ID   ST_POVWU                Reviewed;         194 AA.
AC   A5HBD7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   29-SEP-2021, entry version 64.
DE   RecName: Full=Small t antigen;
DE            Short=ST;
DE            Short=ST-AG;
OS   WU polyomavirus (WUPyV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX   NCBI_TaxID=440266;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B0, S1, S2, S3, S4, and S5;
RX   PubMed=17480120; DOI=10.1371/journal.ppat.0030064;
RA   Gaynor A.M., Nissen M.D., Whiley D.M., Mackay I.M., Lambert S.B., Wu G.,
RA   Brennan D.C., Storch G.A., Sloots T.P., Wang D.;
RT   "Identification of a novel polyomavirus from patients with acute
RT   respiratory tract infections.";
RL   PLoS Pathog. 3:595-604(2007).
CC   -!- FUNCTION: Promotes efficient viral genome replication by accelerating
CC       both G1 and S phase progression of the cell cycle. Inhibits host PP2A
CC       by binding to the A subunit, thereby displacing lower affinity
CC       regulatory B subunit. Inactivation of PP2A in turn results in the
CC       transactivation of cyclin A and cyclin D1 promoters. Late during the
CC       infection cycle, ST may induce dephosphorylation of host MTOR, leading
CC       to the inhibition of cap-dependent translation. May establish and
CC       maintain high levels of viral genomes during persistent infection in
CC       cell culture. {ECO:0000250|UniProtKB:P03081}.
CC   -!- SUBUNIT: Interacts with host PPP2R1A; the interaction inhibits PP2A
CC       activity. {ECO:0000250|UniProtKB:P03081}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm. Host nucleus
CC       {ECO:0000250|UniProtKB:P03081}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Small t antigen;
CC         IsoId=A5HBD7-1; Sequence=Displayed;
CC       Name=Large T antigen;
CC         IsoId=A5HBG1-1; Sequence=External;
CC   -!- DOMAIN: The common region of ST and LT proteins comprises the J domain.
CC       This domain is essential for multiple viral activities, including
CC       virion assembly, viral DNA replication, transformation and
CC       transcriptional activation. This domain is also required for cyclin A-
CC       transactivating activity of ST. {ECO:0000250|UniProtKB:P03081}.
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DR   EMBL; EF444549; ABQ09293.1; -; Genomic_DNA.
DR   EMBL; EF444550; ABQ09298.1; -; Genomic_DNA.
DR   EMBL; EF444551; ABQ09303.1; -; Genomic_DNA.
DR   EMBL; EF444552; ABQ09308.1; -; Genomic_DNA.
DR   EMBL; EF444553; ABQ09313.1; -; Genomic_DNA.
DR   EMBL; EF444554; ABQ09318.1; -; Genomic_DNA.
DR   RefSeq; YP_001285489.1; NC_009539.1. [A5HBD7-1]
DR   SMR; A5HBD7; -.
DR   GeneID; 5309722; -.
DR   KEGG; vg:5309722; -.
DR   Proteomes; UP000096057; Genome.
DR   Proteomes; UP000114161; Genome.
DR   Proteomes; UP000118542; Genome.
DR   Proteomes; UP000119623; Genome.
DR   Proteomes; UP000148617; Genome.
DR   Proteomes; UP000153939; Genome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.110; -; 1.
DR   Gene3D; 1.20.120.1860; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR003354; Papo_T_antigen.
DR   InterPro; IPR036092; Papo_T_antigensf.
DR   Pfam; PF02380; Papo_T_antigen; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF161240; SSF161240; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
PE   3: Inferred from homology;
KW   Acetylation; Activator; Alternative splicing; Early protein;
KW   Host cytoplasm; Host nucleus; Host-virus interaction; Metal-binding;
KW   Oncogene; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..194
FT                   /note="Small t antigen"
FT                   /id="PRO_0000294071"
FT   DOMAIN          12..80
FT                   /note="J"
FT   ZN_FING         121..134
FT                   /note="C4-type; atypical"
FT   ZN_FING         140..161
FT                   /note="H1C3-type; atypical"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03081"
SQ   SEQUENCE   194 AA;  23467 MW;  8F2A175E8BF1236E CRC64;
     MDKTLSRNEA KELMQLLGLD MTCWGNLPLM RTKYLSKCKE FHPDKGGNEE KMKKLNSLYL
     KLQECVSTVH QLNEEEDEVW SSSQVECTEL CCNFPPRKYR LVGEVYGDVF EEYILKDWDI
     CLKGFYYLCN CFYCFLDKRH KQKYKIFRKP PMWIECYCYR CYREWFGFEI SAETFFYWKK
     IIFLTTMQGV GLTR