ID   E1B55_ADECR             Reviewed;         444 AA.
AC   Q96679;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   14-OCT-2015, entry version 40.
DE   RecName: Full=E1B 55 kDa protein;
DE            Short=E1B-55K;
DE   AltName: Full=E1B protein, large T-antigen;
DE   AltName: Full=E1B-495R;
OS   Canine adenovirus serotype 1 (strain RI261) (CAdV-1) (Canine
OS   adenovirus 1 (strain RI261)).
OC   Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus;
OC   Canine mastadenovirus A.
OX   NCBI_TaxID=69151;
OH   NCBI_TaxID=9615; Canis familiaris (Dog) (Canis lupus familiaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9129661;
RA   Morrison M.D., Onions D.E., Nicolson L.;
RT   "Complete DNA sequence of canine adenovirus type 1.";
RL   J. Gen. Virol. 78:873-878(1997).
CC   -!- FUNCTION: Plays a major role to prevent cellular inhibition of
CC       viral genome replication. Assembles an SCF-like E3 ubiquitin
CC       ligase complex based on the cellular proteins TCEB2, TCEB1, CUL5
CC       and RBX1, in cooperation with viral E4orf6. This viral RING-type
CC       ligase ubiquitinates cellular substrates and targets them to
CC       proteasomal degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN)
CC       complex, ITGA3, DAXX and BLM. Degradation of host TP53/p53
CC       activity is essential for preventing E1A-induced TP53 accumulation
CC       that would otherwise lead to cell apoptosis and growth arrest.
CC       E1B-55K also inactivates TP53 transcription-factor activity by
CC       binding its transactivation domain. E1B-55K also functions as a
CC       SUMO1 E3 ligase for TP53 which causes the latter to be sequestered
CC       in promyelocytic leukemia (PML) nuclear bodies thereby
CC       contributing to maximal inhibition of TP53 function.
CC       {ECO:0000250|UniProtKB:P03243}.
CC   -!- SUBUNIT: Interacts with the transactivation domain of TP53 (via N-
CC       terminus); this interaction leads to the inhibition of TP53
CC       function and/or its degradation. Interacts with host PML-4 and
CC       PML-5; this interaction promotes efficient subnuclear targeting of
CC       E1B-55K to PML nuclear bodies. Interacts with E4-ORF3 protein.
CC       Interacts with E4-ORF6 protein. Interacts with host DAXX protein;
CC       this interaction might alterate the normal interactions of DAXX,
CC       PML, and p53, which may contribute to cell transformation.
CC       {ECO:0000250|UniProtKB:P03243, ECO:0000250|UniProtKB:P03244}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03243}.
CC       Host cytoplasm {ECO:0000250|UniProtKB:P03243}. Note=Colocalizes
CC       with host TP53 to host PML nuclear bodies. PML localization of
CC       E1B-55K is necessary for E1B-55K-dependent SUMOylation of TP53.
CC       {ECO:0000250|UniProtKB:P03243}.
CC   -!- DOMAIN: Contains a PML interaction motif that allows the
CC       subnuclear PML localization. {ECO:0000250|UniProtKB:P03243}.
CC   -!- SIMILARITY: Belongs to the adenoviridae E1B 55 kDa protein family.
CC       {ECO:0000305}.
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DR   EMBL; Y07760; CAA69054.1; -; Genomic_DNA.
DR   RefSeq; AP_000047.1; AC_000003.1.
DR   RefSeq; NP_044186.1; NC_001734.1.
DR   GeneID; 1488948; -.
DR   KEGG; vg:1488948; -.
DR   InterPro; IPR002612; Adeno_E1B_55kDa.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF01696; Adeno_E1B_55K; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Early protein; Host cytoplasm; Host nucleus; Host-virus interaction;
KW   Modulation of host cell apoptosis by virus.
FT   CHAIN         1    444       E1B 55 kDa protein.
FT                                /FTId=PRO_0000221731.
SQ   SEQUENCE   444 AA;  49200 MW;  01073C78F1AC8736 CRC64;
     MEQDSDLESG RATNQRPPRV RVRGAGVRGR GRVRRRALSE GQRRSLFRLD DLQLPDSLYV
     TRALQRDHAL EMPRGQVDFS LIEAEERRAG PTDEWYFESV KTYRAKPGDD LQTLIKNYAK
     ISLECGAVYE INSKIVVTGA CYIIGNCAVL RANLPVGTAM FEVLNVDVIP SIGFMERIVF
     SNILFDCRST TAVVCCISER NTLFHNCVFS GPHMLCLDIR AGAEVRGCHF VGAVCALRSK
     GLYSVRVRNS IFEKCAFGVV SGSKASISHS MFKDCACCIM LGGQGTIAHS HFMATTCTDT
     PMNLQLCTCE GNGSHVVPLG NIHFASNREA PWPTFNANVL VRVRLYMGRR RGVFHPKQST
     FSMCVIAAPR GVVQRIYLFS VYDATCAILQ LGEAGDAATE RLCTCGMRHN TPSLRAAYVT
     DTRIDREINS QDTAEFFSSD EDNL
//