PHOSP_VSNJO
ID PHOSP_VSNJO Reviewed; 274 AA.
AC P04877; Q86608;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Phosphoprotein;
DE Short=P protein;
DE AltName: Full=Protein M1;
GN Name=P;
OS Vesicular stomatitis New Jersey virus (strain Ogden subtype Concan)
OS (VSNJV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11283;
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=2989560; DOI=10.1128/jvi.55.1.60-66.1985;
RA Gill D.S., Banerjee A.K.;
RT "Vesicular stomatitis virus NS proteins: structural similarity without
RT extensive sequence homology.";
RL J. Virol. 55:60-66(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-87.
RX PubMed=8388490; DOI=10.1128/jvi.67.6.3103-3110.1993;
RA Spiropoulou C.F., Nichol S.T.;
RT "A small highly basic protein is encoded in overlapping frame within the P
RT gene of vesicular stomatitis virus.";
RL J. Virol. 67:3103-3110(1993).
RN [3]
RP PHOSPHORYLATION AT SER-59 AND SER-61.
RX PubMed=1326645; DOI=10.1128/jvi.66.10.5842-5848.1992;
RA Takacs A.M., Barik S., Das T., Banerjee A.K.;
RT "Phosphorylation of specific serine residues within the acidic domain of
RT the phosphoprotein of vesicular stomatitis virus regulates transcription in
RT vitro.";
RL J. Virol. 66:5842-5848(1992).
RN [4]
RP PHOSPHORYLATION BY HOST CK2.
RX PubMed=7844556; DOI=10.1099/0022-1317-76-2-365;
RA Gupta A.K., Das T., Banerjee A.K.;
RT "Casein kinase II is the P protein phosphorylating cellular kinase
RT associated with the ribonucleoprotein complex of purified vesicular
RT stomatitis virus.";
RL J. Gen. Virol. 76:365-372(1995).
RN [5]
RP FUNCTION.
RX PubMed=9375014; DOI=10.1006/viro.1997.8823;
RA Das T., Pattnaik A.K., Takacs A.M., Li T., Hwang L.N., Banerjee A.K.;
RT "Basic amino acid residues at the carboxy-terminal eleven amino acid region
RT of the phosphoprotein (P) are required for transcription but not for
RT replication of vesicular stomatitis virus genome RNA.";
RL Virology 238:103-114(1997).
RN [6]
RP FUNCTION.
RX PubMed=9343167; DOI=10.1128/jvi.71.11.8167-8175.1997;
RA Pattnaik A.K., Hwang L., Li T., Englund N., Mathur M., Das T.,
RA Banerjee A.K.;
RT "Phosphorylation within the amino-terminal acidic domain I of the
RT phosphoprotein of vesicular stomatitis virus is required for transcription
RT but not for replication.";
RL J. Virol. 71:8167-8175(1997).
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, ECO:0000269|PubMed:9343167,
CC ECO:0000269|PubMed:9375014}.
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; K03387; AAA48453.1; -; Genomic_RNA.
DR EMBL; S61075; AAB26735.1; -; Genomic_RNA.
DR PIR; A04115; MNVNVJ.
DR SMR; P04877; -.
DR DIP; DIP-209N; -.
DR Proteomes; UP000007626; 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 1: Evidence at protein level;
KW Chaperone; Host cytoplasm; Phosphoprotein; Viral RNA replication; Virion.
FT CHAIN 1..274
FT /note="Phosphoprotein"
FT /id="PRO_0000222835"
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 170..196
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 COMPBIAS 170..188
FT /note="Polar 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; 31406 MW; 3D3A81FD45FA5CCF CRC64;
MDSVDRLKTY LATYDNLDSA LQDANESEER REDKYLQDLF IEDQGDKPTP SYYQEEESSD
SDTDYNAEHL TMLSPDERID KWEEDLPELE KIDDDIPVTF SDWTQPVMKE NGGEKSLSLF
PPVGLTKIQT EQWKKTIEAV CESSKYWNLS ECQILNLEDS LTLKGRLMTP DCSSSVKSQN
SVRRSEPLYS SHSPGPPLKV SESINLWDLK STEVQLISKR AGVKDMTVKL TDFFGSEEEY
YSVCPEGAPD LMGAIIMGLK YKKLFNQARM KYRL
