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ST_SV40
ID   ST_SV40                 Reviewed;         174 AA.
AC   P03081;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-SEP-2021, entry version 128.
DE   RecName: Full=Small t antigen;
DE            Short=ST;
DE            Short=ST-AG;
OS   Simian virus 40 (SV40).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX   NCBI_TaxID=1891767;
OH   NCBI_TaxID=9539; Macaca (macaques).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=205947; DOI=10.1126/science.205947;
RA   Reddy V.B., Thimmappaya B., Dhar R., Subramanian K.N., Zain B.S., Pan J.,
RA   Ghosh P.K., Celma M.L., Weissman S.M.;
RT   "The genome of simian virus 40.";
RL   Science 200:494-502(1978).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ACETYLATION AT MET-1.
RC   STRAIN=776;
RX   PubMed=205802; DOI=10.1038/273113a0;
RA   Fiers W., Contreras R., Haegeman G., Rogiers R., van de Voorde A.,
RA   van Heuverswyn H., van Herreweghe J., Volckaert G., Ysebaert M.;
RT   "Complete nucleotide sequence of SV40 DNA.";
RL   Nature 273:113-120(1978).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=6323762; DOI=10.1128/jvi.50.2.623-628.1984;
RA   Ellman M., Bikel I., Figge J., Roberts T., Schlossman R., Livingston D.M.;
RT   "Localization of the simian virus 40 Small t antigen in the nucleus and
RT   cytoplasm of monkey and mouse cells.";
RL   J. Virol. 50:623-628(1984).
RN   [4]
RP   INHIBITION OF HOST PP2A ACTIVITY.
RX   PubMed=1848668; DOI=10.1128/mcb.11.4.1996-2003.1991;
RA   Scheidtmann K.H., Mumby M.C., Rundell K., Walter G.;
RT   "Dephosphorylation of simian virus 40 large-T antigen and p53 protein by
RT   protein phosphatase 2A: inhibition by small-t antigen.";
RL   Mol. Cell. Biol. 11:1996-2003(1991).
RN   [5]
RP   INTERACTION WITH HOST PP2A.
RX   PubMed=1706474; DOI=10.1128/mcb.11.4.1988-1995.1991;
RA   Yang S.-L., Lickteig R.L., Estes R., Rundell K., Walter G., Mumby M.C.;
RT   "Control of protein phosphatase 2A by simian virus 40 small-t antigen.";
RL   Mol. Cell. Biol. 11:1988-1995(1991).
RN   [6]
RP   INTERACTION WITH HOST PP2A.
RX   PubMed=8107228; DOI=10.1128/jvi.68.3.1675-1681.1994;
RA   Mungre S., Enderle K., Turk B., Porras A., Wu Y.Q., Mumby M.C., Rundell K.;
RT   "Mutations which affect the inhibition of protein phosphatase 2A by simian
RT   virus 40 small-t antigen in vitro decrease viral transformation.";
RL   J. Virol. 68:1675-1681(1994).
RN   [7]
RP   FUNCTION.
RX   PubMed=8794333; DOI=10.1128/jvi.70.10.6902-6908.1996;
RA   Porras A., Bennett J., Howe A., Tokos K., Bouck N., Henglein B.,
RA   Sathyamangalam S., Thimmapaya B., Rundell K.;
RT   "A novel simian virus 40 early-region domain mediates transactivation of
RT   the cyclin A promoter by small-t antigen and is required for transformation
RT   in small-t antigen-dependent assays.";
RL   J. Virol. 70:6902-6908(1996).
RN   [8]
RP   FUNCTION.
RX   PubMed=8917510; DOI=10.1073/pnas.93.23.12861;
RA   Watanabe G., Howe A., Lee R.J., Albanese C., Shu I.W., Karnezis A.N.,
RA   Zon L., Kyriakis J., Rundell K., Pestell R.G.;
RT   "Induction of cyclin D1 by simian virus 40 small tumor antigen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12861-12866(1996).
RN   [9]
RP   DOMAIN.
RX   PubMed=9108037; DOI=10.1073/pnas.94.8.3679;
RA   Kelley W.L., Georgopoulos C.;
RT   "The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens
RT   can functionally replace the J-domain of the Escherichia coli DnaJ
RT   molecular chaperone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3679-3684(1997).
RN   [10]
RP   FUNCTION.
RX   PubMed=15890927; DOI=10.1128/jvi.79.11.6882-6889.2005;
RA   Yu Y., Kudchodkar S.B., Alwine J.C.;
RT   "Effects of simian virus 40 large and small tumor antigens on mammalian
RT   target of rapamycin signaling: small tumor antigen mediates
RT   hypophosphorylation of eIF4E-binding protein 1 late in infection.";
RL   J. Virol. 79:6882-6889(2005).
RN   [11]
RP   FUNCTION.
RX   PubMed=15680424; DOI=10.1016/j.virol.2004.12.017;
RA   Skoczylas C., Henglein B., Rundell K.;
RT   "PP2A-dependent transactivation of the cyclin A promoter by SV40 ST is
RT   mediated by a cell cycle-regulated E2F site.";
RL   Virology 332:596-601(2005).
RN   [12]
RP   FUNCTION.
RX   PubMed=17936323; DOI=10.1016/j.virol.2007.09.008;
RA   Fahrbach K.M., Katzman R.B., Rundell K.;
RT   "Role of SV40 ST antigen in the persistent infection of mesothelial
RT   cells.";
RL   Virology 370:255-263(2008).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 87-174.
RX   PubMed=17529992; DOI=10.1038/nsmb1254;
RA   Chen Y., Xu Y., Bao Q., Xing Y., Li Z., Lin Z., Stock J.B., Jeffrey P.D.,
RA   Shi Y.;
RT   "Structural and biochemical insights into the regulation of protein
RT   phosphatase 2A by small t antigen of SV40.";
RL   Nat. Struct. Mol. Biol. 14:527-534(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 eIF4E-binding
CC       protein EIF4EBP1 leading to the inhibition of cap-dependent
CC       translation. May establish and maintain high levels of viral genomes
CC       during persistent infection in cell culture.
CC       {ECO:0000269|PubMed:15680424, ECO:0000269|PubMed:15890927,
CC       ECO:0000269|PubMed:17936323, ECO:0000269|PubMed:8794333,
CC       ECO:0000269|PubMed:8917510}.
CC   -!- SUBUNIT: Interacts with host PPP2R1A; the interaction inhibits PP2A
CC       activity. {ECO:0000269|PubMed:1706474, ECO:0000269|PubMed:8107228}.
CC   -!- INTERACTION:
CC       P03081; P30153: PPP2R1A; Xeno; NbExp=5; IntAct=EBI-1266256, EBI-302388;
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:6323762}. Host
CC       nucleus {ECO:0000269|PubMed:6323762}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC       Name=Small t antigen;
CC         IsoId=P03081-1; Sequence=Displayed;
CC       Name=Large T antigen;
CC         IsoId=P03070-1; Sequence=External;
CC       Name=17kT antigen;
CC         IsoId=P03070-2; Sequence=External;
CC       Name=SELP;
CC         IsoId=P0C6L2-1; Sequence=External;
CC   -!- DOMAIN: The common region of SV40 ST, 17kT and LT proteins comprises
CC       the J domain. This domain is essential for multiple viral activities,
CC       including virion assembly, viral DNA replication, transformation and
CC       transcriptional activation. This domain is also required for cyclin A-
CC       transactivating activity of ST. {ECO:0000269|PubMed:9108037}.
CC   -!- MISCELLANEOUS: [Isoform Small t antigen]: Produced by alternative
CC       splicing.
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DR   EMBL; J02400; AAB59925.1; -; Genomic_DNA.
DR   PIR; C03631; TVVPA4.
DR   RefSeq; YP_003708383.1; NC_001669.1.
DR   PDB; 2PF4; X-ray; 3.10 A; E/F/G/H=1-174.
DR   PDB; 2PKG; X-ray; 3.30 A; C/D=87-174.
DR   PDBsum; 2PF4; -.
DR   PDBsum; 2PKG; -.
DR   SMR; P03081; -.
DR   DIP; DIP-29393N; -.
DR   IntAct; P03081; 3.
DR   MINT; P03081; -.
DR   iPTMnet; P03081; -.
DR   EvolutionaryTrace; P03081; -.
DR   Proteomes; UP000007705; 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   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   CDD; cd06257; DnaJ; 1.
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.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative initiation;
KW   Alternative splicing; Early protein;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus; Host cytoplasm;
KW   Host gene expression shutoff by virus; Host nucleus;
KW   Host-virus interaction; Metal-binding; Oncogene; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..174
FT                   /note="Small t antigen"
FT                   /id="PRO_0000115061"
FT   DOMAIN          12..75
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   ZN_FING         103..116
FT                   /note="C4-type; atypical"
FT   ZN_FING         122..143
FT                   /note="H1C3-type; atypical"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; by host"
FT                   /evidence="ECO:0000269|PubMed:205802"
FT   TURN            2..4
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   HELIX           7..15
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   TURN            16..18
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   HELIX           21..23
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   HELIX           27..37
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   TURN            50..53
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   HELIX           54..69
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   HELIX           73..76
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   TURN            94..96
FT                   /evidence="ECO:0007829|PDB:2PKG"
FT   HELIX           100..104
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:2PKG"
FT   HELIX           114..125
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   TURN            126..128
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   TURN            135..137
FT                   /evidence="ECO:0007829|PDB:2PKG"
FT   HELIX           141..147
FT                   /evidence="ECO:0007829|PDB:2PF4"
FT   HELIX           154..164
FT                   /evidence="ECO:0007829|PDB:2PF4"
SQ   SEQUENCE   174 AA;  20449 MW;  91EC925ED2E29668 CRC64;
     MDKVLNREES LQLMDLLGLE RSAWGNIPLM RKAYLKKCKE FHPDKGGDEE KMKKMNTLYK
     KMEDGVKYAH QPDFGGFWDA TEVFASSLNP GVDAMYCKQW PECAKKMSAN CICLLCLLRM
     KHENRKLYRK DPLVWVDCYC FDCFRMWFGL DLCEGTLLLW CDIIGQTTYR DLKL
 
 
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