ID F2WTJ8_9ADEN Unreviewed; 494 AA.
AC F2WTJ8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=E1B 55 kDa protein {ECO:0000256|ARBA:ARBA00022118};
DE AltName: Full=E1B protein, large T-antigen {ECO:0000256|ARBA:ARBA00030428};
DE AltName: Full=E1B-495R {ECO:0000256|ARBA:ARBA00031863};
OS Simian adenovirus 49.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Simian mastadenovirus B.
OX NCBI_TaxID=995022 {ECO:0000313|EMBL:ADZ39832.1, ECO:0000313|Proteomes:UP000112894};
RN [1] {ECO:0000313|EMBL:ADZ39832.1, ECO:0000313|Proteomes:UP000112894}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C24948 {ECO:0000313|EMBL:ADZ39832.1};
RX PubMed=19578438; DOI=10.1371/journal.ppat.1000503;
RA Roy S., Vandenberghe L.H., Kryazhimskiy S., Grant R., Calcedo R., Yuan X.,
RA Keough M., Sandhu A., Wang Q., Medina-Jaszek C.A., Plotkin J.B.,
RA Wilson J.M.;
RT "Isolation and characterization of adenoviruses persistently shed from the
RT gastrointestinal tract of non-human primates.";
RL PLoS Pathog. 5:E1000503-E1000503(2009).
CC -!- FUNCTION: Plays a major role to prevent cellular inhibition of viral
CC genome replication. Assembles an SCF-like E3 ubiquitin ligase complex
CC based on the cellular proteins ELOB, ELOC, CUL5 and RBX1, in
CC cooperation with viral E4orf6. This viral RING-type ligase
CC ubiquitinates cellular substrates and targets them to proteasomal
CC degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3,
CC DAXX and BLM. Degradation of host TP53/p53 activity is essential for
CC preventing E1A-induced TP53 accumulation that would otherwise lead to
CC cell apoptosis and growth arrest. E1B-55K also inactivates TP53
CC transcription-factor activity by binding its transactivation domain.
CC E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the
CC latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies
CC thereby contributing to maximal inhibition of TP53 function.
CC {ECO:0000256|ARBA:ARBA00002808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the adenoviridae E1B 55 kDa protein family.
CC {ECO:0000256|ARBA:ARBA00008605}.
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DR EMBL; HQ241819; ADZ39832.1; -; Genomic_DNA.
DR RefSeq; YP_004300201.1; NC_015225.1.
DR GeneID; 10400103; -.
DR KEGG; vg:10400103; -.
DR OrthoDB; 3297at10239; -.
DR Proteomes; UP000112894; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0039526; P:perturbation by virus of host apoptosis; IEA:UniProtKB-KW.
DR InterPro; IPR006717; Adeno_E1B_55K_N.
DR InterPro; IPR002612; Adeno_E1B_55kDa.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF01696; Adeno_E1B_55K; 1.
DR Pfam; PF04623; Adeno_E1B_55K_N; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Early protein {ECO:0000256|ARBA:ARBA00022518};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Modulation of host cell apoptosis by virus {ECO:0000256|ARBA:ARBA00023323}.
FT DOMAIN 1..65
FT /note="Adenovirus E1B protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04623"
FT REGION 53..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 53825 MW; 11E9243F7FCAE99E CRC64;
MEQPDPAVPG VHPGLHQPAA VEVLAAPAGL QLLAGAASAR AGIVAGGAVA GGEAEGGGAG
GGAGAGASAA VRPGPSGGEG GLSAEPQVAE GQVGPKRSPK RAKKEEEQSE EALTRLTLSL
INRQRPETVF YYELEHEFQH GDMHLQCKFG FEQIKTHWLE PWEDMATVLN QFVKVALRPD
RVYKVSSTVH LRKCVYVIGN GATVEVEGSD RVAFNCLMQR MGPGVMGLSG VTFENVRLVC
RDFHGVMFSC TTELNLHGVY FFNVNHACVE CWGQLRARGC TFHQCFKGVV GRPKSRVSIK
KCVFERCLLG VCVEGHGRLR HNAASENICF ALIKGTAVLK SNMICGTGDD RGGKHLITCA
NGWCHCLRSV HVVSHPRRSW PLFESNMLMR CTVHLGARRG MFLPHQCNFS HTSVLLEPEA
FTRVCFNAVF DMSLEVFKIV RYDESRARSR LCECGANHLR SVPLTVNVTE ELRADHVMLP
CNRTDYATSD EESG
//
