PHOSP_RABVC
ID PHOSP_RABVC Reviewed; 297 AA.
AC P22363; Q85414;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 23-FEB-2022, entry version 105.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS Rabies virus (strain CVS-11) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=11294;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2148206; DOI=10.1093/nar/18.23.7172;
RA Larson J.K., Wunner W.H.;
RT "Nucleotide and deduced amino acid sequences of the nominal nonstructural
RT phosphoprotein of the ERA, PM and CVS-11 strains of rabies virus.";
RL Nucleic Acids Res. 18:7172-7172(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=CVS;
RA Mannen K., Takita Y., Hiramatsu K., Mifune K.;
RT "Nucleotide sequence of the NS gene of rabies virus CVS strain.";
RL Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH PROTEIN L.
RX PubMed=9499045; DOI=10.1128/jvi.72.3.1925-1930.1998;
RA Chenik M., Schnell M., Conzelmann K.K., Blondel D.;
RT "Mapping the interacting domains between the rabies virus polymerase and
RT phosphoprotein.";
RL J. Virol. 72:1925-1930(1998).
RN [4]
RP INTERACTION WITH HOST STAT1.
RX PubMed=16254375; DOI=10.1128/jvi.79.22.14411-14420.2005;
RA Vidy A., Chelbi-Alix M., Blondel D.;
RT "Rabies virus P protein interacts with STAT1 and inhibits interferon signal
RT transduction pathways.";
RL J. Virol. 79:14411-14420(2005).
RN [5]
RP ALTERNATIVE INITIATION.
RX PubMed=7815533; DOI=10.1128/jvi.69.2.707-712.1995;
RA Chenik M., Chebli K., Blondel D.;
RT "Translation initiation at alternate in-frame AUG codons in the rabies
RT virus phosphoprotein mRNA is mediated by a ribosomal leaky scanning
RT mechanism.";
RL J. Virol. 69:707-712(1995).
RN [6]
RP PHOSPHORYLATION AT SER-63; SER-64; SER-162; SER-210 AND SER-271.
RX PubMed=10590095; DOI=10.1128/jvi.74.1.91-98.2000;
RA Gupta A.K., Blondel D., Choudhary S., Banerjee A.K.;
RT "The phosphoprotein of rabies virus is phosphorylated by a unique cellular
RT protein kinase and specific isomers of protein kinase C.";
RL J. Virol. 74:91-98(2000).
RN [7]
RP INTERACTION WITH RAT DYNLL1 AND DYNLL2.
RX PubMed=11024151; DOI=10.1128/jvi.74.21.10212-10216.2000;
RA Raux H., Flamand A., Blondel D.;
RT "Interaction of the rabies virus P protein with the LC8 dynein light
RT chain.";
RL J. Virol. 74:10212-10216(2000).
RN [8]
RP INTERACTION WITH RAT DYNLL1 AND DYNLL2.
RX PubMed=11602781; DOI=10.1099/0022-1317-82-11-2691;
RA Poisson N., Real E., Gaudin Y., Vaney M.C., King S., Jacob Y., Tordo N.,
RA Blondel D.;
RT "Molecular basis for the interaction between rabies virus phosphoprotein P
RT and the dynein light chain LC8: dissociation of dynein-binding properties
RT and transcriptional functionality of P.";
RL J. Gen. Virol. 82:2691-2696(2001).
RN [9]
RP INTERACTION WITH HAMSTER PML.
RX PubMed=12439746; DOI=10.1038/sj.onc.1205931;
RA Blondel D., Regad T., Poisson N., Pavie B., Harper F., Pandolfi P.P.,
RA De The H., Chelbi-Alix M.K.;
RT "Rabies virus P and small P products interact directly with PML and
RT reorganize PML nuclear bodies.";
RL Oncogene 21:7957-7970(2002).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=15780878; DOI=10.1016/j.virol.2005.02.005;
RA Pasdeloup D., Poisson N., Raux H., Gaudin Y., Ruigrok R.W., Blondel D.;
RT "Nucleocytoplasmic shuttling of the rabies virus P protein requires a
RT nuclear localization signal and a CRM1-dependent nuclear export signal.";
RL Virology 334:284-293(2005).
RN [11]
RP INTERFERON ANTIVIRAL SYSTEM EVASION.
RX PubMed=17287281; DOI=10.1128/jvi.01930-06;
RA Vidy A., El Bougrini J., Chelbi-Alix M.K., Blondel D.;
RT "The nucleocytoplasmic rabies virus P protein counteracts interferon
RT signaling by inhibiting both nuclear accumulation and DNA binding of
RT STAT1.";
RL J. Virol. 81:4255-4263(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 186-297.
RX PubMed=15476803; DOI=10.1016/j.jmb.2004.08.071;
RA Mavrakis M., McCarthy A.A., Roche S., Blondel D., Ruigrok R.W.;
RT "Structure and function of the C-terminal domain of the polymerase cofactor
RT of rabies virus.";
RL J. Mol. Biol. 343:819-831(2004).
CC -!- FUNCTION: Non catalytic polymerase cofactor and regulatory protein that
CC plays a role in viral transcription and replication. Stabilizes the RNA
CC polymerase L to the N-RNA template and binds the soluble protein N,
CC preventing it from encapsidating non-genomic RNA. Also inhibits host
CC IFN-alpha and IFN-beta signaling by binding and retaining
CC phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding
CC of STAT1 in the nucleus. Might be involved, through interaction with
CC host dynein, in intracellular microtubule-dependent virus transport of
CC incoming virus from the synapse toward the cell body.
CC -!- SUBUNIT: [Phosphoprotein]: Homotrimer when phosphorylated. This trimer
CC is stabilized by binding to the L protein. Binds soluble protein N, and
CC ribonucleocapsid. Interacts with host DYNLL1 and DYNLL2; this
CC interaction may play a role in intracellular microtubule-dependent
CC virus transport of incoming virus. Interacts with host STAT1, STAT2 and
CC PML. {ECO:0000269|PubMed:11024151, ECO:0000269|PubMed:11602781,
CC ECO:0000269|PubMed:16254375, ECO:0000269|PubMed:9499045}.
CC -!- SUBUNIT: [Isoform P3]: Binds host PML. {ECO:0000269|PubMed:12439746}.
CC -!- SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform P3]: Host nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform P4]: Host nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=5;
CC Name=P;
CC IsoId=P22363-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=P22363-2; Sequence=VSP_026786;
CC Name=P3;
CC IsoId=P22363-3; Sequence=VSP_026785;
CC Name=P4;
CC IsoId=P22363-4; Sequence=VSP_026784;
CC Name=P5;
CC IsoId=P22363-5; Sequence=VSP_026783;
CC -!- PTM: Phosphorylated by host PKC and by an unknown kinase.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lyssavirus protein P family. {ECO:0000305}.
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DR EMBL; X55727; CAA39258.1; -; Genomic_RNA.
DR EMBL; X57783; CAA40929.1; -; Genomic_RNA.
DR PIR; S13706; S13706.
DR PDB; 1VYI; X-ray; 1.50 A; A=186-297.
DR PDBsum; 1VYI; -.
DR SMR; P22363; -.
DR ELM; P22363; -.
DR iPTMnet; P22363; -.
DR EvolutionaryTrace; P22363; -.
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:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019083; P:viral transcription; IEA:InterPro.
DR Gene3D; 1.20.120.820; -; 1.
DR InterPro; IPR004259; PP_M1.
DR InterPro; IPR037199; PP_M1_C.
DR Pfam; PF03012; PP_M1; 1.
DR SUPFAM; SSF118173; SSF118173; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Chaperone;
KW Cytoplasmic inwards viral transport; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host STAT1 by virus; Inhibition of host STAT2 by virus;
KW Interferon antiviral system evasion; Microtubular inwards viral transport;
KW Phosphoprotein; Viral immunoevasion; Viral RNA replication; Virion;
KW Virus entry into host cell.
FT CHAIN 1..297
FT /note="Phosphoprotein"
FT /id="PRO_0000222828"
FT REGION 132..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..172
FT /note="DYNLL1 and DYNLL2 binding"
FT MOTIF 49..58
FT /note="Nuclear export signal"
FT MOTIF 211..214
FT /note="Nuclear localization signal"
FT COMPBIAS 152..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:10590095"
FT MOD_RES 64
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:10590095"
FT MOD_RES 162
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000269|PubMed:10590095"
FT MOD_RES 210
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000269|PubMed:10590095"
FT MOD_RES 271
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000269|PubMed:10590095"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform P5)"
FT /evidence="ECO:0000305"
FT /id="VSP_026783"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform P4)"
FT /evidence="ECO:0000305"
FT /id="VSP_026784"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform P3)"
FT /evidence="ECO:0000305"
FT /id="VSP_026785"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026786"
FT VARIANT 122
FT /note="V -> I (in strain: CVS)"
FT HELIX 190..207
FT /evidence="ECO:0007829|PDB:1VYI"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1VYI"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1VYI"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1VYI"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:1VYI"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:1VYI"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:1VYI"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:1VYI"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:1VYI"
FT HELIX 280..292
FT /evidence="ECO:0007829|PDB:1VYI"
SQ SEQUENCE 297 AA; 33616 MW; E93EDE6BFFA4AAB6 CRC64;
MSKIFVNPSA IRAGLADLEM AEETVDLINR NIEDNQAHLQ GEPIEVDNLP EDMKRLHLDD
EKSSNLGEMV RVGEGKYRED FQMDEGEDPN LLFQSYLDNV GVQIVRQMRS GERFLKIWSQ
TVEEIVSYVT VNFPNPPRRS SEDKSTQTTG RELKKETTSA FSQRESQPSK ARMVAQVAPG
PPALEWSATN EEDDLSVEAE IAHQIAESFS KKYKFPSRSS GIFLYNFEQL KMNLDDIVKE
AKNVPGVTRL AHDGSKIPLR CVLGWVALAN SKKFQLLVEA DKLSKIMQDD LNRYTSC
