PHOSP_RABVS
ID PHOSP_RABVS Reviewed; 297 AA.
AC P16286; A3F5M1; Q6HA97;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 23-FEB-2022, entry version 99.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS Rabies virus (strain SAD B19) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=11300;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2139267; DOI=10.1016/0042-6822(90)90433-r;
RA Conzelmann K.-K., Cox J.H., Schneider L.G., Thiel H.-J.;
RT "Molecular cloning and complete nucleotide sequence of the attenuated
RT rabies virus SAD B19.";
RL Virology 175:485-499(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=SRV9;
RA Wang T., Zhang S., Hu R.;
RT "Analysis of the whole sequence of rabies virus vaccine strain SRV9.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate SAD B19, Isolate SAD Bern, Isolate SAD Bern original var 1,
RC Isolate SAD Bern original var 2, Isolate SAD Bern original var 3,
RC Isolate SAD Bern original var 4, Isolate SAD Bern original var 5,
RC Isolate SAD P5/88, Isolate SAD VA1, and Isolate SAG 2;
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 [4]
RP FUNCTION.
RX PubMed=15557246; DOI=10.1099/vir.0.80325-0;
RA Liu P., Yang J., Wu X., Fu Z.F.;
RT "Interactions amongst rabies virus nucleoprotein, phosphoprotein and
RT genomic RNA in virus-infected and transfected cells.";
RL J. Gen. Virol. 85:3725-3734(2004).
RN [5]
RP INTERACTION WITH HOST STAT1 AND STAT2.
RX PubMed=16501077; DOI=10.1128/jvi.80.6.2675-2683.2006;
RA Brzozka K., Finke S., Conzelmann K.K.;
RT "Inhibition of interferon signaling by rabies virus phosphoprotein P:
RT activation-dependent binding of STAT1 and STAT2.";
RL J. Virol. 80:2675-2683(2006).
RN [6]
RP INTERACTION WITH DYNLL1.
RX PubMed=17438267; DOI=10.1073/pnas.0701397104;
RA Tan G.S., Preuss M.A., Williams J.C., Schnell M.J.;
RT "The dynein light chain 8 binding motif of rabies virus phosphoprotein
RT promotes efficient viral transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7229-7234(2007).
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, ECO:0000269|PubMed:15557246}.
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 -!- 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 P5]: Host nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=4;
CC Name=P;
CC IsoId=P16286-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=P16286-2; Sequence=VSP_026882;
CC Name=P3;
CC IsoId=P16286-3; Sequence=VSP_026881;
CC Name=P5;
CC IsoId=P16286-4; Sequence=VSP_026880;
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; M31046; AAA47200.1; -; Genomic_RNA.
DR EMBL; AF499686; AAT48624.1; -; Genomic_RNA.
DR EMBL; EF206708; ABN11297.1; -; Genomic_RNA.
DR EMBL; EF206709; ABN11302.1; -; Genomic_RNA.
DR EMBL; EF206710; ABN11307.1; -; Genomic_RNA.
DR EMBL; EF206711; ABN11312.1; -; Genomic_RNA.
DR EMBL; EF206712; ABN11317.1; -; Genomic_RNA.
DR EMBL; EF206713; ABN11322.1; -; Genomic_RNA.
DR EMBL; EF206714; ABN11327.1; -; Genomic_RNA.
DR EMBL; EF206715; ABN11332.1; -; Genomic_RNA.
DR EMBL; EF206716; ABN11337.1; -; Genomic_RNA.
DR EMBL; EF206719; ABN11352.1; -; Genomic_RNA.
DR EMBL; EF206720; ABN11357.1; -; Genomic_RNA.
DR PIR; B34746; MNVNSB.
DR PDB; 6UEB; EM; 3.30 A; B=51-87.
DR PDBsum; 6UEB; -.
DR SMR; P16286; -.
DR Proteomes; UP000006363; Genome.
DR Proteomes; UP000007308; Genome.
DR Proteomes; UP000100286; Genome.
DR Proteomes; UP000115894; Genome.
DR Proteomes; UP000123862; Genome.
DR Proteomes; UP000132522; Genome.
DR Proteomes; UP000133682; Genome.
DR Proteomes; UP000142143; Genome.
DR Proteomes; UP000151156; Genome.
DR Proteomes; UP000167748; Genome.
DR Proteomes; UP000172072; Genome.
DR Proteomes; UP000174835; Genome.
DR Proteomes; UP000175378; 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:0039653; P:suppression by virus of host transcription; IMP:CACAO.
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; Reference proteome; Viral immunoevasion;
KW Viral RNA replication; Virion; Virus entry into host cell.
FT CHAIN 1..297
FT /note="Phosphoprotein"
FT /id="PRO_0000222832"
FT REGION 132..175
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..174
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_026880"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform P3)"
FT /evidence="ECO:0000305"
FT /id="VSP_026881"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026882"
FT VARIANT 69
FT /note="I -> M (in strain: Isolate SAD Bern, Isolate SAD
FT Bern original var 1, Isolate SAD Bern original var 2,
FT Isolate SAD Bern original var 3, Isolate SAD Bern original
FT var 4 and Isolate SAD Bern original var 5)"
FT VARIANT 77
FT /note="Y -> S (in strain: Isolate SAD Bern, Isolate SAD
FT Bern original var 1, Isolate SAD Bern original var 2,
FT Isolate SAD Bern original var 3, Isolate SAD Bern original
FT var 4 and Isolate SAD Bern original var 5)"
FT VARIANT 156
FT /note="E -> G (in strain: Isolate SAD Bern, Isolate SAD
FT Bern original var 1, Isolate SAD Bern original var 2,
FT Isolate SAD Bern original var 3, Isolate SAD Bern original
FT var 4 and Isolate SAD Bern original var 5)"
FT VARIANT 169
FT /note="S -> L (in strain: Isolate SAD Bern, Isolate SAD
FT Bern original var 1, Isolate SAD Bern original var 2,
FT Isolate SAD Bern original var 3, Isolate SAD Bern original
FT var 4 and Isolate SAD Bern original var 5)"
FT VARIANT 177
FT /note="I -> T (in strain: Isolate SAD Bern, Isolate SAD
FT Bern original var 1, Isolate SAD Bern original var 2,
FT Isolate SAD Bern original var 3, Isolate SAD Bern original
FT var 4 and Isolate SAD Bern original var 5)"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6UEB"
SQ SEQUENCE 297 AA; 33248 MW; 93310052F6C35E78 CRC64;
MSKIFVNPSA IRAGLADLEM AEETVDLINR NIEDNQAHLQ GEPIEVDNLP EDMGRLHLDD
GKSPNHGEIA KVGEGKYRED FQMDEGEDPS FLFQSYLENV GVQIVRQMRS GERFLKIWSQ
TVEEIISYVA VNFPNPPGKS SEDKSTQTTG RELKKETTPT PSQRESQSSK ARMAAQIASG
PPALEWSATN EEDDLSVEAE IAHQIAESFS KKYKFPSRSS GILLYNFEQL KMNLDDIVKE
AKNVPGVTRL AHDGSKLPLR CVLGWVALAN SKKFQLLVES DKLSKIMQDD LNRYTSC
