PHOSP_RABVE
ID PHOSP_RABVE Reviewed; 297 AA.
AC P69479; A3F5L6; P22559;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 23-FEB-2022, entry version 68.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS Rabies virus (strain ERA) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=11295;
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].
RA Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B.,
RA Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R., Peterhans E.,
RA Cox J., Mueller T.;
RT "Complete nucleotide sequencing of SAD derivatives of attenuated rabies
RT virus vaccine strains.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH NUCLEOPROTEIN.
RX PubMed=8178445; DOI=10.1006/viro.1994.1222;
RA Fu Z.F., Zheng Y., Wunner W.H., Koprowski H., Dietzschold B.;
RT "Both the N- and the C-terminal domains of the nominal phosphoprotein of
RT rabies virus are involved in binding to the nucleoprotein.";
RL Virology 200:590-597(1994).
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 (By similarity).
CC {ECO:0000250}.
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:0000250}.
CC -!- SUBUNIT: [Isoform P3]: Binds host PML. {ECO:0000250}.
CC -!- INTERACTION:
CC P69479; P61221: ABCE1; Xeno; NbExp=3; IntAct=EBI-25568013, EBI-2510446;
CC -!- SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform P3]: Host nucleus {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform P4]: Host nucleus {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=5;
CC Name=P;
CC IsoId=P69479-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=P69479-2; Sequence=VSP_026871;
CC Name=P3;
CC IsoId=P69479-3; Sequence=VSP_026870;
CC Name=P4;
CC IsoId=P69479-4; Sequence=VSP_026869;
CC Name=P5;
CC IsoId=P69479-5; Sequence=VSP_026868;
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; X55728; CAA39259.1; -; Genomic_RNA.
DR EMBL; EF206707; ABN11292.1; -; Viral_cRNA.
DR PIR; S13708; S13708.
DR SMR; P69479; -.
DR IntAct; P69479; 1465.
DR Proteomes; UP000008619; 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: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 Alternative initiation; Chaperone; Cytoplasmic inwards viral transport;
KW Host cytoplasm; Host nucleus; Host-virus interaction;
KW 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_0000222829"
FT REGION 132..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..172
FT /note="DYNLL1 and DYNLL2 binding"
FT /evidence="ECO:0000250"
FT MOTIF 49..58
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 211..214
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 152..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 162
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 210
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 271
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform P5)"
FT /evidence="ECO:0000305"
FT /id="VSP_026868"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform P4)"
FT /evidence="ECO:0000305"
FT /id="VSP_026869"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform P3)"
FT /evidence="ECO:0000305"
FT /id="VSP_026870"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026871"
SQ SEQUENCE 297 AA; 33213 MW; B69C4287A220A7E4 CRC64;
MSKIFVNPSA IRAGLADLEM AEETVDLINR NIEDNQAHLQ GEPIEVDNLP EDMGRLHLDD
GKSPNPGEMA KVGEGKYRED FQMDEGEDPS FLFQSYLENV GVQIVRQMRS GERFLKIWSQ
TVEEIISYVA VNFPNPPGKS SEDKSTQTTG RELKKETTPT PSQRESQSSK ARMAAQTASG
PPALEWSATN EKDDLSVEAE IAHQIAESFS KKYKFPSRSS GILLYNFEQL KMNLDDIVKE
AKNVPGVTRL AHDGSKLPLR CVLGWVALAN SKKFQLLVES DKLSKIMQDD LNRYTSC
