AGNO_POVJC
ID AGNO_POVJC Reviewed; 71 AA.
AC P03086;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Agnoprotein;
DE AltName: Full=Agno;
OS JC polyomavirus (JCPyV) (JCV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=10632;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6086957; DOI=10.1128/jvi.51.2.458-469.1984;
RA Frisque R.J., Bream G.L., Cannella M.T.;
RT "Human polyomavirus JC virus genome.";
RL J. Virol. 51:458-469(1984).
RN [2]
RP SUBCELLULAR LOCATION, FUNCTION, AND PHOSPHORYLATION.
RX PubMed=11517407; DOI=10.1080/13550280152537148;
RA Okada Y., Endo S., Takahashi H., Sawa H., Umemura T., Nagashima K.;
RT "Distribution and function of JCV agnoprotein.";
RL J. Neurovirol. 7:302-306(2001).
RN [3]
RP INTERACTION WITH LARGE T ANTIGEN.
RX PubMed=11152520; DOI=10.1128/jvi.75.3.1476-1486.2001;
RA Safak M., Barrucco R., Darbinyan A., Okada Y., Nagashima K., Khalili K.;
RT "Interaction of JC virus agno protein with T antigen modulates
RT transcription and replication of the viral genome in glial cells.";
RL J. Virol. 75:1476-1486(2001).
RN [4]
RP INTERACTION WITH HOST YBX1.
RX PubMed=11907223; DOI=10.1128/jvi.76.8.3828-3838.2002;
RA Safak M., Sadowska B., Barrucco R., Khalili K.;
RT "Functional interaction between JC virus late regulatory agnoprotein and
RT cellular Y-box binding transcription factor, YB-1.";
RL J. Virol. 76:3828-3838(2002).
RN [5]
RP INTERACTION WITH HOST TP53, AND FUNCTION.
RX PubMed=12165856; DOI=10.1038/sj.onc.1205744;
RA Darbinyan A., Darbinian N., Safak M., Radhakrishnan S., Giordano A.,
RA Khalili K.;
RT "Evidence for dysregulation of cell cycle by human polyomavirus, JCV, late
RT auxiliary protein.";
RL Oncogene 21:5574-5581(2002).
RN [6]
RP INTERACTION WITH HOST FEZ1.
RX PubMed=15843383; DOI=10.1074/jbc.m411499200;
RA Suzuki T., Okada Y., Semba S., Orba Y., Yamanouchi S., Endo S., Tanaka S.,
RA Fujita T., Kuroda S., Nagashima K., Sawa H.;
RT "Identification of FEZ1 as a protein that interacts with JC virus
RT agnoprotein and microtubules: role of agnoprotein-induced dissociation of
RT FEZ1 from microtubules in viral propagation.";
RL J. Biol. Chem. 280:24948-24956(2005).
RN [7]
RP INTERACTION WITH HUMAN CBX5, AND SUBCELLULAR LOCATION.
RX PubMed=15864296; DOI=10.1038/sj.embor.7400406;
RA Okada Y., Suzuki T., Sunden Y., Orba Y., Kose S., Imamoto N., Takahashi H.,
RA Tanaka S., Hall W.W., Nagashima K., Sawa H.;
RT "Dissociation of heterochromatin protein 1 from lamin B receptor induced by
RT human polyomavirus agnoprotein: role in nuclear egress of viral
RT particles.";
RL EMBO Rep. 6:452-457(2005).
RN [8]
RP MUTAGENESIS OF SER-7; SER-11 AND THR-21, AND PHOSPHORYLATION AT SER-7;
RP SER-11 AND THR-21.
RX PubMed=16571806; DOI=10.1128/jvi.80.8.3893-3903.2006;
RA Sariyer I.K., Akan I., Palermo V., Gordon J., Khalili K., Safak M.;
RT "Phosphorylation mutants of JC virus agnoprotein are unable to sustain the
RT viral infection cycle.";
RL J. Virol. 80:3893-3903(2006).
RN [9]
RP INTERACTION WITH SMALL T ANTIGEN AND HOST PP2A.
RX PubMed=18353419; DOI=10.1016/j.virol.2008.02.020;
RA Sariyer I.K., Khalili K., Safak M.;
RT "Dephosphorylation of JC virus agnoprotein by protein phosphatase 2A:
RT inhibition by small t antigen.";
RL Virology 375:464-479(2008).
RN [10]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTATION OF 8-ARG-LYS-9.
RX PubMed=20300659; DOI=10.1371/journal.ppat.1000801;
RA Suzuki T., Orba Y., Okada Y., Sunden Y., Kimura T., Tanaka S.,
RA Nagashima K., Hall W.W., Sawa H.;
RT "The human polyoma JC virus agnoprotein acts as a viroporin.";
RL PLoS Pathog. 6:E1000801-E1000801(2010).
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. {ECO:0000269|PubMed:11517407,
CC ECO:0000269|PubMed:12165856, ECO:0000269|PubMed:20300659}.
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 PP2A subunits for
CC dephosphorylation. Interacts (via N-terminus) with host YBX1; this
CC interaction modulates transcriptional activity genomic promoters.
CC Interacts (via N-terminus) with host TP53. Interacts with host FEZ1;
CC this interaction disrupts the association between FEZ1 and
CC microtubules. Interacts with host CBX5; this interaction induces the
CC dissociation of CBX5 from LBR, resulting in destabilization of the
CC nuclear envelope. {ECO:0000250, ECO:0000269|PubMed:11152520,
CC ECO:0000269|PubMed:11907223, ECO:0000269|PubMed:12165856,
CC ECO:0000269|PubMed:15843383, ECO:0000269|PubMed:15864296,
CC ECO:0000269|PubMed:18353419, ECO:0000269|PubMed:20300659}.
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:11517407,
CC ECO:0000269|PubMed:15864296, ECO:0000269|PubMed:20300659}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=5;
CC Name=Agno;
CC IsoId=P03086-1; Sequence=Displayed;
CC Name=VP1; Synonyms=Major capsid protein VP1;
CC IsoId=P03089-1; Sequence=External;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P03095-1; Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P03095-2; Sequence=External;
CC Name=VP4; Synonyms=Viroporin VP4;
CC IsoId=P03095-3; Sequence=External;
CC -!- PTM: Phosphorylated by host PKC. Phosphorylation alters the stability
CC and may also have an impact on the subcellular location (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Agno]: Produced by alternative initiation of
CC the late mRNA.
CC -!- SIMILARITY: Belongs to the polyomavirus agnoprotein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02226; AAA82098.1; -; Genomic_DNA.
DR PIR; A03623; DNVPJ.
DR RefSeq; NP_043508.1; NC_001699.1. [P03086-1]
DR PDB; 2MJ2; NMR; -; A=17-52.
DR PDB; 5NHQ; NMR; -; A=1-71.
DR PDBsum; 2MJ2; -.
DR PDBsum; 5NHQ; -.
DR BMRB; P03086; -.
DR SMR; P03086; -.
DR TCDB; 1.A.96.1.1; the human polyoma virus viroporin (pvvp) family.
DR iPTMnet; P03086; -.
DR DNASU; 1489519; -.
DR GeneID; 1489519; -.
DR KEGG; vg:1489519; -.
DR Proteomes; UP000008478; 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 3D-structure; Alternative initiation; Alternative splicing;
KW Host cell membrane; Host cytoplasm; Host endoplasmic reticulum;
KW Host membrane; Host nucleus; Host-virus interaction; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport; Viral ion channel.
FT CHAIN 1..71
FT /note="Agnoprotein"
FT /id="PRO_0000115033"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 45..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:16571806"
FT MOD_RES 11
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:16571806"
FT MOD_RES 21
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000269|PubMed:16571806"
FT MUTAGEN 7
FT /note="S->A: Partial loss of phosphorylation, defective in
FT encapsidation of viral DNA; when associated with A-8 and T-
FT 21."
FT /evidence="ECO:0000269|PubMed:16571806"
FT MUTAGEN 8..9
FT /note="RK->AA: Impaired viral propagation."
FT MUTAGEN 11
FT /note="S->A: Partial loss of phosphorylation, defective in
FT encapsidation of viral DNA; when associated with A-7 and T-
FT 21."
FT /evidence="ECO:0000269|PubMed:16571806"
FT MUTAGEN 21
FT /note="T->A: Partial loss of phosphorylation, defective in
FT encapsidation of viral DNA; when associated with A-7 and A-
FT 8."
FT /evidence="ECO:0000269|PubMed:16571806"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:5NHQ"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:5NHQ"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:2MJ2"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2MJ2"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5NHQ"
SQ SEQUENCE 71 AA; 8081 MW; 3E459BFCC541E53B CRC64;
MVLRQLSRKA SVKVSKTWSG TKKRAQRILI FLLEFLLDFC TGEDSVDGKK RQRHSGLTEQ
TYSALPEPKA T
