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E1A_ADE41
ID   E1A_ADE41               Reviewed;         251 AA.
AC   P10542;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   23-FEB-2022, entry version 81.
DE   RecName: Full=Early E1A protein;
DE   AltName: Full=Early E1A 27 kDa protein;
OS   Human adenovirus F serotype 41 (HAdV-41) (Human adenovirus 41).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX   NCBI_TaxID=10524;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2961652; DOI=10.1016/0378-1119(87)90034-5;
RA   van Loon A.E., Ligtenberg M., Reemst A.M.C.B., Sussenbach J.S.,
RA   Rozijn T.H.;
RT   "Structure and organization of the left-terminal DNA regions of fastidious
RT   adenovirus types 40 and 41.";
RL   Gene 58:109-126(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2834871; DOI=10.1016/0042-6822(88)90639-3;
RA   Allard A., Wadell G.;
RT   "Physical organization of the enteric adenovirus type 41 early region 1A.";
RL   Virology 164:220-229(1988).
CC   -!- FUNCTION: Plays a role in viral genome replication by driving entry of
CC       quiescent cells into the cell cycle. Stimulation of progression from G1
CC       to S phase allows the virus to efficiently use the cellular DNA
CC       replicating machinery to achieve viral genome replication. E1A protein
CC       has both transforming and trans-activating activities. Induces the
CC       disassembly of the E2F1 transcription factor from RB1 by direct
CC       competition for the same binding site on RB1, with subsequent
CC       transcriptional activation of E2F1-regulated S-phase genes and of the
CC       E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-
CC       mediated inhibition of MDM2 and causes TP53/p53 to accumulate because
CC       it is not targeted for degradation by MDM2-mediated ubiquitination
CC       anymore. This increase in TP53, in turn, would arrest the cell
CC       proliferation and direct its death but this effect is counteracted by
CC       the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest
CC       the cell cycle is critical for cellular transformation, uncontrolled
CC       cellular growth and proliferation induced by viral infection.
CC       Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins
CC       targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to
CC       unregulated host cell proliferation. The tumorigenesis-restraining
CC       activity of E1A may be related to the disruption of the host CtBP-CtIP
CC       complex through the CtBP binding motif. Interaction with host
CC       TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic
CC       DNA and promote the production of type I interferon (IFN-alpha and IFN-
CC       beta). Promotes the sumoylation of host ZBED1/hDREF with SUMO1 (By
CC       similarity). {ECO:0000250|UniProtKB:P03255}.
CC   -!- SUBUNIT: Interacts with host UBE2I; this interaction interferes with
CC       polySUMOylation. Interacts with host RB1; this interaction induces the
CC       aberrant dissociation of RB1-E2F1 complex thereby disrupting the
CC       activity of RB1 and activating E2F1-regulated genes. Interacts with
CC       host ATF7; the interaction enhances ATF7-mediated viral transactivation
CC       activity which requires the zinc binding domains of both proteins.
CC       Isoform early E1A 32 kDa protein and isoform early E1A 26 kDa protein
CC       interact (via N-terminus) with CUL1 and E3 ubiquitin ligase RBX1; these
CC       interactions inhibit RBX1-CUL1-dependent elongation reaction of
CC       ubiquitin chains and attenuate ubiquitination of SCF(FBXW7) target
CC       proteins. Interacts (via PXLXP motif) with host ZMYND11/BS69 (via MYND-
CC       type zinc finger); this interaction inhibits E1A mediated
CC       transactivation. Interacts with host EP300; this interaction stimulates
CC       the acetylation of RB1 by recruiting EP300 and RB1 into a multimeric-
CC       protein complex. Interacts with host CTBP1 and CTBP2; this interaction
CC       seems to potentiate viral replication. Interacts with host DCAF7.
CC       Interacts with host DYRK1A. Interacts with host KPNA4; this interaction
CC       allows E1A import into the host nucleus. Interacts with host EP400;
CC       this interaction stabilizes MYC. Interacts with host TBP protein; this
CC       interaction probably disrupts the TBP-TATA complex. Interacts (via
CC       LXCXE motif) with host TMEM173/STING; this interaction impairs the
CC       ability of TMEM173/STING to sense cytosolic DNA and promote the
CC       production of type I interferon (IFN-alpha and IFN-beta). Interacts
CC       (via C-terminus) with host ZBED1/hDREF (via C-terminus); the
CC       interaction is direct (By similarity). {ECO:0000250|UniProtKB:P03254,
CC       ECO:0000250|UniProtKB:P03255}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Isoforms are derived from the E1 region of the genome.;
CC       Name=1; Synonyms=Early E1A 27 kDa protein;
CC         IsoId=P10542-1; Sequence=Displayed;
CC       Name=2; Synonyms=Early E1A 25 kDa protein;
CC         IsoId=P10542-2; Sequence=VSP_000206;
CC   -!- SIMILARITY: Belongs to the adenoviridae E1A protein family.
CC       {ECO:0000305}.
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DR   EMBL; M18289; AAA42450.1; -; mRNA.
DR   EMBL; M20300; AAA42439.1; -; Genomic_DNA.
DR   EMBL; M20300; AAA42440.1; -; Genomic_DNA.
DR   PIR; D27333; WMADF4.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR   GO; GO:0039649; P:modulation by virus of host ubiquitin-protein ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR014410; Aden_E1A.
DR   Pfam; PF02703; Adeno_E1A; 1.
DR   PIRSF; PIRSF003669; Aden_E1A; 1.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; Early protein;
KW   G1/S host cell cycle checkpoint dysregulation by virus; Host nucleus;
KW   Host-virus interaction; Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host STAT1 by virus; Metal-binding;
KW   Modulation of host cell cycle by virus;
KW   Modulation of host E3 ubiquitin ligases by virus;
KW   Modulation of host ubiquitin pathway by virus; Oncogene; Transcription;
KW   Transcription regulation; Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN           1..251
FT                   /note="Early E1A protein"
FT                   /id="PRO_0000221698"
FT   ZN_FING         150..170
FT                   /evidence="ECO:0000250|UniProtKB:P03254"
FT   REGION          38..46
FT                   /note="Interaction with RB1 in competition with E2F1"
FT                   /evidence="ECO:0000250"
FT   REGION          74..136
FT                   /note="Interaction with UBE2I"
FT                   /evidence="ECO:0000250"
FT   REGION          102..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           97..101
FT                   /note="LXCXE motif, interaction with host RB1 and
FT                   TMEM173/STING"
FT                   /evidence="ECO:0000255"
FT   MOTIF           240..244
FT                   /note="PXDLS motif, CTBP-binding"
FT                   /evidence="ECO:0000250"
FT   MOTIF           246..250
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         154..181
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000206"
SQ   SEQUENCE   251 AA;  27476 MW;  BA48F87487EECE0B CRC64;
     MRMLPDFFTG NWDDMFQGLL EAEHPFDFPE PSQAFEEISL HNLFDVELDE SEGDPNEEAV
     DGMFPNWMLS EDHSADSGAA SGDSGVGEDL VEVNLDLKCY EEGLPPSGSE ADEAEERAEE
     EETAVSNYVN IAEGASQLVL DCPENPGRGC RACDFHRGSS GNPEAMCALC YMRLTGHCIY
     SPISDAEGEC ELGSNEETEL PCSLTATAPV RPTPCRVSCR RRPAVDCIED LLEEDPTDEP
     LNLSLKRPKS S
 
 
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