PHOSP_BDVV
ID PHOSP_BDVV Reviewed; 201 AA.
AC P0C799; P26668;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 23-FEB-2022, entry version 39.
DE RecName: Full=Phosphoprotein;
DE Short=P protein;
DE AltName: Full=p23;
DE AltName: Full=p24;
GN Name=P/X;
OS Borna disease virus (strain V) (BDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Bornaviridae; unclassified Bornaviridae.
OX NCBI_TaxID=928296;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9352; Bradypodidae (three-fingered sloths).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=9850; Cervidae (deer).
OH NCBI_TaxID=109474; Crocidura leucodon (Bicoloured white-toothed shrew) (Celebes shrew).
OH NCBI_TaxID=9788; Equidae (horses).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=56798; Hexaprotodon liberiensis (Pygmy hippopotamus) (Choeropsis liberiensis).
OH NCBI_TaxID=9844; Lama glama (Llama).
OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=8801; Struthio camelus (Common ostrich).
OH NCBI_TaxID=9455; Varecia variegata (Black-and-white ruffed lemur) (Lemur variegatus).
OH NCBI_TaxID=30538; Vicugna pacos (Alpaca) (Lama pacos).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8183914; DOI=10.1073/pnas.91.10.4362;
RA Briese T., Schneemann A., Lewis A.J., Park Y.-S., Kim S., Ludwig H.,
RA Lipkin W.I.;
RT "Genomic organization of Borna disease virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4362-4366(1994).
RN [2]
RP INTERACTION WITH NUCLEOPROTEIN.
RX PubMed=9880009; DOI=10.1099/0022-1317-79-12-2957;
RA Berg M., Ehrenborg C., Blomberg J., Pipkorn R., Berg A.L.;
RT "Two domains of the Borna disease virus p40 protein are required for
RT interaction with the p23 protein.";
RL J. Gen. Virol. 79:2957-2963(1998).
RN [3]
RP SUBCELLULAR LOCATION, AND MOTIF.
RX PubMed=9811710; DOI=10.1128/jvi.72.12.9755-9762.1998;
RA Shoya Y., Kobayashi T., Koda T., Ikuta K., Kakinuma M., Kishi M.;
RT "Two proline-rich nuclear localization signals in the amino- and carboxyl-
RT terminal regions of the Borna disease virus phosphoprotein.";
RL J. Virol. 72:9755-9762(1998).
RN [4]
RP INTERACTION WITH POLYMERASE L, AND SUBCELLULAR LOCATION.
RX PubMed=10756058; DOI=10.1128/jvi.74.9.4425-4428.2000;
RA Walker M.P., Jordan I., Briese T., Fischer N., Lipkin W.I.;
RT "Expression and characterization of the Borna disease virus polymerase.";
RL J. Virol. 74:4425-4428(2000).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12829848; DOI=10.1128/jvi.77.14.8099-8107.2003;
RA Kobayashi T., Zhang G., Lee B.J., Baba S., Yamashita M., Kamitani W.,
RA Yanai H., Tomonaga K., Ikuta K.;
RT "Modulation of Borna disease virus phosphoprotein nuclear localization by
RT the viral protein X encoded in the overlapping open reading frame.";
RL J. Virol. 77:8099-8107(2003).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15509569; DOI=10.1074/jbc.m408913200;
RA Schneider U., Blechschmidt K., Schwemmle M., Staeheli P.;
RT "Overlap of interaction domains indicates a central role of the P protein
RT in assembly and regulation of the Borna disease virus polymerase complex.";
RL J. Biol. Chem. 279:55290-55296(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=16414989; DOI=10.1128/jvi.80.3.1121-1129.2006;
RA Yanai H., Kobayashi T., Hayashi Y., Watanabe Y., Ohtaki N., Zhang G.,
RA de la Torre J.C., Ikuta K., Tomonaga K.;
RT "A methionine-rich domain mediates CRM1-dependent nuclear export activity
RT of Borna disease virus phosphoprotein.";
RL J. Virol. 80:1121-1129(2006).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PHOSPHOPROTEIN.
RX PubMed=17079312; DOI=10.1128/jvi.01351-06;
RA Chase G., Mayer D., Hildebrand A., Frank R., Hayashi Y., Tomonaga K.,
RA Schwemmle M.;
RT "Borna disease virus matrix protein is an integral component of the viral
RT ribonucleoprotein complex that does not interfere with polymerase
RT activity.";
RL J. Virol. 81:743-749(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH HOST HMGB1.
RX PubMed=22607802; DOI=10.1016/j.chom.2012.04.009;
RA Matsumoto Y., Hayashi Y., Omori H., Honda T., Daito T., Horie M., Ikuta K.,
RA Fujino K., Nakamura S., Schneider U., Chase G., Yoshimori T., Schwemmle M.,
RA Tomonaga K.;
RT "Bornavirus closely associates and segregates with host chromosomes to
RT ensure persistent intranuclear infection.";
RL Cell Host Microbe 11:492-503(2012).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25810554; DOI=10.1128/jvi.00454-15;
RA Bonnaud E.M., Szelechowski M., Betourne A., Foret C., Thouard A.,
RA Gonzalez-Dunia D., Malnou C.E.;
RT "Borna disease virus phosphoprotein modulates epigenetic signaling in
RT neurons to control viral replication.";
RL J. Virol. 89:5996-6008(2015).
CC -!- FUNCTION: Essential component of the RNA polymerase transcription and
CC replication complex. Acts as a scaffold which brings L in close
CC proximity to the N-RNA complex. Plays a role in the segregation of the
CC viral genome in host daughter cells during mitosis by interacting with
CC host HMGB1, a host chromatin-remodeling DNA architectural protein,
CC thereby stabilizing RNP on chromosomes. Interacts with host TBK1 and
CC thus interferes with activation of cellular antiviral state. Inhibits
CC cellular histone acetyltransferase activities.
CC {ECO:0000250|UniProtKB:P0C798, ECO:0000269|PubMed:15509569,
CC ECO:0000269|PubMed:22607802, ECO:0000269|PubMed:25810554}.
CC -!- SUBUNIT: Homomultimer; only active in its oligomeric state
CC (PubMed:15509569). Interacts with nucleoprotein/N (PubMed:9880009).
CC Interacts with matrix/M protein (PubMed:17079312). Interacts with host
CC TBK1 (By similarity). Interacts with polymerase L (PubMed:10756058).
CC Interacts with host HMGB1; this interaction is required to stabilize
CC RNP on chromosomes (PubMed:22607802). {ECO:0000250|UniProtKB:P0C798,
CC ECO:0000269|PubMed:10756058, ECO:0000269|PubMed:15509569,
CC ECO:0000269|PubMed:17079312, ECO:0000269|PubMed:22607802,
CC ECO:0000269|PubMed:9880009}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:10756058,
CC ECO:0000269|PubMed:12829848, ECO:0000269|PubMed:16414989,
CC ECO:0000269|PubMed:25810554, ECO:0000269|PubMed:9811710}. Host
CC cytoplasm {ECO:0000269|PubMed:12829848, ECO:0000269|PubMed:16414989}.
CC Note=P subcellular localization is modulated by the interaction with
CC protein X. {ECO:0000269|PubMed:12829848}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=p24;
CC IsoId=P0C799-1; Sequence=Displayed;
CC Name=p16;
CC IsoId=P0C799-2; Sequence=VSP_040674;
CC -!- PTM: Phosphorylated by host PKC epsilon and casein kinase II.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: The P/X gene has two overlapping open reading frames.
CC One encodes the P protein and the other the X protein. The P (p24), X
CC and P'(p16) proteins are produced by ribosomal leaky scanning.
CC {ECO:0000250|UniProtKB:P0C798}.
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DR EMBL; U04608; AAA20225.1; -; Genomic_RNA.
DR RefSeq; NP_042021.1; NC_001607.1.
DR SMR; P0C799; -.
DR IntAct; P0C799; 1.
DR GeneID; 26799164; -.
DR KEGG; vg:26799164; -.
DR Proteomes; UP000007804; 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:0039675; P:exit of virus from host cell nucleus through nuclear pore; IDA:UniProtKB.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039723; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity; IEA:UniProtKB-KW.
DR InterPro; IPR009517; BDV_P24.
DR Pfam; PF06595; BDV_P24; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Inhibition of host innate immune response by virus;
KW Inhibition of host RLR pathway by virus; Inhibition of host TBK1 by virus;
KW Inhibition of host TLR pathway by virus; Phosphoprotein;
KW Reference proteome; Viral immunoevasion.
FT CHAIN 1..201
FT /note="Phosphoprotein"
FT /id="PRO_0000405343"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 29..36
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000269|PubMed:9811710"
FT MOTIF 181..193
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000269|PubMed:9811710"
FT COMPBIAS 9..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform p16)"
FT /evidence="ECO:0000305"
FT /id="VSP_040674"
SQ SEQUENCE 201 AA; 22489 MW; 035002A13220D709 CRC64;
MATRPSSLVD SLEDEEDPQT LRRERPGSPR PRKVPRNALT QPVDQLLKDL RKNPSMISDP
DQRTGREQLS NDELIKKLVT ELAENSMIEA EEVRGTLGDI SARIEAGFES LSALQVETIQ
TAQRCDHSDS IRILGENIKI LDRSMKTMME TMKLMMEKVD LLYASTAVGT SAPMLPSHPA
PPRIYPQLPS APTTDEWDII P
