TERM_ADE02
ID TERM_ADE02 Reviewed; 671 AA.
AC P03269;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 3.
DT 25-MAY-2022, entry version 83.
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 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 PROTEIN SEQUENCE, AND COVALENT DNA LINKAGE AT SER-580.
RX PubMed=7142163; DOI=10.1016/s0021-9258(18)33475-6;
RA Smart J.E., Stillman B.W.;
RT "Adenovirus terminal protein precursor. Partial amino acid sequence and the
RT site of covalent linkage to virus DNA.";
RL J. Biol. Chem. 257:13499-13506(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7142161; DOI=10.1016/s0021-9258(18)33473-2;
RA Gingeras T.R., Sciaky D., Gelinas R.E., Bing-Dong J., Yen C.E., Kelly M.M.,
RA Bullock P.A., Parsons B.L., O'Neill K.E., Roberts R.J.;
RT "Nucleotide sequences from the adenovirus-2 genome.";
RL J. Biol. Chem. 257:13475-13491(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7142162; DOI=10.1016/s0021-9258(18)33474-4;
RA Alestroem P., Akusjaervi G., Pettersson M., Pettersson U.;
RT "DNA sequence analysis of the region encoding the terminal protein and the
RT hypothetical N-gene product of adenovirus type 2.";
RL J. Biol. Chem. 257:13492-13498(1982).
RN [4]
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=3203379; DOI=10.1016/0092-8674(88)90245-0;
RA Zhao L.J., Padmanabhan R.;
RT "Nuclear transport of adenovirus DNA polymerase is facilitated by
RT interaction with preterminal protein.";
RL Cell 55:1005-1015(1988).
RN [5]
RP MUTAGENESIS OF CYS-8 AND SER-580.
RX PubMed=2511338; DOI=10.1128/jvi.63.12.5244-5250.1989;
RA Pettit S.C., Horwitz M.S., Engler J.A.;
RT "Mutations of the precursor to the terminal protein of adenovirus serotypes
RT 2 and 5.";
RL J. Virol. 63:5244-5250(1989).
RN [6]
RP FUNCTION.
RX PubMed=1291241; DOI=10.1007/bf02451784;
RA Pronk R., Stuiver M.H., van der Vliet P.C.;
RT "Adenovirus DNA replication: the function of the covalently bound terminal
RT protein.";
RL Chromosoma 102:S39-S45(1992).
RN [7]
RP INTERACTION WITH THE POLYMERASE.
RX PubMed=8985382; DOI=10.1128/jvi.71.1.539-547.1997;
RA Webster A., Leith I.R., Hay R.T.;
RT "Domain organization of the adenovirus preterminal protein.";
RL J. Virol. 71:539-547(1997).
RN [8]
RP PROTEOLYTIC CLEAVAGE BY VIRAL PROTEASE.
RX PubMed=9261355; DOI=10.1128/jvi.71.9.6381-6389.1997;
RA Webster A., Leith I.R., Nicholson J., Hounsell J., Hay R.T.;
RT "Role of preterminal protein processing in adenovirus replication.";
RL J. Virol. 71:6381-6389(1997).
RN [9]
RP NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF 384-ARG-ARG-385;
RP 386-ARG-ARG-387; 437-GLU-GLU-438 AND TYR-492.
RX PubMed=11457998; DOI=10.1099/0022-1317-82-8-1917;
RA Botting C.H., Hay R.T.;
RT "Role of conserved residues in the activity of adenovirus preterminal
RT protein.";
RL J. Gen. Virol. 82:1917-1927(2001).
RN [10]
RP DNA-BINDING.
RX PubMed=12799455; DOI=10.1093/nar/gkg405;
RA de Jong R.N., Meijer L.A., van der Vliet P.C.;
RT "DNA binding properties of the adenovirus DNA replication priming protein
RT pTP.";
RL Nucleic Acids Res. 31:3274-3286(2003).
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:1291241}.
CC -!- SUBUNIT: Heterodimer with the polymerase (PubMed:8985382); this
CC heterodimer binds to bp 9 to 18 of the genome. Interacts with host
CC POU2F1; POU2F1 binds to the auxiliary sequences in the inverted
CC terminal repeats and tethers the pTP-POL heterodimer to the origin DNA
CC thereby participating in the assembly of the pre-initiation complex
CC (POL-TP-DBP-NFIA-POU2F1). {ECO:0000255|HAMAP-Rule:MF_04061,
CC ECO:0000269|PubMed:8985382}.
CC -!- SUBCELLULAR LOCATION: Host nucleus matrix {ECO:0000255|HAMAP-
CC Rule:MF_04061}.
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 ECO:0000269|PubMed:9261355}.
CC -!- SIMILARITY: Belongs to the adenoviridae terminal protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04061, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA92208.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J01917; AAA92208.1; ALT_INIT; Genomic_DNA.
DR PIR; A92353; UZADP2.
DR RefSeq; AP_000167.1; AC_000007.1.
DR RefSeq; NP_040518.2; NC_001405.1.
DR GeneID; 2652985; -.
DR Proteomes; UP000008167; Genome.
DR GO; GO:0044204; C:host cell nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; Direct protein sequencing; DNA replication;
KW DNA-binding; Host nucleus; Phosphoprotein; Reference proteome;
KW Viral DNA replication.
FT CHAIN 1..671
FT /note="Preterminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000221893"
FT CHAIN 176..671
FT /note="Intermediate terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000421691"
FT CHAIN 350..671
FT /note="Terminal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04061"
FT /id="PRO_0000421692"
FT REGION 386..409
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 ECO:0000269|PubMed:3203379"
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:7142163"
FT MUTAGEN 8
FT /note="C->S: Almost no effect on pTP activity."
FT /evidence="ECO:0000269|PubMed:2511338"
FT MUTAGEN 384..385
FT /note="RR->AA: Complete loss of DNA replication initiation
FT and DNA binding."
FT /evidence="ECO:0000269|PubMed:11457998"
FT MUTAGEN 386..387
FT /note="RR->AA: Complete loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:11457998"
FT MUTAGEN 437..438
FT /note="EE->AA: Complete loss of DNA replication
FT initiation."
FT /evidence="ECO:0000269|PubMed:11457998"
FT MUTAGEN 492
FT /note="Y->A: Complete loss of DNA replication initiation."
FT /evidence="ECO:0000269|PubMed:11457998"
FT MUTAGEN 580
FT /note="S->T: Complete loss of initiation and elongation."
FT /evidence="ECO:0000269|PubMed:2511338"
SQ SEQUENCE 671 AA; 76543 MW; 0B66AF54FEA7AF92 CRC64;
MALSVNDCAR LTGQSVPTME HFLPLRNIWN RVRDFPRAST TAAGITWMSR YIYGYHRLML
EDLAPGAPAT LRWPLYRQPP PHFLVGYQYL VRTCNDYVFD SRAYSRLRYT ELSQPGHQTV
NWSVMANCTY TINTGAYHRF VDMDDFQSTL TQVQQAILAE RVVADLALLQ PMRGFGVTRM
GGRGRHLRPN SAAAVAIDAR DAGQEEGEEE VPVERLMQDY YKDLRRCQNE AWGMADRLRI
QQAGPKDMVL LSTIRRLKTA YFNYIISSTS ARNNPDRHPL PPATVLSLPC DCDWLDAFLE
RFSDPVDADS LRSLGGGVPT QQLLRCIVSA VSLPHGSPPP THNRDMTGGV FQLRPRENGR
AVTETMRRRR GEMIERFVDR LPVRRRRRRV PPPPPPPEEE EEGEALMEEE IEEEEAPVAF
EREVRDTVAE LIRLLEEELT VSARNSQFFN FAVDFYEAME RLEALGDINE STLRRWVMYF
FVAEHTATTL NYLFQRLRNY AVFARHVELN LAQVVMRARD AEGGVVYSRV WNEGGLNAFS
QLMARISNDL AATVERAGRG DLQEEEIEQF MAEIAYQDNS GDVQEILRQA AVNDTEIDSV
ELSFRFKLTG PVVFTQRRQI QEINRRVVAF ASNLRAQHQL LPARGADVPL PPLPAGPEPP
LPPGARPRHR F
