ID   PHOSP_VSNJM             Reviewed;         274 AA.
AC   P04878; Q86133;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   29-SEP-2021, entry version 89.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
DE   AltName: Full=Protein M1;
GN   Name=P;
OS   Vesicular stomatitis New Jersey virus (strain Missouri subtype Hazelhurst)
OS   (VSNJV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Vesiculovirus.
OX   NCBI_TaxID=11282;
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=58271; Culicoides.
OH   NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=252607; Lutzomyia.
OH   NCBI_TaxID=7370; Musca domestica (House fly).
OH   NCBI_TaxID=7190; Simuliidae (black flies).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3014048; DOI=10.1099/0022-1317-67-7-1351;
RA   Rae B.P., Elliott R.M.;
RT   "Conservation of potential phosphorylation sites in the NS proteins of the
RT   New Jersey and Indiana serotypes of vesicular stomatitis virus.";
RL   J. Gen. Virol. 67:1351-1360(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3025344; DOI=10.1099/0022-1317-67-12-2635;
RA   Rae B.P., Elliott R.M.;
RT   "Characterization of the mutations responsible for the electrophoretic
RT   mobility differences in the NS proteins of vesicular stomatitis virus New
RT   Jersey complementation group E mutants.";
RL   J. Gen. Virol. 67:2635-2643(1986).
RN   [3]
RP   ERRATUM OF PUBMED:3025344.
RA   Rae B.P., Elliott R.M.;
RL   J. Gen. Virol. 68:1499-1499(1987).
CC   -!- FUNCTION: Essential component of the RNA polymerase transcription and
CC       replication complex. Binds the viral ribonucleocapsid and positions the
CC       L polymerase on the template. May act as a chaperone for newly
CC       synthesized free N protein, so-called N(0). Plays a role in virion
CC       assembly (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer when phosphorylated in domain I. This trimer is
CC       stabilized by binding to the L protein. Binds N(0), and N in
CC       ribonucleocapsid (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Sequences comparison studies have defined several domains.
CC       Domain I binds the protein L, contains phosphorylation sites required
CC       for trimerization and is involved in transcription. Hinge region is
CC       highly variable and may act as a spacer between domain I and II. Domain
CC       II is also phosphorylated, binds protein L, and plays a role in
CC       replication. Domain III is basic and essential for binding the N-RNA
CC       template (By similarity). {ECO:0000250}.
CC   -!- PTM: Domain I is phosphorylated by host CK2. Domain II is
CC       phosphorylated by other unknown kinases. Phosphorylation play an
CC       important role in facilitating trimerization and possibly P-L complex
CC       formation (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the vesiculovirus protein P family.
CC       {ECO:0000305}.
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DR   EMBL; X04063; CAA27695.1; -; mRNA.
DR   EMBL; X04718; CAB37190.1; -; mRNA.
DR   PIR; A29143; MNVNVM.
DR   SMR; P04878; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   Gene3D; 1.10.8.440; -; 1.
DR   InterPro; IPR043036; Phosphoprotein_C_viral.
DR   InterPro; IPR037263; Phosphoprotein_central.
DR   SUPFAM; SSF160892; SSF160892; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Host cytoplasm; Phosphoprotein; Viral RNA replication; Virion.
FT   CHAIN           1..274
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000222836"
FT   REGION          1..132
FT                   /note="Domain I"
FT                   /evidence="ECO:0000250"
FT   REGION          22..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..219
FT                   /note="Hinge"
FT                   /evidence="ECO:0000250"
FT   REGION          174..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..253
FT                   /note="Domain II"
FT                   /evidence="ECO:0000250"
FT   REGION          254..274
FT                   /note="Domain III:"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        23..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         59
FT                   /note="Phosphoserine; by host CK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         61
FT                   /note="Phosphoserine; by host CK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         236
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   274 AA;  31300 MW;  59D74F80E9AE6989 CRC64;
     MDSIDRLKTY LATYDNLDSA LQDANESEER REDKYLQDLF IEDQGDKPTP SYYQEEESSD
     SDTDYNAEHL TMLSPDERID KWEEDLPELE KIDDDIPVTF SDWTQPVMKE NGGEKSLSLF
     PPVGLTKVQT DQWRKTIEAV CESSKYWNLS ECQIMNSEDR LILKGRIMTP DCSSSIKSQN
     SIQSSESLSS SHSPGPAPKS RNQLGLWDSK STEVQLISKR AGVKDMMVKL TDFFGSEEEY
     YSVCPEGAPD LMGAIIMGLK HKKLFNQARM KYRI