PHOSP_VSIVM
ID PHOSP_VSIVM Reviewed; 265 AA.
AC P04880;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS Vesicular stomatitis Indiana virus (strain Mudd-Summers) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11279;
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=3016152; DOI=10.1099/0022-1317-67-8-1571;
RA Hudson L.D., Condra C., Lazzarini R.A.;
RT "Cloning and expression of a viral phosphoprotein: structure suggests
RT vesicular stomatitis virus NS may function by mimicking an RNA template.";
RL J. Gen. Virol. 67:1571-1579(1986).
RN [2]
RP INTERACTION WITH PROTEIN L AND RIBONUCLEOCAPSID.
RX PubMed=2441389; DOI=10.1073/pnas.84.16.5655;
RA Emerson S.U., Schubert M.;
RT "Location of the binding domains for the RNA polymerase L and the
RT ribonucleocapsid template within different halves of the NS phosphoprotein
RT of vesicular stomatitis virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5655-5659(1987).
RN [3]
RP PHOSPHORYLATION AT SER-226 AND SER-227.
RX PubMed=9123826; DOI=10.1006/viro.1996.8401;
RA Chen J.L., Das T., Banerjee A.K.;
RT "Phosphorylated states of vesicular stomatitis virus P protein in vitro and
RT in vivo.";
RL Virology 228:200-212(1997).
RN [4]
RP HOMOTRIMERIZATION.
RX PubMed=8931554; DOI=10.1021/bi9613133;
RA Gao Y., Greenfield N.J., Cleverley D.Z., Lenard J.;
RT "The transcriptional form of the phosphoprotein of vesicular stomatitis
RT virus is a trimer: structure and stability.";
RL Biochemistry 35:14569-14573(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 107-177.
RX PubMed=16501089; DOI=10.1128/jvi.80.6.2808-2814.2006;
RA Ding H., Green T.J., Lu S., Luo M.;
RT "Crystal structure of the oligomerization domain of the phosphoprotein of
RT vesicular stomatitis virus.";
RL J. Virol. 80:2808-2814(2006).
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.
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; X04196; CAA27788.1; -; Genomic_RNA.
DR PIR; A29144; MNVNIM.
DR PDB; 2FQM; X-ray; 2.30 A; A/B/C/D/E/F=107-177.
DR PDB; 3HHW; X-ray; 2.70 A; A/B/C/D/E=183-265.
DR PDB; 3HHZ; X-ray; 3.50 A; A/B/C/D/E=183-265.
DR PDBsum; 2FQM; -.
DR PDBsum; 3HHW; -.
DR PDBsum; 3HHZ; -.
DR SMR; P04880; -.
DR EvolutionaryTrace; P04880; -.
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 3D-structure; Chaperone; Host cytoplasm; Phosphoprotein;
KW Viral RNA replication; Virion.
FT CHAIN 1..265
FT /note="Phosphoprotein"
FT /id="PRO_0000222837"
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"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2FQM"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:2FQM"
FT HELIX 132..151
FT /evidence="ECO:0007829|PDB:2FQM"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2FQM"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:2FQM"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:2FQM"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:3HHW"
SQ SEQUENCE 265 AA; 30035 MW; 49E9C49627191803 CRC64;
MDNLTKVREY LKSYSRLDQA VGEIDEIEAQ RAEKSNYELF QEDGVEEHTR PSYFQAADDS
DTESEPEIED NQGLYVPDPE AEQVEGFIQG PLDDYADEDV DVVFTSDWKQ PELESDEHGK
TLRLTLPEGL SGEQKSQWLL TIKAVVQSAK HWNLAECTFE ASGEGVIIKK RQITPDVYKV
TPVMNTHPYQ SEAVSDVWSL SKTSMTFQPK KASLQPLTIS LDELFSSRGE FISVGGNGRM
SHKEAILLGL RYKKLYNQAR VKYSL
