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AGNO_SV40
ID   AGNO_SV40               Reviewed;          62 AA.
AC   P03084;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-DEC-2020, entry version 82.
DE   RecName: Full=Agnoprotein;
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].
RC   STRAIN=A2895;
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].
RC   STRAIN=776, and A2895;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A2895;
RX   PubMed=1328671; DOI=10.1128/jvi.66.11.6353-6360.1992;
RA   Ilyinskii P.O., Daniel M.D., Horvath C., Desrosiers R.C.;
RT   "Genetic analysis of simian virus 40 from brains and kidneys of macaque
RT   monkeys.";
RL   J. Virol. 66:6353-6360(1992).
RN   [4]
RP   ALTERNATIVE SPLICING.
RX   PubMed=211423; DOI=10.1038/273070a0;
RA   Haegeman G., Fiers W.;
RT   "Evidence for 'splicing' of SV40 16S mRNA.";
RL   Nature 273:70-73(1978).
RN   [5]
RP   PRELIMINARY CHARACTERIZATION.
RX   PubMed=6262654; DOI=10.1038/291346a0;
RA   Jay G., Nomura S., Anderson C.W., Khoury G.;
RT   "Identification of the SV40 agnogene product: a DNA binding protein.";
RL   Nature 291:346-349(1981).
RN   [6]
RP   PHOSPHORYLATION.
RX   PubMed=6273846; DOI=10.1073/pnas.78.10.6081;
RA   Jackson V., Chalkley R.;
RT   "Use of whole-cell fixation to visualize replicating and maturing simian
RT   virus 40: identification of new viral gene product.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:6081-6085(1981).
RN   [7]
RP   FUNCTION.
RX   PubMed=6286139; DOI=10.1016/0092-8674(82)90102-7;
RA   Hay N., Skolnik-David H., Aloni Y.;
RT   "Attenuation in the control of SV40 gene expression.";
RL   Cell 29:183-193(1982).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=6296448; DOI=10.1128/jvi.45.1.428-433.1983;
RA   Nomura S., Khoury G., Jay G.;
RT   "Subcellular localization of the simian virus 40 agnoprotein.";
RL   J. Virol. 45:428-433(1983).
RN   [9]
RP   FUNCTION.
RX   PubMed=3023658; DOI=10.1128/jvi.60.3.1055-1061.1986;
RA   Carswell S., Alwine J.C.;
RT   "Simian virus 40 agnoprotein facilitates perinuclear-nuclear localization
RT   of VP1, the major capsid protein.";
RL   J. Virol. 60:1055-1061(1986).
RN   [10]
RP   FUNCTION.
RX   PubMed=3023661; DOI=10.1128/jvi.60.3.1098-1106.1986;
RA   Resnick J., Shenk T.;
RT   "Simian virus 40 agnoprotein facilitates normal nuclear location of the
RT   major capsid polypeptide and cell-to-cell spread of virus.";
RL   J. Virol. 60:1098-1106(1986).
RN   [11]
RP   REVIEW.
RX   PubMed=15573377; DOI=10.1002/jcp.20266;
RA   Khalili K., White M.K., Sawa H., Nagashima K., Safak M.;
RT   "The agnoprotein of polyomaviruses: a multifunctional auxiliary protein.";
RL   J. Cell. Physiol. 204:1-7(2005).
CC   -!- FUNCTION: Alters the structure of the nuclear envelope by interacting
CC       with host CBX5 and disrupting CBX5 association with LBR. Involved in
CC       the perinuclear-nuclear localization of the capsid protein VP1 during
CC       virion assembly and maturation. Plays an important role in the release
CC       of progeny virions from infected cells and in viral propagation,
CC       probably by acting as a viral ionic channel in the host plasma
CC       membrane. Allows influx of extracellular calcium ions in the host cell.
CC       May contribute to viral genome transcription and translation of viral
CC       late proteins (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:3023658, ECO:0000269|PubMed:3023661,
CC       ECO:0000269|PubMed:6286139}.
CC   -!- SUBUNIT: Homooligomer. Interacts with VP1 (By similarity). Interacts
CC       with large T antigen; this interaction may impact upon the activity of
CC       T-antigen on the control of viral gene transcription and replication.
CC       Interacts with small t antigen. Interacts with host CBX5; this
CC       interaction induces the dissociation of CBX5 from LBR, resulting in
CC       destabilization of the nuclear envelope (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. Host nucleus
CC       membrane {ECO:0000305}; Single-pass type II membrane protein
CC       {ECO:0000305}. Host rough endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass type II membrane protein {ECO:0000305}. Host cell membrane
CC       {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC       Note=Mostly perinuclear. {ECO:0000269|PubMed:6296448}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=5;
CC       Name=Agno;
CC         IsoId=P03084-1; Sequence=Displayed;
CC       Name=VP1; Synonyms=Major capsid protein VP1;
CC         IsoId=P03087-1; Sequence=External;
CC       Name=VP2; Synonyms=Minor capsid protein VP2;
CC         IsoId=P03093-1; Sequence=External;
CC       Name=VP3; Synonyms=Minor capsid protein VP3;
CC         IsoId=P03093-2; Sequence=External;
CC       Name=VP4; Synonyms=Viroporin VP4;
CC         IsoId=P03093-3; Sequence=External;
CC   -!- PTM: Phosphorylated by host kinase. Phosphorylation segregates
CC       agnoprotein in cytoplasm, whereas unphosphorylated agnoprotein migrate
CC       to the nucleus (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform Agno]: Produced by alternative initiation of
CC       the late mRNA (16s and 19s mRNAs).
CC   -!- SIMILARITY: Belongs to the polyomaviruses agnoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; M99357; AAB59791.1; -; Genomic_DNA.
DR   EMBL; M99359; AAB59794.1; -; Genomic_DNA.
DR   EMBL; M99361; AAB59777.1; -; Genomic_DNA.
DR   EMBL; M99363; AAB59778.1; -; Genomic_DNA.
DR   EMBL; J02400; AAB59920.1; -; Genomic_DNA.
DR   EMBL; M99346; AAB59800.1; -; Genomic_DNA.
DR   PIR; D03631; DNVPA4.
DR   RefSeq; YP_003708378.1; NC_001669.1.
DR   SMR; P03084; -.
DR   Proteomes; UP000007705; Genome.
DR   GO; GO:0044200; C:host cell nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044169; C:host cell rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   InterPro; IPR002643; Polyoma_agno.
DR   Pfam; PF01736; Polyoma_agno; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; Alternative splicing; Host cell membrane;
KW   Host cytoplasm; Host endoplasmic reticulum; Host membrane; Host nucleus;
KW   Host-virus interaction; Ion channel; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Transport; Viral ion channel.
FT   CHAIN           1..62
FT                   /note="Agnoprotein"
FT                   /id="PRO_0000115034"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..40
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..62
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        26
FT                   /note="Q -> R (in Ref. 3; AAB59800)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   62 AA;  7336 MW;  C6E6E59E2D9FECEA CRC64;
     MVLRRLSRQA SVKVRRSWTE SKKTAQRLFV FVLELLLQFC EGEDTVDGKR KKPERLTEKP
     ES
 
 
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