PHOSP_SENDF
ID PHOSP_SENDF Reviewed; 568 AA.
AC P14252;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 02-JUN-2021, entry version 105.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P/V/C;
OS Sendai virus (strain Fushimi) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11195;
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=2557576; DOI=10.1093/nar/17.23.10101;
RA Neubert W.J.;
RT "Cloning and sequencing of the polymerase gene (P) of Sendai virus (strain
RT Fushimi).";
RL Nucleic Acids Res. 17:10101-10101(1989).
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.
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; Note=Partially edited. RNA editing
CC at this position consists of an insertion of one or two guanine
CC nucleotides. The sequence displayed here is the P protein, derived from
CC the unedited RNA. The edited RNA gives rise to the V protein (+1G) (AC
CC P69284), and the W protein (+2G) (AC P69285).;
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; X17008; CAA34871.1; -; Genomic_RNA.
DR PIR; S06922; RRNZSF.
DR BMRB; P14252; -.
DR SMR; P14252; -.
DR Proteomes; UP000006825; 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:0039697; P:negative stranded viral RNA transcription; IDA:UniProtKB.
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; RNA editing;
KW Viral RNA replication.
FT CHAIN 1..568
FT /note="Phosphoprotein"
FT /id="PRO_0000142713"
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 495..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"
SQ SEQUENCE 568 AA; 62032 MW; 494A6BE4A71A7961 CRC64;
MDQDAFILKE DSEVEREAPG GRESLSDVIG FLDAVLSSEP TDIGGDRSWL HNTINTPQGP
GSAHRAKSEG EGEVSTPSTQ DNRSGEESRV SGRTSKPEAE AHAGNLDKQN IHRAFGGRTG
TNSVSQDLGD GGDSGILENP PNERGYPRSG IEDENREMAA HPDKRGEDQA EGLPEEVRGG
TSLPDEGEGG ASNNGRSMEP GSSHSARVTG VLVIPSPELE EAVLRRNKRR PTNSGSKPLT
PATVPGTRSP PLNRYNSTGS PPGKPPSTQD EHINSGDTPA VRVKDRKPPI GTRSVSDCPA
NGRPIHPGLE TDSTKKGIGE NTSSMKEMAT LLTSLGVIQS AQEFESSRDA SYVFARRALK
SANYAEMTFN VCGLILSAEK SSARKVDENK QLLKQIQESV ESFRDIYKRF SEYQKEQNSL
LMSNLSTLHI ITDRGGKTDN TDSLTRSPSV FAKSKENKTK ATRFDPSMET LEDMKYKPDL
IREDEFRDEI RNPLYQERDT EPRASNASRL LPSKEKPTMH SLRLVIESSP LSRAEKAAYV
KSLSKCKTDQ EVKAVMELVE EDIESLTN
