ID   PHOSP_VSIVG             Reviewed;         265 AA.
AC   P04879;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
DE   AltName: Full=Protein M1;
GN   Name=P;
OS   Vesicular stomatitis Indiana virus (strain Glasgow) (VSIV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Vesiculovirus.
OX   NCBI_TaxID=11278;
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 [GENOMIC RNA].
RX   PubMed=3005478; DOI=10.1099/0022-1317-67-3-441;
RA   Vandepol S.B., Holland J.J.;
RT   "Evolution of vesicular stomatitis virus in athymic nude mice: mutations
RT   associated with natural killer cell selection.";
RL   J. Gen. Virol. 67:441-451(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3027375; DOI=10.1128/jvi.61.2.454-464.1987;
RA   Depolo N.J., Giachetti C., Holland J.J.;
RT   "Continuing coevolution of virus and defective interfering particles and of
RT   viral genome sequences during undiluted passages: virus mutants exhibiting
RT   nearly complete resistance to formerly dominant defective interfering
RT   particles.";
RL   J. Virol. 61:454-464(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; X04453; CAA28052.1; -; Genomic_RNA.
DR   EMBL; M15121; AAA48375.1; -; Genomic_RNA.
DR   PIR; A26794; MNVNV4.
DR   SMR; P04879; -.
DR   Proteomes; UP000007544; Genome.
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   3: Inferred from homology;
KW   Chaperone; Host cytoplasm; Phosphoprotein; Reference proteome;
KW   Viral RNA replication; Virion.
FT   CHAIN           1..265
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000222834"
FT   REGION          1..137
FT                   /note="Domain I"
FT                   /evidence="ECO:0000250"
FT   REGION          42..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..210
FT                   /note="Hinge"
FT                   /evidence="ECO:0000250"
FT   REGION          211..244
FT                   /note="Domain II"
FT                   /evidence="ECO:0000250"
FT   REGION          245..265
FT                   /note="Domain III:"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         60
FT                   /note="Phosphoserine; by host CK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         62
FT                   /note="Phosphothreonine; by host CK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         64
FT                   /note="Phosphoserine; by host CK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         226
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         227
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   265 AA;  29905 MW;  CFAA5CB1AABF6279 CRC64;
     MDNLTKVREY LKSYSRLDQA VGEIDEIEAQ RAEKSNYELF QEDGVEEHTR PSYFQAADDS
     DTESEPEIED NQGLYVPDPE AEQVEGFIQG PLDDYADDDV DVVFTSDWKQ PELESDEHGK
     TLRLTLPEGL SGEQKSQWLS TIKAVVQSAK HWNLAECTFE ASGEGVIIKK RQITPDVYKV
     TPVMNTHPSQ SEAVSDVWSL SKTSMTFQPK KASLQPLTVS LDELFSSRGE FISVGGNGRM
     SHKEAILLGL RYKKLYNQAR VKYSL