COR10_ADE02
ID COR10_ADE02 Reviewed; 80 AA.
AC P14269;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Pre-core protein X;
DE Short=pX;
DE AltName: Full=11 kDa core protein;
DE AltName: Full=Protein mu;
DE Short=pMu;
DE Contains:
DE RecName: Full=Core protein X;
GN ORFNames=L2;
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=455453; DOI=10.1016/0092-8674(79)90100-4;
RA Zain S., Sambrook J., Roberts R.J., Keller W., Fried M., Dunn A.R.;
RT "Nucleotide sequence analysis of the leader segments in a cloned copy of
RT adenovirus 2 fiber mRNA.";
RL Cell 16:851-861(1979).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 2-57.
RX PubMed=3357209; DOI=10.1128/jvi.62.5.1741-1745.1988;
RA Weber J.M., Anderson C.W.;
RT "Identification of the gene coding for the precursor of adenovirus core
RT protein X.";
RL J. Virol. 62:1741-1745(1988).
RN [4]
RP INTERACTION WITH 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 [5]
RP DNA-BINDING.
RX PubMed=11781106; DOI=10.1021/bi0156299;
RA Keller M., Tagawa T., Preuss M., Miller A.D.;
RT "Biophysical characterization of the DNA binding and condensing properties
RT of adenoviral core peptide mu.";
RL Biochemistry 41:652-659(2002).
RN [6]
RP SUBCELLULAR LOCATION OF PRE-CORE PROTEIN X.
RX PubMed=14718634; DOI=10.1099/vir.0.19352-0;
RA Lee T.W., Lawrence F.J., Dauksaite V., Akusjarvi G., Blair G.E.,
RA Matthews D.A.;
RT "Precursor of human adenovirus core polypeptide Mu targets the nucleolus
RT and modulates the expression of E2 proteins.";
RL J. Gen. Virol. 85:185-196(2004).
RN [7]
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 [8]
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: [Pre-core protein X]: Interacts with the viral DNA and aids
CC in tightly condensing it within the capsid. Cleavage of pre-core
CC protein X may serve to partially relax this structure within the mature
CC virion prior to its entry into the nucleus.
CC -!- SUBUNIT: Interacts with the core-capsid bridging protein; this
CC interaction bridges the virus core to the capsid.
CC {ECO:0000269|PubMed:4020954}.
CC -!- SUBCELLULAR LOCATION: [Pre-core protein X]: Host nucleus, host
CC nucleolus. Note=Excluded from adenovirus DNA-binding protein (DBP)-rich
CC replication centers in adenovirus-infected cells.
CC -!- SUBCELLULAR LOCATION: [Core protein X]: Virion. Note=Located inside the
CC capsid in association with the viral DNA (core). Present in about 126-
CC 160 copies per virion. Excluded from adenovirus DNA-binding protein
CC (DBP)-rich replication centers in adenovirus-infected cells.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- PTM: Cleaved by the viral protease during virion maturation to form the
CC mature protein.
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.
CC -!- SIMILARITY: Belongs to the adenoviridae core protein X family.
CC {ECO:0000305}.
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DR EMBL; J01917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D03837; WMADH2.
DR RefSeq; AP_000173.1; AC_000007.1.
DR Proteomes; UP000008167; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR008393; Adenovirus_late_L2_mu_core.
DR Pfam; PF05829; Adeno_PX; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Host nucleus; Late protein;
KW Reference proteome; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:3357209"
FT CHAIN 2..80
FT /note="Pre-core protein X"
FT /id="PRO_0000421077"
FT PROPEP 2..32
FT /id="PRO_0000036519"
FT PEPTIDE 33..51
FT /note="Core protein X"
FT /id="PRO_0000036520"
FT PROPEP 52..80
FT /id="PRO_0000036521"
FT REGION 18..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 32..33
FT /note="Cleavage; by viral protease"
FT SITE 51..52
FT /note="Cleavage; by viral protease"
SQ SEQUENCE 80 AA; 8846 MW; 83555D1C6CD0D324 CRC64;
MALTCRLRFP VPGFRGRMHR RRGMAGHGLT GGMRRAHHRR RRASHRRMRG GILPLLIPLI
AAAIGAVPGI ASVALQAQRH
