PKG3_ADE02
ID PKG3_ADE02 Reviewed; 415 AA.
AC P03262;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 71.
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 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=6334081; DOI=10.1016/s0021-9258(18)89839-8;
RA Roberts R.J., O'Neill K.E., Yen C.E.;
RT "DNA sequences from the adenovirus 2 genome.";
RL J. Biol. Chem. 259:13968-13975(1984).
RN [2]
RP PROTEIN SEQUENCE OF 71-78 AND 357-369, AND PHOSPHORYLATION AT SER-75 AND
RP SER-360.
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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=1527852; DOI=10.1128/jvi.66.10.6133-6142.1992;
RA Hasson T.B., Ornelles D.A., Shenk T.;
RT "Adenovirus L1 52- and 55-kilodalton proteins are present within assembling
RT virions and colocalize with nuclear structures distinct from replication
RT centers.";
RL J. Virol. 66:6133-6142(1992).
RN [4]
RP FUNCTION, AND INTERACTION WITH PACKAGING PROTEIN 1.
RC STRAIN=Human adenovirus C serotype 5;
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 FUNCTION, AND INTERACTION WITH PACKAGING PROTEIN 1.
RX PubMed=16439552; DOI=10.1128/jvi.80.4.1965-1971.2006;
RA Perez-Romero P., Gustin K.E., Imperiale M.J.;
RT "Dependence of the encapsidation function of the adenovirus L1 52/55-
RT kilodalton protein on its ability to bind the packaging sequence.";
RL J. Virol. 80:1965-1971(2006).
RN [6]
RP FUNCTION.
RX PubMed=18337584; DOI=10.1128/jvi.00040-08;
RA Wohl B.P., Hearing P.;
RT "Role for the L1-52/55K protein in the serotype specificity of adenovirus
RT DNA packaging.";
RL J. Virol. 82:5089-5092(2008).
RN [7]
RP INTERACTION WITH HEXON-LINKING PROTEIN IIIA.
RC STRAIN=Human adenovirus C serotype 5, and Human adenovirus D serotype 17;
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 [8]
RP IDENTIFICATION IN THE GENOME PACKAGING COMPLEX.
RC STRAIN=Human adenovirus C serotype 5;
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).
RN [9]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE BY VIRAL PROTEASE.
RX PubMed=24227847; DOI=10.1128/jvi.02884-13;
RA Perez-Berna A.J., Mangel W.F., McGrath W.J., Graziano V., Flint J.,
RA San Martin C.;
RT "Processing of the l1 52/55k protein by the adenovirus protease: a new
RT substrate and new insights into virion maturation.";
RL J. Virol. 88:1513-1524(2014).
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, ECO:0000269|PubMed:16439552,
CC ECO:0000269|PubMed:18337584, ECO:0000269|PubMed:24227847}.
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:16439552,
CC ECO:0000269|PubMed:21632753, ECO:0000269|PubMed:22811519}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04058,
CC ECO:0000269|PubMed:1527852}. Note=Nuclear protein present in empty
CC capsids and assembly intermediates. {ECO:0000255|HAMAP-Rule:MF_04058,
CC ECO:0000269|PubMed:1527852}.
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 ECO:0000269|PubMed:24227847}.
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}.
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DR EMBL; J01917; AAA92209.1; -; Genomic_DNA.
DR PIR; A03830; WMAD52.
DR RefSeq; AP_000168.1; AC_000007.1.
DR RefSeq; NP_040519.1; NC_001405.1.
DR iPTMnet; P03262; -.
DR GeneID; 2652993; -.
DR Proteomes; UP000008167; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0019073; P:viral DNA genome packaging; IMP:UniProtKB.
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 Direct protein sequencing; Host nucleus; Late protein; Phosphoprotein;
KW Reference proteome; Viral genome packaging; Viral release from host cell.
FT CHAIN 1..415
FT /note="Packaging protein 3"
FT /id="PRO_0000221865"
FT REGION 1..173
FT /note="Interaction with packaging protein 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04058"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..85
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..37
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 ECO:0000269|PubMed:24227847"
FT MOD_RES 75
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04058,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 360
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04058,
FT ECO:0000269|PubMed:22939182"
SQ SEQUENCE 415 AA; 46996 MW; B82843AFB9E7C2CA CRC64;
MHPVLRQMRP PPQQRQEQEQ RQTCRAPSPS PTASGGATSA ADAAADGDYE PPRRRARHYL
DLEEGEGLAR LGAPSPERHP 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
