).
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:24899200,
CC ECO:0000269|PubMed:25071205, ECO:0000269|PubMed:7175505}.
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:24899200, ECO:0000269|PubMed:25071205}.
CC -!- INTERACTION:
CC P24938; P06748: NPM1; Xeno; NbExp=4; IntAct=EBI-7481199, EBI-78579;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04053,
CC ECO:0000269|PubMed:25071205}. Host nucleus, host nucleolus
CC {ECO:0000255|HAMAP-Rule:MF_04053}. Note=Located inside the capsid
CC (core). Present in 157 copies per virion. Localizes in the nucleoli
CC during infection, then translocates from the nucleoli to the
CC nucleoplasm as the infection progresses and is finally incorporated
CC into the viral particles. {ECO:0000255|HAMAP-Rule:MF_04053,
CC ECO:0000269|PubMed:25071205}.
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; M73260; AAA96409.1; -; Genomic_DNA.
DR PIR; C39449; FOADM5.
DR RefSeq; AP_000208.1; AC_000008.1.
DR IntAct; P24938; 2.
DR MINT; P24938; -.
DR Proteomes; UP000004992; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IDA:CACAO.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
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 DNA-binding; Host nucleus; Late protein; Viral capsid assembly;
KW Viral release from host cell; Virion.
FT CHAIN 1..368
FT /note="Core-capsid bridging protein"
FT /id="PRO_0000221904"
FT REGION 17..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..340
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 41447 MW; 722E6C6D22C692A4 CRC64;
MSKRKIKEEM LQVIAPEIYG PPKKEEQDYK PRKLKRVKKK KKDDDDELDD EVELLHATAP
RRRVQWKGRR VKRVLRPGTT VVFTPGERST RTYKRVYDEV YGDEDLLEQA NERLGEFAYG
KRHKDMLALP LDEGNPTPSL KPVTLQQVLP ALAPSEEKRG LKRESGDLAP TVQLMVPKRQ
RLEDVLEKMT VEPGLEPEVR VRPIKQVAPG LGVQTVDVQI PTTSSTSIAT ATEGMETQTS
PVASAVADAA VQAVAAAASK TSTEVQTDPW MFRVSAPRRP RGSRKYGAAS ALLPEYALHP
SIAPTPGYRG YTYRPRRRAT TRRRTTTGTR RRRRRRQPVL APISVRRVAR EGGRTLVLPT
ARYHPSIV
