PHOSP_VSIVA
ID PHOSP_VSIVA Reviewed; 265 AA.
AC P03520;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 29-SEP-2021, entry version 110.
DE RecName: Full=Phosphoprotein;
DE Short=P protein;
DE AltName: Full=Protein M1;
GN Name=P;
OS Vesicular stomatitis Indiana virus (strain San Juan) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11285;
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=6268841; DOI=10.1128/jvi.39.2.529-535.1981;
RA Gallione C.J., Greene J.R., Iverson L.E., Rose J.K.;
RT "Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus
RT N and NS proteins.";
RL J. Virol. 39:529-535(1981).
RN [2]
RP INTERACTION WITH N.
RX PubMed=3016338; DOI=10.1128/jvi.59.3.751-754.1986;
RA Davis N.L., Arnheiter H., Wertz G.W.;
RT "Vesicular stomatitis virus N and NS proteins form multiple complexes.";
RL J. Virol. 59:751-754(1986).
RN [3]
RP FUNCTION, AND INTERACTION WITH N AND L.
RX PubMed=2845648; DOI=10.1016/0042-6822(88)90505-3;
RA Paul P.R., Chattopadhyay D., Banerjee A.K.;
RT "The functional domains of the phosphoprotein (NS) of vesicular stomatitis
RT virus (Indiana serotype).";
RL Virology 166:350-357(1988).
RN [4]
RP PHOSPHORYLATION AT SER-60; THR-62 AND SER-64.
RX PubMed=8525614; DOI=10.1006/viro.1995.9941;
RA Jackson R.L., Spadafora D., Perrault J.;
RT "Hierarchal constitutive phosphorylation of the vesicular stomatitis virus
RT P protein and lack of effect on P1 to P2 conversion.";
RL Virology 214:189-197(1995).
RN [5]
RP FUNCTION.
RX PubMed=8676480; DOI=10.1128/jvi.70.7.4538-4548.1996;
RA Spadafora D., Canter D.M., Jackson R.L., Perrault J.;
RT "Constitutive phosphorylation of the vesicular stomatitis virus P protein
RT modulates polymerase complex formation but is not essential for
RT transcription or replication.";
RL J. Virol. 70:4538-4548(1996).
RN [6]
RP FUNCTION.
RX PubMed=15163735; DOI=10.1128/jvi.78.12.6420-6430.2004;
RA Das S.C., Pattnaik A.K.;
RT "Phosphorylation of vesicular stomatitis virus phosphoprotein P is
RT indispensable for virus growth.";
RL J. Virol. 78:6420-6430(2004).
RN [7]
RP FUNCTION.
RX PubMed=15956555; DOI=10.1128/jvi.79.13.8101-8112.2005;
RA Das S.C., Pattnaik A.K.;
RT "Role of the hypervariable hinge region of phosphoprotein P of vesicular
RT stomatitis virus in viral RNA synthesis and assembly of infectious virus
RT particles.";
RL J. Virol. 79:8101-8112(2005).
RN [8]
RP INTERACTION WITH N.
RX PubMed=21207454; DOI=10.1002/pro.587;
RA Leyrat C., Jensen M.R., Ribeiro E.A. Jr., Gerard F.C., Ruigrok R.W.,
RA Blackledge M., Jamin M.;
RT "The N(0)-binding region of the vesicular stomatitis virus phosphoprotein
RT is globally disordered but contains transient alpha-helices.";
RL Protein Sci. 20:542-556(2011).
RN [9]
RP PHOSPHORYLATION AT TYR-14.
RX PubMed=24257610; DOI=10.1128/jvi.02384-13;
RA Mondal A., Victor K.G., Pudupakam R.S., Lyons C.E., Wertz G.W.;
RT "Newly identified phosphorylation site in the vesicular stomatitis virus P
RT protein is required for viral RNA synthesis.";
RL J. Virol. 88:1461-1472(2014).
RN [10]
RP STRUCTURE BY NMR OF 195-265.
RX PubMed=18657547; DOI=10.1016/j.jmb.2008.07.028;
RA Ribeiro E.A. Jr., Favier A., Gerard F.C., Leyrat C., Brutscher B.,
RA Blondel D., Ruigrok R.W., Blackledge M., Jamin M.;
RT "Solution structure of the C-terminal nucleoprotein-RNA binding domain of
RT the vesicular stomatitis virus phosphoprotein.";
RL J. Mol. Biol. 382:525-538(2008).
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. {ECO:0000269|PubMed:15163735, ECO:0000269|PubMed:15956555,
CC ECO:0000269|PubMed:2845648, ECO:0000269|PubMed:8676480}.
CC -!- SUBUNIT: Homotrimer when phosphorylated in domain I. This trimer is
CC stabilized by binding to the L protein (PubMed:2845648). Binds N(0),
CC and N in ribonucleocapsid (PubMed:2845648).
CC {ECO:0000269|PubMed:21207454, ECO:0000269|PubMed:2845648}.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm.
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.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02428; AAA48368.1; -; Genomic_RNA.
DR RefSeq; NP_041713.1; NC_001560.1.
DR PDB; 2K47; NMR; -; A=195-265.
DR PDB; 6U1X; EM; 3.00 A; P=1-265.
DR PDBsum; 2K47; -.
DR PDBsum; 6U1X; -.
DR SMR; P03520; -.
DR IntAct; P03520; 1.
DR iPTMnet; P03520; -.
DR DNASU; 1489832; -.
DR GeneID; 1489832; -.
DR KEGG; vg:1489832; -.
DR EvolutionaryTrace; P03520; -.
DR Proteomes; UP000002327; 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 GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR GO; GO:0019079; P:viral genome replication; IDA:UniProtKB.
DR GO; GO:0019083; P:viral transcription; IDA:UniProtKB.
DR DisProt; DP01391; -.
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 Reference proteome; Viral RNA replication; Viral transcription; Virion.
FT CHAIN 1..265
FT /note="Phosphoprotein"
FT /id="PRO_0000222838"
FT REGION 1..137
FT /note="Domain I"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000269|PubMed:21207454"
FT REGION 150..210
FT /note="Hinge"
FT REGION 211..244
FT /note="Domain II"
FT REGION 245..265
FT /note="Domain III:"
FT COMPBIAS 35..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000269|PubMed:24257610"
FT MOD_RES 60
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000269|PubMed:8525614"
FT MOD_RES 62
FT /note="Phosphothreonine; by host CK2"
FT /evidence="ECO:0000269|PubMed:8525614"
FT MOD_RES 64
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000269|PubMed:8525614"
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 97..99
FT /evidence="ECO:0007829|PDB:6U1X"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:2K47"
FT STRAND 204..214
FT /evidence="ECO:0007829|PDB:2K47"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:2K47"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:2K47"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:2K47"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:2K47"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:2K47"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2K47"
SQ SEQUENCE 265 AA; 29911 MW; 5AC51A1F0273EBDA CRC64;
MDNLTKVREY LKSYSRLDQA VGEIDEIEAQ RAEKSNYELF QEDGVEEHTK PSYFQAADDS
DTESEPEIED NQGLYAQDPE AEQVEGFIQG PLDDYADEEV DVVFTSDWKP PELESDEHGK
TLRLTSPEGL SGEQKSQWLS TIKAVVQSAK YWNLAECTFE ASGEGVIMKE RQITPDVYKV
TPVMNTHPSQ SEAVSDVWSL SKTSMTFQPK KASLQPLTIS LDELFSSRGE FISVGGDGRM
SHKEAILLGL RYKKLYNQAR VKYSL
