TERM_ADE05
ID TERM_ADE05 Reviewed; 671 AA.
AC P04499;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Preterminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
DE Short=pTP {ECO:0000255|HAMAP-Rule:MF_04061};
DE AltName: Full=Bellett protein {ECO:0000255|HAMAP-Rule:MF_04061};
DE AltName: Full=Precursor terminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
DE Contains:
DE RecName: Full=Intermediate terminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
DE Short=iTP {ECO:0000255|HAMAP-Rule:MF_04061};
DE Contains:
DE RecName: Full=Terminal protein {ECO:0000255|HAMAP-Rule:MF_04061};
DE Short=TP {ECO:0000255|HAMAP-Rule:MF_04061};
GN Name=PTP {ECO:0000255|HAMAP-Rule:MF_04061};
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE 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 [3]
RP COVALENT DNA LINKAGE AT SER-580.
RX PubMed=7265205; DOI=10.1016/0022-2836(81)90208-4;
RA Desiderio S.V., Kelly T.J. Jr.;
RT "Structure of the linkage between adenovirus DNA and the 55,000 molecular
RT weight terminal protein.";
RL J. Mol. Biol. 145:319-337(1981).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8497057; DOI=10.1128/jvi.67.6.3384-3395.1993;
RA Fredman J.N., Engler J.A.;
RT "Adenovirus precursor to terminal protein interacts with the nuclear matrix
RT in vivo and in vitro.";
RL J. Virol. 67:3384-3395(1993).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8416372; DOI=10.1128/jvi.67.1.265-276.1993;
RA Roovers D.J., van der Lee F.M., van der Wees J., Sussenbach J.S.;
RT "Analysis of the adenovirus type 5 terminal protein precursor and DNA
RT polymerase by linker insertion mutagenesis.";
RL J. Virol. 67:265-276(1993).
RN [6]
RP INTERACTION WITH HOST POU2F1.
RX PubMed=9013582; DOI=10.1074/jbc.272.6.3398;
RA van Leeuwen H.C., Rensen M., van der Vliet P.C.;
RT "The Oct-1 POU homeodomain stabilizes the adenovirus preinitiation complex
RT via a direct interaction with the priming protein and is displaced when the
RT replication fork passes.";
RL J. Biol. Chem. 272:3398-3405(1997).
RN [7]
RP INTERACTION WITH HOST POU2F1.
RX PubMed=10373599; DOI=10.1093/nar/27.13.2799;
RA Botting C.H., Hay R.T.;
RT "Characterisation of the adenovirus preterminal protein and its interaction
RT with the POU homeodomain of NFIII (Oct-1).";
RL Nucleic Acids Res. 27:2799-2805(1999).
RN [8]
RP FUNCTION, AND INTERACTION WITH HOST POU2F1.
RX PubMed=11847120; DOI=10.1093/emboj/21.4.725;
RA de Jong R.N., Mysiak M.E., Meijer L.A., van der Linden M.,
RA van der Vliet P.C.;
RT "Recruitment of the priming protein pTP and DNA binding occur by
RT overlapping Oct-1 POU homeodomain surfaces.";
RL EMBO J. 21:725-735(2002).
RN [9]
RP INTERACTION WITH THE POLYMERASE.
RX PubMed=12134025; DOI=10.1128/jvi.76.16.8200-8207.2002;
RA Brenkman A.B., Breure E.C., van der Vliet P.C.;
RT "Molecular architecture of adenovirus DNA polymerase and location of the
RT protein primer.";
RL J. Virol. 76:8200-8207(2002).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN THE INITIATION COMPLEX.
RX PubMed=12747549; DOI=10.1007/978-3-662-05597-7_5;
RA Liu H., Naismith J.H., Hay R.T.;
RT "Adenovirus DNA replication.";
RL Curr. Top. Microbiol. Immunol. 272:131-164(2003).
RN [11]
RP FUNCTION, INTERACTION WITH THE POLYMERASE, AND MUTAGENESIS OF ASP-578 AND
RP ASP-582.
RX PubMed=15273278; DOI=10.1093/nar/gkh726;
RA Mysiak M.E., Holthuizen P.E., van der Vliet P.C.;
RT "The adenovirus priming protein pTP contributes to the kinetics of
RT initiation of DNA replication.";
RL Nucleic Acids Res. 32:3913-3920(2004).
CC -!- FUNCTION: Protein covalently bound to the viral DNA that acts as a
CC primer for viral genomic replication by DNA strand displacement.
CC Assembles on the viral origin of replication in an initiation complex
CC with viral polymerase, DBP, host NFIA and host POU2F1/OCT1. During
CC initiation, the polymerase covalently couples the first dCTP with Ser-
CC 580 of pTP. The terminal protein stimulates the template activity over
CC 20 fold compared to protein-free templates. Neo-synthesized viral
CC genomes are linked to two preterminal proteins, one for each 5' end.
CC These new genomes are encapsidated in the nucleus, and during capsid
CC maturation by viral protease, preterminal protein is first cleaved into
CC intermediary (iTP), then into mature TP. May play a role in host
CC nuclear matrix localization of genomic DNA. {ECO:0000255|HAMAP-
CC Rule:MF_04061, ECO:0000269|PubMed:11847120,
CC ECO:0000269|PubMed:12747549, ECO:0000269|PubMed:15273278,
CC ECO:0000269|PubMed:8416372, ECO:0000269|PubMed:8497057}.
CC -!- SUBUNIT: Heterodimer with the polymerase; this heterodimer binds to bp
CC 9 to 18 of the genome (PubMed:12134025, PubMed:15273278). Interacts
CC with host POU2F1; POU2F1 binds to the auxiliary sequences in the
CC inverted terminal repeats and tethers the pTP-POL heterodimer to the
CC origin DNA thereby participating in the assembly of the pre-initiation
CC complex (POL-TP-DBP-NFIA-POU2F1) (PubMed:9013582, PubMed:10373599,
CC PubMed:11847120, PubMed:12747549). {ECO:0000255|HAMAP-Rule:MF_04061,
CC ECO:0000269|PubMed:10373599, ECO:0000269|PubMed:11847120,
CC ECO:0000269|PubMed:12134025, ECO:0000269|PubMed:15273278,
CC ECO:0000269|PubMed:9013582, ECO:0000305|PubMed:12747549}.
CC -!- SUBCELLULAR LOCATION: Host nucleus matrix {ECO:0000255|HAMAP-
CC Rule:MF_04061, ECO:0000269|PubMed:8416372, ECO:0000269|PubMed:8497057}.
CC -!- PTM: Preterminal protein is used to replicate viral genome, upon
CC genomic encapsidation it is processed first into iTP and finally into
CC TP by adenovirus protease. {ECO:0000255|HAMAP-Rule:MF_04061}.
CC -!- SIMILARITY: Belongs to the adenoviridae terminal protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04061, ECO:0000305}.
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DR EMBL; X02996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A03840; UZADP5.
DR RefSeq; AP_000203.1; AC_000008.1.
DR DIP; DIP-44807N; -.
DR IntAct; P04499; 1.
DR PRIDE; P04499; -.
DR Proteomes; UP000004992; Genome.
DR GO; GO:0044204; C:host cell nuclear matrix; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
DR GO; GO:0039687; P:viral DNA strand displacement replication; IDA:UniProtKB.
DR HAMAP; MF_04061; ADV_TERM; 1.
DR InterPro; IPR003391; Adeno_preterminal.
DR Pfam; PF02459; Adeno_terminal; 1.
PE 1: Evidence at protein level;
KW Covalent protein-DNA linkage; DNA replication; DNA-binding; Host nucleus;
KW Phosphoprotein; Viral DNA replication.
FT CHAIN 1..671
FT /note="Preterminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000221894"
FT CHAIN 176..671
FT /note="Intermediate terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000433932"
FT CHAIN 350..671
FT /note="Terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000433933"
FT REGION 386..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 380..389
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT COMPBIAS 647..664
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 175..176
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 349..350
FT /note="Cleavage; by adenovirus protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT SITE 580
FT /note="Priming of strand displacement replication by
FT covalently linking the first nucleotide of the new DNA
FT chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT MOD_RES 580
FT /note="O-(5'-phospho-DNA)-serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061,
FT ECO:0000269|PubMed:7265205"
FT MUTAGEN 578
FT /note="D->E: No effect on pTP initiation activity. No
FT effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:15273278"
FT MUTAGEN 578
FT /note="D->N: Decreased pTP initiation activity to 29% of
FT wild-type activity. No effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:15273278"
FT MUTAGEN 578
FT /note="D->R: Decreased pTP initiation activity to 7% of
FT wild-type activity. No effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:15273278"
FT MUTAGEN 582
FT /note="D->E,N,R: Decreased pTP initiation activity to 65%
FT of wild-type activity. No effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:15273278"
FT MUTAGEN 582
FT /note="D->N: Decreased pTP initiation activity to 85% of
FT wild-type activity. No effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:15273278"
FT MUTAGEN 582
FT /note="D->R: Complete loss of pTP initiation activity. No
FT effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:15273278"
SQ SEQUENCE 671 AA; 76500 MW; 075A579546FA3F91 CRC64;
MALSVNDCAR LTGQSVPTME HFLPLRNIWN RVRDFPRAST TAAGITWMSR YIYGYHRLML
EDLAPGAPAT LRWPLYRQPP PHFLVGYQYL VRTCNDYVFD SRAYSRLRYT ELSQPGHQTV
NWSVMANCTY TINTGAYHRF VDMDDFQSTL TQVQQAILAE RVVADLALLQ PMRGFGVTRM
GGRGRHLRPN SAAAAAIDAR DAGQEEGEEE VPVERLMQDY YKDLRRCQNE AWGMADRLRI
QQAGPKDMVL LSTIRRLKTA YFNYIISSTS ARNNPDRRPL PPATVLSLPC DCDWLDAFLE
RFSDPVDADS LRSLGGGVPT QQLLRCIVSA VSLPHGSPPP THNRDMTGGV FQLRPRENGR
AVTETMRRRR GEMIERFVDR LPVRRRRRRV PPPPPPPEEE EGEALMEEEI EEEEEAPVAF
EREVRDTVAE LIRLLEEELT VSARNSQFFN FAVDFYEAME RLEALGDINE STLRRWVMYF
FVAEHTATTL NYLFQRLRNY AVFARHVELN LAQVVMRARD AEGGVVYSRV WNEGGLNAFS
QLMARISNDL AATVERAGRG DLQEEEIEQF MAEIAYQDNS GDVQEILRQA AVNDTEIDSV
ELSFRLKLTG PVVFTQRRQI QEINRRVVAF ASNLRAQHQL LPARGADVPL PPLPAGPEPP
LPPGARPRHR F
