PHOSP_SENDO
ID PHOSP_SENDO Reviewed; 568 AA.
AC O57285;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 02-JUN-2021, entry version 91.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P/V/C;
OS Sendai virus (strain Ohita) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=302272;
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=9400971; DOI=10.1099/0022-1317-78-12-3207;
RA Itoh M., Isegawa Y., Hotta H., Homma M.;
RT "Isolation of an avirulent mutant of Sendai virus with two amino acid
RT mutations from a highly virulent field strain through adaptation to LLC-MK2
RT cells.";
RL J. Gen. Virol. 78:3207-3215(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 (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 -!- SUBCELLULAR LOCATION: Host cytoplasm.
CC -!- DOMAIN: The L protein binding domain is necessary for viral RNA
CC synthesis, whereas the N(0) binding domain is not. Two separate regions
CC are required for binding to the nucleocapsid (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:0000250}; Note=Partially
CC edited. RNA editing at this position consists of an insertion of one or
CC two guanine nucleotides. The sequence displayed here is the P protein,
CC derived from the unedited RNA. The edited RNA gives rise to the V
CC protein (+1G) (AC P69287), and the W protein (+2G) (AC P69288) (By
CC similarity). {ECO:0000250};
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}.
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DR EMBL; AB005796; BAA24395.1; -; Genomic_RNA.
DR EMBL; AB005795; BAA24386.1; -; Genomic_RNA.
DR RefSeq; NP_056873.1; NC_001552.1.
DR SMR; O57285; -.
DR GeneID; 1489780; -.
DR KEGG; vg:1489780; -.
DR Proteomes; UP000006563; Genome.
DR Proteomes; UP000007311; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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; Host cytoplasm; Phosphoprotein; Reference proteome;
KW RNA editing; Viral RNA replication.
FT CHAIN 1..568
FT /note="Phosphoprotein"
FT /id="PRO_0000142715"
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 54..317
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 433..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..568
FT /note="Bipartite nucleocapsid binding domain 2"
FT /evidence="ECO:0000250"
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 72..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 568 AA; 62651 MW; BCBCDB09722DB9BF CRC64;
MDQDALISKE DSEVEREASG GRESLSDVIG FLDAVLSSEP TDIGGDRSWL HNTINTLQRP
GSTHRVKGEG EGEVSTSSTQ DNRSGEESRV SGGTSEPEAE AHARNVDKQN IHWATGRGAS
TDSVPQDLGN GRDSGILEDP PNEGGYPRSG AEDENREMAA NPDKRGEDQA EGLPEEIRRS
APLPDEREGR ADNNGRGVEP GSPHSARVTG VLVIPSPELE EAVLQRNKRR PANSGSRSLT
PVVVPSTRSP PPDHDNSTRS PPRKPPTTQD EHTNPRNTPA VRIKDRRPPT GTRSAPDRPT
DGYPTHPSPE TDATKKGIEE NTSSMKEMAT LLTSLGVIQS AQEFESSRDA SYVFAKRALK
SANYAEMAFN VCGLILSAEK SFANRVDENK QLLKQIQESV ESFRDIYKRF SEYQKEQNSL
LMSNLSTLHI ITDRGGKTDN PDSPTRSPSV FAKTKENKTK ATRFDPSMET MGDMRYKPDL
LREDEFREEI RNPVYQERDT EPRASNASRL LPSREKPTIH SLKLVIESSP LSRAEKAAYV
KSLSKCKTDQ EVKAVMELVE EDIESLTN
