E1A_ADEM1
ID E1A_ADEM1 Reviewed; 200 AA.
AC P12534;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 23-FEB-2022, entry version 64.
DE RecName: Full=Early E1A 21 kDa protein;
OS Murine adenovirus A serotype 1 (MAdV-1) (Murine adenovirus 1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Murine mastadenovirus A.
OX NCBI_TaxID=10530;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3172335; DOI=10.1128/jvi.62.11.3947-3957.1988;
RA Ball A.O., Williams M.E., Spindler K.R.;
RT "Identification of mouse adenovirus type 1 early region 1: DNA sequence and
RT a conserved transactivating function.";
RL J. Virol. 62:3947-3957(1988).
CC -!- FUNCTION: E1A protein has both transforming and trans-activating
CC activities. Plays a role in viral genome replication by driving entry
CC of quiescent cells into the cell cycle. Disrupts the function of host
CC retinoblastoma protein RB1/pRb and isoform early E1A 26 kDa protein
CC stabilizes TP53, which are key regulators of the cell cycle. Induces
CC the disassembly of the E2F1 transcription factors from RB1 by direct
CC competition for the same binding site on RB1, with subsequent
CC transcriptional activation of E2F1-regulated S-phase genes.
CC Inactivation of the ability of RB1 to arrest the cell cycle is critical
CC for cellular transformation, uncontrolled cellular growth and
CC proliferation induced by viral infection. Stimulation of progression
CC from G1 to S phase allows the virus to efficiently use the cellular DNA
CC replicating machinery to achieve viral genome replication (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interaction with host RB1 induces the aberrant dissociation of
CC RB1-E2F1 complex thereby disrupting RB1's activity. {ECO:0000250}.
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DR EMBL; M22245; AAA42424.1; -; Genomic_DNA.
DR RefSeq; NP_015532.1; NC_000942.1.
DR IntAct; P12534; 2.
DR GeneID; 1732772; -.
DR KEGG; vg:1732772; -.
DR Proteomes; UP000243112; Genome.
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: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.
PE 3: Inferred from homology;
KW Activator; Early protein;
KW G1/S host cell cycle checkpoint dysregulation by virus;
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; Transcription;
KW Transcription regulation; Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..200
FT /note="Early E1A 21 kDa protein"
FT /id="PRO_0000221704"
FT ZN_FING 136..151
FT /evidence="ECO:0000255"
FT REGION 78..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..118
FT /note="LXCXE motif, interaction with host RB1"
FT /evidence="ECO:0000255"
FT MOTIF 196..200
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 200 AA; 21878 MW; 5B63D6E6272639E5 CRC64;
MSRLLRLSLS SRVWLAAQEA TRNVSEDPVV CRTPWDGSPT CTAVRVVRAE VLADGTMDLD
IVFPEAAVQA VFSRTPWQDS TTATSAEEPS ASTDSISSDP LPISCVESFE DMDLRCYEQL
SPSPESIETI EVFPPCSTCG GHEVNGFCSL CYLRGLTDLL PQADDAGEAE VPDESAKDLC
FMDLLTWAME DKTECSRHDE