ID   E1B55_ADECC             Reviewed;         444 AA.
AC   Q65943;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   23-FEB-2022, entry version 39.
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 CLL) (CAdV-1) (Canine adenovirus 1
OS   (strain CLL)).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX   NCBI_TaxID=69150;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Campbell J.B., Zhao Y.;
RT   "DNA sequence and genomic organization of canine adenovirus type 1.";
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P03243}.
CC   -!- SUBUNIT: Interacts with the transactivation domain of TP53 (via N-
CC       terminus); this interaction leads to the inhibition of TP53 function
CC       and/or its degradation. Interacts with host PML-4 and PML-5; this
CC       interaction promotes efficient subnuclear targeting of E1B-55K to PML
CC       nuclear bodies. Interacts with E4-ORF3 protein. Interacts with E4-ORF6
CC       protein. Interacts with host DAXX protein; this interaction might
CC       alterate the normal interactions of DAXX, PML, and p53, which may
CC       contribute to cell transformation. {ECO:0000250|UniProtKB:P03243,
CC       ECO:0000250|UniProtKB:P03244}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03243}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P03243}. Note=Colocalizes with host
CC       TP53 to host PML nuclear bodies. PML localization of E1B-55K is
CC       necessary for E1B-55K-dependent SUMOylation of TP53.
CC       {ECO:0000250|UniProtKB:P03243}.
CC   -!- DOMAIN: Contains a PML interaction motif that allows the subnuclear PML
CC       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; U55001; AAB05431.1; -; Genomic_DNA.
DR   SMR; Q65943; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
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
FT                   /note="E1B 55 kDa protein"
FT                   /id="PRO_0000221730"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   444 AA;  49271 MW;  4A37C8980D242064 CRC64;
     MEQDSDLESG RATNQRPPRV RVRGAGVRGR GRVRRRALSE GQRRSPFRLD DLQLPDSLYV
     TRALQRDHAL EMPRGQVDFS LIEAEERRAG PTDEWYFESV KTYRAKPGDD LQTLIKNYAK
     ISLECGAVYE INSKIVVTGA CYIIGNCAVL RANLPVGTAM FEVLNVDVIP SIGFMERIVF
     SNILFDCRST TAVVCCISER NTLFHNCVFS GPHMLCLDIR AGAEVRGCHF VGAVCALRSK
     GLYSVRVRNS IFEKCAFGVV SGSKASISHS MFKDCACCIM FGGQGTIAHS HFMATTCTDT
     PMNLQLCTCE GNGSHVVPLG NIHFASNREA PWPTFNANVL VRVRLYMGRR RGVFHPKQST
     FSMCVIAAPR GVVQRIYLFS VYDATCAILQ LGEAGDAATE RLCTRGMRHN TPSLRAAYVT
     DTRIDREINS QDTAEFFSSD EDNL