ID   PHOSP_CHAV              Reviewed;         293 AA.
AC   P16380; Q5IX71; Q5IX73; Q5IX75; Q5IX77; Q5IX79; Q5IX81; Q5IX83; Q5IX85;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   29-SEP-2021, entry version 77.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
DE   AltName: Full=Protein M1;
GN   Name=P;
OS   Chandipura virus (strain I653514) (CHPV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Vesiculovirus.
OX   NCBI_TaxID=11273;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=7198; Phlebotominae (sandflies).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3029973; DOI=10.1016/0042-6822(87)90272-8;
RA   Masters P.S., Banerjee A.K.;
RT   "Sequences of Chandipura virus N and NS genes: evidence for high mutability
RT   of the NS gene within vesiculoviruses.";
RL   Virology 157:298-306(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate CIN0309R, Isolate CIN0318R, Isolate CIN0327M,
RC   Isolate CIN0327R, Isolate CIN0331M, Isolate CIN0360R, and Isolate CIN0360V;
RX   PubMed=15705335; DOI=10.3201/eid1101.040602;
RA   Arankalle V.A., Prabhakar S.S., Madhukar W.A., Hanumaih X.,
RA   Dattatraya P.S., Akhilesh Chandra M.;
RT   "G, N, and P gene-based analysis of Chandipura viruses, India.";
RL   Emerg. Infect. Dis. 11:123-126(2005).
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   -!- PTM: Phosphorylated by host kinases. Phosphorylation play an important
CC       role in facilitating trimerization and possibly P-L complex formation
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the vesiculovirus protein P family.
CC       {ECO:0000305}.
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DR   EMBL; M16608; AAA48451.1; -; Genomic_RNA.
DR   EMBL; AY614724; AAU81941.1; -; Genomic_RNA.
DR   EMBL; AY614725; AAU81943.1; -; Genomic_RNA.
DR   EMBL; AY614726; AAU81945.1; -; Genomic_RNA.
DR   EMBL; AY614727; AAU81947.1; -; Genomic_RNA.
DR   EMBL; AY614728; AAU81949.1; -; Genomic_RNA.
DR   EMBL; AY614729; AAU81951.1; -; Genomic_RNA.
DR   EMBL; AY614730; AAU81953.1; -; Genomic_RNA.
DR   EMBL; AY614731; AAU81955.1; -; Genomic_RNA.
DR   PIR; B44502; B44502.
DR   Proteomes; UP000008448; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.10.8.440; -; 1.
DR   InterPro; IPR043036; Phosphoprotein_C_viral.
PE   3: Inferred from homology;
KW   Chaperone; Host cytoplasm; Phosphoprotein; Reference proteome;
KW   Viral RNA replication; Virion.
FT   CHAIN           1..293
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000222825"
FT   REGION          22..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..71
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         250
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
FT   VARIANT         64
FT                   /note="E -> D (in strain: Isolate CIN0309R, Isolate
FT                   CIN0318R, Isolate CIN0327M, Isolate CIN0327R, Isolate
FT                   CIN0331M, Isolate CIN0360R and Isolate CIN0360V)"
FT   VARIANT         103
FT                   /note="Q -> R (in strain: Isolate CIN0309R)"
FT   VARIANT         112
FT                   /note="G -> E (in strain: Isolate CIN0309R, Isolate
FT                   CIN0327M, Isolate CIN0327R and Isolate CIN0331M)"
FT   VARIANT         180
FT                   /note="I -> V (in strain: Isolate CIN0360R and Isolate
FT                   CIN0360V)"
FT   VARIANT         214
FT                   /note="A -> V (in strain: Isolate CIN0309R, Isolate
FT                   CIN0318R, Isolate CIN0327M, Isolate CIN0331M and Isolate
FT                   CIN0360V)"
FT   VARIANT         258
FT                   /note="N -> T (in strain: Isolate CIN0327M)"
FT   VARIANT         270
FT                   /note="I -> V (in strain: Isolate CIN0309R, Isolate
FT                   CIN0318R and Isolate CIN0331M)"
SQ   SEQUENCE   293 AA;  32523 MW;  8CB7D36EBA67A26C CRC64;
     MEDSQLYQAL KNYPKLQDTL DSIENLEDDT KSEPSECGSP TERGIPSYYL AEELDECEEE
     DSEEDDDNLP TEIPDPPTVD MLEAIMEDEI DDTAYQVHFE AKQTWKPVIE TGGNERGKFT
     LSVPQNLSAL QLLQWETGIH ALAERLGGCR LLQISTRGTR DGIEFTVRET PCVSPASDPI
     PSTSRSSSIA SNVSTRQTES PGSKSNTSLG IPEAPANLID MGAIDKEFIL AAISPSDPPY
     KNTLRNLFGS GDSFEQYNQT GIYSLKELVI AGLKRKGIYN RIRIRCHLEP QFN