PHOSP_SEND6
ID PHOSP_SEND6 Reviewed; 568 AA.
AC P14251; P14255;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, 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 6/94) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11193;
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=2557577; DOI=10.1093/nar/17.23.10102;
RA Homann H.E., Neubert W.J.;
RT "Cloning and sequencing of the polymerase gene (P) of Sendai virus (strain
RT 6/94).";
RL Nucleic Acids Res. 17:10102-10102(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.
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 (By 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; X17007; CAA34867.1; -; Genomic_RNA.
DR PIR; S06923; RRNZS6.
DR BMRB; P14251; -.
DR SMR; P14251; -.
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; RNA editing;
KW Viral RNA replication.
FT CHAIN 1..568
FT /note="Phosphoprotein"
FT /id="PRO_0000142711"
FT REGION 1..22
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 40..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 COILED 364..429
FT /evidence="ECO:0000250"
FT COMPBIAS 48..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..105
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..254
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 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; 62178 MW; 7E5443D083BCE03D CRC64;
MDQDAFILKE DSEVERKAPG GRESLSDVIG FLDAVLSSEP TDIGGDRSWL HNTINTSQGP
GSAHRAKSEG EGEVSTPSTQ DNRSGEESRV SGRTSKPEAE AHAGNLDKQN IHWAFRGRTG
TNSVSQDLGD GGDSGILENP PNERGYPRSG IEDENREMAA HPDKRGEDQA EGLPEEVRGG
TSLPDEGEGG ASNNGRSMEP GSSHSARVTG VLVIPSPELE EAVLRRNKRR PTNSGSKPLT
PATVPGTRSP PLNRYNSTGP PPGKPPSTQD EHINSGDTPA VRVKDRKPPI GTRSVSDCPA
NGRPIHPGIE TDSTKKGIGE NTSSMKEMAT LLTGLGVIQS AQEFESSRDA SYVFARRALK
SANYAEMTFN VCGLILSAEK SSARKVDENK QLLKQIQENV ESFRDIYKRF SEYQKEQNSL
LMSNLSTLHI ITDRGGKTDN TDSLTRSPSV FAKSKENKTK ATRFDPSMET LEDMKYKPDL
IREDEFRDEI RNPVYQERDT EPRASNASRL FPSKEKPTMH SLRLVIESSP LSRAEKAAYV
KSLSKCKTDQ EVKAVMELVE EDIESLTN
