PHOSP_SENDZ
ID PHOSP_SENDZ Reviewed; 568 AA.
AC P04860; P27565;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 02-JUN-2021, entry version 95.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P/V/C;
OS Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11198;
OH NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6316257; DOI=10.1093/nar/11.21.7317;
RA Shioda T., Hidaka Y., Kanda T., Shibuta H., Nomoto A., Iwasaki K.;
RT "Sequence of 3,687 nucleotides from the 3' end of Sendai virus genome RNA
RT and the predicted amino acid sequences of viral NP, P and C proteins.";
RL Nucleic Acids Res. 11:7317-7330(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Shibuta H.;
RL Submitted (FEB-1985) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant F1-R, and Mutant ts-f1;
RX PubMed=2161155; DOI=10.1016/0042-6822(90)90040-x;
RA Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E.,
RA Klenk H.-D., Rott R., Seto J.T.;
RT "Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L
RT proteins of two host range mutants of Sendai virus.";
RL Virology 176:656-657(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant F1-R / T-5 revertant;
RX PubMed=1651590; DOI=10.1016/0042-6822(91)90839-4;
RA Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D., Rott R.,
RA Seto J.T.;
RT "Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai
RT virus.";
RL Virology 184:227-234(1991).
RN [5]
RP RNA EDITING.
RX PubMed=1655410; DOI=10.1002/j.1460-2075.1991.tb07860.x;
RA Curran J., Boeck R., Kolakofsky D.;
RT "The Sendai virus P gene expresses both an essential protein and an
RT inhibitor of RNA synthesis by shuffling modules via mRNA editing.";
RL EMBO J. 10:3079-3085(1991).
CC -!- FUNCTION: Essential component of the RNA polymerase transcription and
CC replication complex. Binds the viral ribonucleocapsid and positions the
CC polymerase on the template (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Acts as a chaperone for newly synthesized free N protein, so-
CC called N(0). Stabilizes the L protein upon binding it (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. Binds to the L protein, N(0) and to the C-
CC terminal domain of N in ribonucleocapsid (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by PKC/PRKCZ, and other unknown kinases.
CC Phosphorylation is necessary for viral transcription and replication.
CC The N-terminus contains the majority of phosphorylated sites. Ser-249
CC is the major site of phosphorylation, but is not necessary for most
CC functions (By similarity). {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=318 {ECO:0000269|PubMed:1655410};
CC Note=Partially edited. RNA editing at this position consists of an
CC insertion of one or two guanine nucleotides. The sequence displayed
CC here is the P protein, derived from the unedited RNA. The edited RNA
CC gives rise to the V protein (+1G) (AC P69282), and the W protein (+2G)
CC (AC P69283).;
CC -!- MISCELLANEOUS: The P/V/C gene has two overlapping open reading frames.
CC One encodes the P/V/W proteins and the other the C/Y proteins.
CC -!- SIMILARITY: Belongs to the respirovirus P protein 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; X00087; CAA24946.1; -; Genomic_RNA.
DR EMBL; M30202; AAB06279.1; -; Genomic_RNA.
DR EMBL; M30203; AAB06285.1; -; Genomic_RNA.
DR EMBL; M30204; AAB06197.1; -; Genomic_RNA.
DR EMBL; M69046; AAB06291.1; -; Genomic_RNA.
DR PIR; A00726; RRNZSV.
DR BMRB; P04860; -.
DR SMR; P04860; -.
DR Proteomes; UP000006560; Genome.
DR Proteomes; UP000110830; Genome.
DR Proteomes; UP000163956; Genome.
DR Proteomes; UP000169749; Genome.
DR Proteomes; UP000181310; Genome.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR Gene3D; 1.10.287.320; -; 1.
DR InterPro; IPR002693; Paramyxo_PProtein_C.
DR InterPro; IPR043097; PProtein_oligomer_dom1.
DR InterPro; IPR016075; RNA_pol_Pprot-P_XD_paramyxovir.
DR Pfam; PF01806; Paramyxo_P; 1.
DR SUPFAM; SSF101089; SSF101089; 1.
PE 3: Inferred from homology;
KW Chaperone; Coiled coil; Phosphoprotein; Reference proteome; RNA editing;
KW Viral RNA replication.
FT CHAIN 1..568
FT /note="Phosphoprotein"
FT /id="PRO_0000142716"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..41
FT /note="N(0) binding"
FT /evidence="ECO:0000250"
FT REGION 38..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..412
FT /note="Bipartite nucleocapsid binding domain 1"
FT /evidence="ECO:0000250"
FT REGION 413..445
FT /note="L protein binding"
FT /evidence="ECO:0000250"
FT REGION 479..568
FT /note="Bipartite nucleocapsid binding domain 2"
FT /evidence="ECO:0000250"
FT REGION 496..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 364..429
FT /evidence="ECO:0000250"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 125
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 249
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 257
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 260
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 447
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 449
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT VARIANT 155
FT /note="N -> S (in strain: Mutant F1-R / T-5 revertant)"
FT VARIANT 180
FT /note="S -> G (in strain: Mutant F1-R, Mutant ts-f1 and
FT Mutant F1-R / T-5 revertant)"
FT VARIANT 304
FT /note="S -> P (in strain: Mutant F1-R, Mutant ts-f1 and
FT Mutant F1-R / T-5 revertant)"
FT VARIANT 406
FT /note="T -> I (in strain: Mutant F1-R, Mutant ts-f1 and
FT Mutant F1-R / T-5 revertant)"
SQ SEQUENCE 568 AA; 62026 MW; 563A3C4CF51C91E7 CRC64;
MDQDAFILKE DSEVEREAPG GRESLSDVIG FLDAVLSSEP TDIGGDRSWL HNTINTPQGP
GSAHRAKSEG EGEVSTPSTQ DNRSGEESRV SGRTSKPEAE AHAGNLDKQN IHRAFGGRTG
TNSVSQDLGD GGDSGILENP PNERGYPRSG IEDENREMAA HPDKRGEDQA EGLPEEVRGS
TSLPDEGEGG ASNNGRSMEP GSSHSARVTG VLVIPSPELE EAVLRRNKRR PTNSGSKPLT
PATVPGTRSP PLNRYNSTGS PPGKPPSTQD EHINSGDTPA VRVKDRKPPI GTRSVSDCPA
NGRSIHPGLE TDSTKKGIGE NTSSMKEMAT LLTSLGVIQS AQEFESSRDA SYVFARRALK
SANYAEMTFN VCGLILSAEK SSARKVDENK QLLKQIQESV ESFRDTYKRF SEYQKEQNSL
LMSNLSTLHI ITDRGGKTDN TDSLTRSPSV FAKSKENKTK ATRFDPSMET LEDMKYKPDL
IREDEFRDEI RNPVYQERDT EPRASNASRL LPSKEKPTMH SLRLVIESSP LSRAEKAAYV
KSLSKCKTDQ EVKAVMELVE EDIESLTN
