NP_ADE02
ID NP_ADE02 Reviewed; 198 AA.
AC P68950; P03266; P12542;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Pre-histone-like nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04056};
DE AltName: Full=Pre-core protein VII {ECO:0000255|HAMAP-Rule:MF_04056};
DE Short=pVII {ECO:0000255|HAMAP-Rule:MF_04056};
DE Contains:
DE RecName: Full=Histone-like nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04056};
DE Short=NP {ECO:0000255|HAMAP-Rule:MF_04056};
DE AltName: Full=Core protein VII {ECO:0000255|HAMAP-Rule:MF_04056};
GN Name=L2 {ECO:0000255|HAMAP-Rule:MF_04056};
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], PROTEIN SEQUENCE OF 2-165 AND 170-196,
RP ACETYLATION AT SER-2, AND PROTEOLYTIC PROCESSING.
RX PubMed=6574459; DOI=10.1073/pnas.80.10.2902;
RA Sung M.T., Cao T.M., Coleman R.T., Budelier K.A.;
RT "Gene and protein sequences of adenovirus protein VII, a hybrid basic
RT chromosomal protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2902-2906(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEOLYTIC PROCESSING.
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 [3]
RP PROTEIN SEQUENCE OF 70-90 AND 182-188, AND PHOSPHORYLATION AT THR-74 AND
RP SER-185.
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 [4]
RP DNA-BINDING.
RC STRAIN=Human adenovirus C serotype 5;
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 [5]
RP INTERACTION WITH THE CORE-CAPSID BRIDGING PROTEIN.
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=14645923; DOI=10.1099/vir.0.19546-0;
RA Lee T.W., Blair G.E., Matthews D.A.;
RT "Adenovirus core protein VII contains distinct sequences that mediate
RT targeting to the nucleus and nucleolus, and colocalization with human
RT chromosomes.";
RL J. Gen. Virol. 84:3423-3428(2003).
RN [7]
RP FUNCTION.
RX PubMed=15163739; DOI=10.1128/jvi.78.12.6459-6468.2004;
RA Johnson J.S., Osheim Y.N., Xue Y., Emanuel M.R., Lewis P.W., Bankovich A.,
RA Beyer A.L., Engel D.A.;
RT "Adenovirus protein VII condenses DNA, represses transcription, and
RT associates with transcriptional activator E1A.";
RL J. Virol. 78:6459-6468(2004).
RN [8]
RP FUNCTION, AND NUCLEAR LOCALIZATION SIGNALS.
RX PubMed=16973564; DOI=10.1128/jvi.00850-06;
RA Wodrich H., Cassany A., D'Angelo M.A., Guan T., Nemerow G., Gerace L.;
RT "Adenovirus core protein pVII is translocated into the nucleus by multiple
RT import receptor pathways.";
RL J. Virol. 80:9608-9618(2006).
RN [9]
RP FUNCTION.
RX PubMed=17848175; DOI=10.1111/j.1600-0854.2007.00618.x;
RA Hindley C.E., Lawrence F.J., Matthews D.A.;
RT "A role for transportin in the nuclear import of adenovirus core proteins
RT and DNA.";
RL Traffic 8:1313-1322(2007).
RN [10]
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 [11]
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 [12]
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 [13]
RP FUNCTION, INTERACTION WITH HOST HMGB1, SUBCELLULAR LOCATION, ACETYLATION AT
RP LYS-27 AND LYS-48, AND PHOSPHORYLATION AT THR-55; THR-74 AND SER-183.
RX PubMed=27362237; DOI=10.1038/nature18317;
RA Avgousti D.C., Herrmann C., Kulej K., Pancholi N.J., Sekulic N.,
RA Petrescu J., Molden R.C., Blumenthal D., Paris A.J., Reyes E.D.,
RA Ostapchuk P., Hearing P., Seeholzer S.H., Worthen G.S., Black B.E.,
RA Garcia B.A., Weitzman M.D.;
RT "A core viral protein binds host nucleosomes to sequester immune danger
RT signals.";
RL Nature 535:173-177(2016).
CC -!- FUNCTION: Plays a role in the inhibition of host immune response within
CC the nucleus. Interacts with cellular nucleosomes and immobilizes the
CC host immune danger signal HMGB1 on chromatin. In turn, prevents HMGB1
CC release out of the cell and thus decreases inflammation. Also plays a
CC role in the wrapping and condensation of the viral DNA. May also
CC promote viral genome import into the nucleus. {ECO:0000255|HAMAP-
CC Rule:MF_04056, ECO:0000269|PubMed:15163739,
CC ECO:0000269|PubMed:16973564, ECO:0000269|PubMed:17848175,
CC ECO:0000269|PubMed:27362237}.
CC -!- SUBUNIT: Interacts with the core-capsid bridging protein; this
CC interaction bridges the virus core to the capsid. Interacts with host
CC NPM1; this interaction might play a role in placing the pre-histone-
CC like nucleoprotein on the viral DNA or regulating viral gene
CC expression. Interacts with host HMGB1; this interaction inhibits host
CC immune response. {ECO:0000255|HAMAP-Rule:MF_04056,
CC ECO:0000269|PubMed:17602943, ECO:0000269|PubMed:27362237,
CC ECO:0000269|PubMed:4020954}.
CC -!- SUBCELLULAR LOCATION: [Histone-like nucleoprotein]: Virion
CC {ECO:0000255|HAMAP-Rule:MF_04056}. Note=Located inside the capsid in
CC association with the viral DNA (core). Present in about 1070 copies per
CC virion. {ECO:0000255|HAMAP-Rule:MF_04056}.
CC -!- SUBCELLULAR LOCATION: [Pre-histone-like nucleoprotein]: Host nucleus,
CC host nucleolus {ECO:0000255|HAMAP-Rule:MF_04056,
CC ECO:0000269|PubMed:27362237}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04056}.
CC -!- PTM: Cleaved near the N-terminus by the viral protease during virion
CC maturation to form the mature protein. {ECO:0000255|HAMAP-
CC Rule:MF_04056}.
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_04056}.
CC -!- SIMILARITY: Belongs to the adenoviridae histone-like nucleoprotein
CC family. {ECO:0000255|HAMAP-Rule:MF_04056, ECO:0000305}.
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DR EMBL; J01917; AAA92212.1; -; Genomic_DNA.
DR PIR; C03837; FOAD72.
DR RefSeq; AP_000171.1; AC_000007.1.
DR RefSeq; NP_040522.1; NC_001405.1.
DR SMR; P68950; -.
DR iPTMnet; P68950; -.
DR PRIDE; P68950; -.
DR GeneID; 2652996; -.
DR Proteomes; UP000008167; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04056; ADV_PVII; 1.
DR InterPro; IPR004912; Adeno_VII.
DR Pfam; PF03228; Adeno_VII; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; DNA-binding; Host nucleus;
KW Host-virus interaction; Late protein; Phosphoprotein; Reference proteome;
KW Viral penetration into host nucleus; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056,
FT ECO:0000269|PubMed:6574459"
FT CHAIN 2..198
FT /note="Pre-histone-like nucleoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT /id="PRO_0000421079"
FT PROPEP 2..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT /id="PRO_0000036575"
FT CHAIN 25..198
FT /note="Histone-like nucleoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT /id="PRO_0000036576"
FT REGION 24..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 188..198
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT SITE 24..25
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT MOD_RES 2
FT /note="N-acetylserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056,
FT ECO:0000269|PubMed:6574459"
FT MOD_RES 27
FT /note="N6-acetyllysine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056,
FT ECO:0000269|PubMed:27362237"
FT MOD_RES 48
FT /note="N6-acetyllysine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056,
FT ECO:0000269|PubMed:27362237"
FT MOD_RES 55
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056,
FT ECO:0000269|PubMed:27362237"
FT MOD_RES 74
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056,
FT ECO:0000269|PubMed:22939182, ECO:0000269|PubMed:27362237"
FT MOD_RES 183
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056,
FT ECO:0000269|PubMed:27362237"
FT MOD_RES 185
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056,
FT ECO:0000269|PubMed:22939182"
FT CONFLICT 112
FT /note="Missing (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21992 MW; 7D5A8D426F08E952 CRC64;
MSILISPSNN TGWGLRFPSK MFGGAKKRSD QHPVRVRGHY RAPWGAHKRG RTGRTTVDDA
IDAVVEEARN YTPTPPPVST VDAAIQTVVR GARRYAKMKR RRRRVARRHR RRPGTAAQRA
AAALLNRARR TGRRAAMRAA RRLAAGIVTV PPRSRRRAAA AAAAAISAMT QGRRGNVYWV
RDSVSGLRVP VRTRPPRN
