位置:首页 > 蛋白库 > PKG3_ADE05
PKG3_ADE05
ID   PKG3_ADE05              Reviewed;         415 AA.
AC   P04496;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 2.
DT   23-FEB-2022, entry version 77.
DE   RecName: Full=Packaging protein 3 {ECO:0000255|HAMAP-Rule:MF_04058};
DE   AltName: Full=L1-52/55 kDa protein {ECO:0000255|HAMAP-Rule:MF_04058};
DE   AltName: Full=Packaging protein 52K {ECO:0000255|HAMAP-Rule:MF_04058};
GN   Name=L1 {ECO:0000255|HAMAP-Rule:MF_04058};
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-173.
RX   PubMed=6325298; DOI=10.1016/0378-1119(84)90244-0;
RA   Dekker B.M.M., van Ormondt H.;
RT   "The nucleotide sequence of fragment HindIII-C of human adenovirus type 5
RT   DNA (map positions 17.1-31.7).";
RL   Gene 27:115-120(1984).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH PACKAGING PROTEIN 1.
RX   PubMed=15681437; DOI=10.1128/jvi.79.4.2366-2374.2005;
RA   Perez-Romero P., Tyler R.E., Abend J.R., Dus M., Imperiale M.J.;
RT   "Analysis of the interaction of the adenovirus L1 52/55-kilodalton and IVa2
RT   proteins with the packaging sequence in vivo and in vitro.";
RL   J. Virol. 79:2366-2374(2005).
RN   [5]
RP   INTERACTION WITH HEXON-LINKING PROTEIN IIIA PROTEIN.
RX   PubMed=21632753; DOI=10.1128/jvi.00467-11;
RA   Ma H.C., Hearing P.;
RT   "Adenovirus structural protein IIIa is involved in the serotype specificity
RT   of viral DNA packaging.";
RL   J. Virol. 85:7849-7855(2011).
RN   [6]
RP   IDENTIFICATION IN THE GENOME PACKAGING COMPLEX.
RX   PubMed=22811519; DOI=10.1128/jvi.01463-12;
RA   Wu K., Orozco D., Hearing P.;
RT   "The adenovirus L4-22K Protein is multifunctional and is an integral
RT   component of crucial aspects of infection.";
RL   J. Virol. 86:10474-10483(2012).
CC   -!- FUNCTION: Involved in viral genome packaging through its interaction
CC       with packaging proteins 1 and 2. After proteolytic cleavage by
CC       adenovirus protease, L1 52/55k protein is removed from the capsid
CC       during viral maturation. {ECO:0000255|HAMAP-Rule:MF_04058,
CC       ECO:0000269|PubMed:15681437}.
CC   -!- SUBUNIT: Part of the genome packaging complex composed of packaging
CC       proteins 1, 2 and 3; this complex specifically binds to the packaging
CC       sequence on the left end of viral genomic DNA and performs packaging of
CC       the viral genome (PubMed:22811519). Interacts with hexon-linking
CC       protein IIIa; this interaction is required to promote correct genome
CC       packaging (PubMed:21632753). {ECO:0000255|HAMAP-Rule:MF_04058,
CC       ECO:0000269|PubMed:15681437, ECO:0000269|PubMed:21632753,
CC       ECO:0000269|PubMed:22811519}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04058}.
CC       Note=Nuclear protein present in empty capsids and assembly
CC       intermediates. {ECO:0000255|HAMAP-Rule:MF_04058}.
CC   -!- INDUCTION: Expressed in the early phase and late phase of the viral
CC       replicative cycle. {ECO:0000255|HAMAP-Rule:MF_04058}.
CC   -!- PTM: Cleaved at different sites by the viral protease during virion
CC       maturation. {ECO:0000255|HAMAP-Rule:MF_04058}.
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_04058}.
CC   -!- SIMILARITY: Belongs to the adenoviridae packaging protein 3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04058}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M73260; AAA96406.1; -; Genomic_DNA.
DR   EMBL; X02996; CAA26751.1; -; Genomic_DNA.
DR   PIR; G39449; WMAD65.
DR   RefSeq; AP_000204.1; AC_000008.1.
DR   Proteomes; UP000004992; Genome.
DR   GO; GO:0044815; C:DNA packaging complex; IDA:UniProtKB.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04058; ADV_PKG3; 1.
DR   InterPro; IPR037536; ADV_PKG3.
DR   InterPro; IPR004292; L1-like.
DR   Pfam; PF03052; Adeno_52K; 1.
PE   1: Evidence at protein level;
KW   Host nucleus; Late protein; Phosphoprotein; Viral genome packaging;
KW   Viral release from host cell.
FT   CHAIN           1..415
FT                   /note="Packaging protein 3"
FT                   /id="PRO_0000221866"
FT   REGION          1..173
FT                   /note="Interaction with packaging protein 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04058"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..415
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            351..352
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04058"
FT   MOD_RES         75
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04058"
FT   MOD_RES         360
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04058"
FT   CONFLICT        79
FT                   /note="Y -> H (in Ref. 2; no nucleotide entry)"
SQ   SEQUENCE   415 AA;  47060 MW;  DA51B34066BA0129 CRC64;
     MHPVLRQMRP PPQQRQEQEQ RQTCRAPSPP PTASGGATSA VDAAADGDYE PPRRRARHYL
     DLEEGEGLAR LGAPSPERYP RVQLKRDTRE AYVPRQNLFR DREGEEPEEM RDRKFHAGRE
     LRHGLNRERL LREEDFEPDA RTGISPARAH VAAADLVTAY EQTVNQEINF QKSFNNHVRT
     LVAREEVAIG LMHLWDFVSA LEQNPNSKPL MAQLFLIVQH SRDNEAFRDA LLNIVEPEGR
     WLLDLINILQ SIVVQERSLS LADKVAAINY SMLSLGKFYA RKIYHTPYVP IDKEVKIEGF
     YMRMALKVLT LSDDLGVYRN ERIHKAVSVS RRRELSDREL MHSLQRALAG TGSGDREAES
     YFDAGADLRW APSRRALEAA GAGPGLAVAP ARAGNVGGVE EYDEDDEYEP EDGEY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024