ST_POVK3
ID ST_POVK3 Reviewed; 191 AA.
AC P0DOJ0; A3R4N0; A3R4N5; A3R4P0;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 23-FEB-2022, entry version 13.
DE RecName: Full=Small t antigen;
DE Short=ST;
DE Short=ST-AG;
OS KI polyomavirus (isolate Stockholm 380) (KIPyV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=423448;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17287263; DOI=10.1128/jvi.00028-07;
RA Allander T., Andreasson K., Gupta S., Bjerkner A., Bogdanovic G.,
RA Persson M.A., Dalianis T., Ramqvist T., Andersson B.;
RT "Identification of a third human polyomavirus.";
RL J. Virol. 81:4130-4136(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=P0DOJ0-1, A3R4N5-1;
CC Sequence=Displayed;
CC Name=Large T antigen;
CC IsoId=P0DOI7-1, A3R4N4-1;
CC 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; EF127908; ABN09930.1; -; Genomic_DNA.
DR SMR; P0DOJ0; -.
DR Proteomes; UP000166765; 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; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..191
FT /note="Small t antigen"
FT /id="PRO_0000442717"
FT DOMAIN 12..80
FT /note="J"
FT ZN_FING 117..130
FT /note="C4-type; atypical"
FT ZN_FING 136..157
FT /note="H1C3-type; atypical"
FT MOD_RES 1
FT /note="N-acetylmethionine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03081"
SQ SEQUENCE 191 AA; 23179 MW; C5657006B8B3CF8C CRC64;
MDKTLSREEA KQLMQLLCLD MSCWGNLPLM RRQYLVKCKE YHPDKGGNEE SMKLLNSLYL
KLQDSVSSVH DLNEEEDNIW QSSQVYCKDL CCNKFRLVGA IYGDYYEAYI MKQWDVCIHG
YNHECQCIHC ILSKYHKEKY KIYRKPPVWI ECYCYKCYRE WFFFPISMQT FFFWKVIIFN
TEIRAVQPLL R