NP_ADE05
ID NP_ADE05 Reviewed; 198 AA.
AC P68951; P03266; P12542;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 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 [GENOMIC DNA] OF 1-136.
RX PubMed=3224820; DOI=10.1016/0378-1119(88)90389-7;
RA Neumann R., Chroboczek J., Jacrot B.;
RT "Determination of the nucleotide sequence for the penton-base gene of human
RT adenovirus type 5.";
RL Gene 69:153-157(1988).
RN [3]
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 [4]
RP 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 [5]
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 [6]
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: 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}.
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 -!- INTERACTION:
CC P68951; P06748: NPM1; Xeno; NbExp=5; IntAct=EBI-7481182, EBI-78579;
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96408.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M73260; AAA96408.1; ALT_INIT; Genomic_DNA.
DR EMBL; M22141; AAA42520.1; -; Genomic_DNA.
DR RefSeq; AP_000207.1; AC_000008.1.
DR PDB; 6B1T; EM; 3.20 A; W=14-24.
DR PDBsum; 6B1T; -.
DR SMR; P68951; -.
DR DIP; DIP-44057N; -.
DR IntAct; P68951; 3.
DR MINT; P68951; -.
DR Proteomes; UP000004992; 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 3D-structure; Acetylation; DNA-binding; Host nucleus;
KW Host-virus interaction; Late protein; Phosphoprotein;
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 CHAIN 2..198
FT /note="Pre-histone-like nucleoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT /id="PRO_0000421134"
FT PROPEP 2..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT /id="PRO_0000036579"
FT CHAIN 25..198
FT /note="Histone-like nucleoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT /id="PRO_0000036580"
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 MOD_RES 27
FT /note="N6-acetyllysine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT MOD_RES 48
FT /note="N6-acetyllysine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT MOD_RES 55
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT MOD_RES 74
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT MOD_RES 183
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
FT MOD_RES 185
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04056"
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
