PHOSP_RABVN
ID PHOSP_RABVN Reviewed; 297 AA.
AC Q9IPJ8; O55595; Q75T11;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS Rabies virus (strain Nishigahara RCEH) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=11298;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Nishigahara, and RC-HL;
RX PubMed=11270607; DOI=10.1111/j.1348-0421.2001.tb01274.x;
RA Ito N., Kakemizu M., Ito K.A., Yamamoto A., Yoshida Y., Sugiyama M.,
RA Minamoto N.;
RT "A comparison of complete genome sequences of the attenuated RC-HL strain
RT of rabies virus used for production of animal vaccine in Japan, and the
RT parental Nishigahara strain.";
RL Microbiol. Immunol. 45:51-58(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Ni-CE;
RX PubMed=17010466; DOI=10.1016/j.virusres.2006.08.011;
RA Shimizu K., Ito N., Mita T., Yamada K., Hosokawa-Muto J., Sugiyama M.,
RA Minamoto N.;
RT "Involvement of nucleoprotein, phosphoprotein, and matrix protein genes of
RT rabies virus in virulence for adult mice.";
RL Virus Res. 123:154-160(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}.
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 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=Q9IPJ8-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=Q9IPJ8-2; Sequence=VSP_026916;
CC Name=P3;
CC IsoId=Q9IPJ8-3; Sequence=VSP_026915;
CC Name=P4;
CC IsoId=Q9IPJ8-4; Sequence=VSP_026914;
CC Name=P5;
CC IsoId=Q9IPJ8-5; Sequence=VSP_026913;
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; AB044824; BAA96803.1; -; Genomic_RNA.
DR EMBL; AB009663; BAA24084.1; -; Genomic_RNA.
DR EMBL; AB128149; BAD04911.1; -; Genomic_RNA.
DR PIR; B58460; B58460.
DR PDB; 7C20; X-ray; 3.00 A; A=186-297.
DR PDBsum; 7C20; -.
DR SMR; Q9IPJ8; -.
DR Proteomes; UP000006366; Genome.
DR Proteomes; UP000007309; Genome.
DR Proteomes; UP000007310; 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 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_0000295254"
FT REGION 57..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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_026913"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform P4)"
FT /evidence="ECO:0000305"
FT /id="VSP_026914"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform P3)"
FT /evidence="ECO:0000305"
FT /id="VSP_026915"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026916"
FT VARIANT 15
FT /note="L -> M (in strain: RC-HL)"
FT VARIANT 56..58
FT /note="LHL -> PHP (in strain: Ni-CE)"
FT VARIANT 56
FT /note="L -> I (in strain: RC-HL)"
FT VARIANT 60
FT /note="D -> Y (in strain: RC-HL)"
FT VARIANT 66
FT /note="L -> P (in strain: Ni-CE)"
FT VARIANT 81
FT /note="F -> P (in strain: Ni-CE)"
FT VARIANT 100
FT /note="V -> I (in strain: RC-HL)"
FT VARIANT 148
FT /note="T -> I (in strain: RC-HL)"
FT VARIANT 165
FT /note="K -> A (in strain: RC-HL)"
FT VARIANT 226
FT /note="N -> H (in strain: Ni-CE)"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:7C20"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:7C20"
FT STRAND 213..225
FT /evidence="ECO:0007829|PDB:7C20"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:7C20"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:7C20"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:7C20"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:7C20"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:7C20"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:7C20"
SQ SEQUENCE 297 AA; 33326 MW; 70F7184CC1B9C99C CRC64;
MSKIFVNPSA IRAGLADLEM AEETVDLINR NIEDNQAHLQ GEPIEVDSLP EDMSRLHLDD
GKLPDLGRMS KAGEGRHQED FQMDEGEDPS LLFQSYLDNV GVQIVRQMRS GERFLKIWSQ
TVEEIISYVT VNFPNPSGRS SEDKSTQTTS QEPKKETTST PSQRKSQSLK SRTMAQTASG
PPSLEWSATN EEDDLSVEAE IAHQIAESFS KKYKFPSRSS GIFLYNFEQL KMNLDDIVKE
AKNVPGVTRL AHDGSKLPLR CVLGWVALAN SKKFQLLVEA NKLNKIMQDD LNRYASC
