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COR10_ADE05
ID   COR10_ADE05             Reviewed;          80 AA.
AC   Q2KS10;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 35.
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 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].
RC   STRAIN=Isolate NHRC Ad5FS 7151;
RX   PubMed=16481660; DOI=10.1101/gr.4337206;
RA   Lin B., Wang Z., Vora G.J., Thornton J.A., Schnur J.M., Thach D.C.,
RA   Blaney K.M., Ligler A.G., Malanoski A.P., Santiago J., Walter E.A.,
RA   Agan B.K., Metzgar D., Seto D., Daum L.T., Kruzelock R., Rowley R.K.,
RA   Hanson E.H., Tibbetts C., Stenger D.A.;
RT   "Broad-spectrum respiratory tract pathogen identification using
RT   resequencing DNA microarrays.";
RL   Genome Res. 16:527-535(2006).
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   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).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the core-capsid bridging protein; this
CC       interaction bridges the virus core to the capsid. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Pre-core protein X]: Host nucleus, host
CC       nucleolus {ECO:0000250}. Note=Excluded from adenovirus DNA-binding
CC       protein (DBP)-rich 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 (By
CC       similarity). {ECO:0000250}.
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. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenoviridae core protein X family.
CC       {ECO:0000305}.
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DR   EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY601635; AAW65512.1; -; Genomic_DNA.
DR   RefSeq; AP_000209.1; AC_000008.1.
DR   PRIDE; Q2KS10; -.
DR   Proteomes; UP000004992; Genome.
DR   Proteomes; UP000125273; 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   2: Evidence at transcript level;
KW   DNA-binding; Host nucleus; Late protein; Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..80
FT                   /note="Pre-core protein X"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000421136"
FT   PROPEP          2..32
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000421137"
FT   PEPTIDE         33..51
FT                   /note="Core protein X"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000421138"
FT   PROPEP          52..80
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000421139"
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                   /evidence="ECO:0000250"
FT   SITE            51..52
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   80 AA;  8846 MW;  83555D1C6CD0D324 CRC64;
     MALTCRLRFP VPGFRGRMHR RRGMAGHGLT GGMRRAHHRR RRASHRRMRG GILPLLIPLI
     AAAIGAVPGI ASVALQAQRH
 
 
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