ID PHOSP_SENDH Reviewed; 568 AA. AC P04859; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 18-JUN-2025, entry version 123. DE RecName: Full=Phosphoprotein; DE Short=Protein P; GN Name=P/V/C; OS Sendai virus (strain Harris) (SeV). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Feraresvirinae; OC Respirovirus; Respirovirus muris. OX NCBI_TaxID=11196; 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=6317203; DOI=10.1016/0092-8674(83)90115-0; RA Giorgi C., Blumberg B.M., Kolakofsky D.; RT "Sendai virus contains overlapping genes expressed from a single mRNA."; RL Cell 35:829-836(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA Kolakofsky D.; RL Submitted (JAN-2005) to UniProtKB. RN [3] RP INTERACTION WITH THE NUCLEOCAPSID. RX PubMed=2154886; DOI=10.1016/0042-6822(90)90105-z; RA Ryan K.W., Portner A.; RT "Separate domains of Sendai virus P protein are required for binding to RT viral nucleocapsids."; RL Virology 174:515-521(1990). RN [4] RP INTERACTION WITH L PROTEIN. RX PubMed=8030249; DOI=10.1006/viro.1994.1409; RA Curran J., Pelet T., Kolakofsky D.; RT "An acidic activation-like domain of the Sendai virus P protein is required RT for RNA SYnthesis and encapsidation."; RL Virology 202:875-884(1994). RN [5] RP INTERACTION WITH NUCLEOPROTEIN N0. RX PubMed=7815552; DOI=10.1128/jvi.69.2.849-855.1995; RA Curran J., Marq J.-B., Kolakofsky D.; RT "An N-terminal domain of the Sendai paramyxovirus P protein acts as a RT chaperone for the NP protein during the nascent chain assembly step of RT genome replication."; RL J. Virol. 69:849-855(1995). RN [6] RP DOMAIN. RX PubMed=8525609; DOI=10.1006/viro.1995.9946; RA Curran J., Boeck R., Lin-Marq N., Lupas A., Kolakofsky D.; RT "Paramyxovirus phosphoproteins form homotrimers as determined by an epitope RT dilution assay, via predicted coiled coils."; RL Virology 214:139-149(1995). RN [7] RP PHOSPHORYLATION AT SER-249. RX PubMed=8614993; DOI=10.1006/viro.1996.0052; RA Byrappa S., Pan Y.-B., Gupta K.C.; RT "Sendai virus P protein is constitutively phosphorylated at serine249: high RT phosphorylation potential of the P protein."; RL Virology 216:228-234(1996). RN [8] RP RNA EDITING. RX PubMed=9034340; DOI=10.1093/emboj/16.3.578; RA Kato A., Kiyotani K., Sakai Y., Yoshida T., Nagai Y.; RT "The paramyxovirus, Sendai virus, V protein encodes a luxury function RT required for viral pathogenesis."; RL EMBO J. 16:578-587(1997). RN [9] RP PHOSPHORYLATION BY PKC ZETA. RX PubMed=9195969; DOI=10.1074/jbc.272.26.16578; RA Huntley C.C., De B.P., Banerjee A.K.; RT "Phosphorylation of Sendai virus phosphoprotein by cellular protein kinase RT C zeta."; RL J. Biol. Chem. 272:16578-16584(1997). RN [10] RP PHOSPHORYLATION AT SER-249, AND MUTAGENESIS OF SER-249 AND PRO-250. RX PubMed=10544094; DOI=10.1006/viro.1999.9953; RA Hu C.-J., Kato A., Bowman M.C., Kiyotani K., Yoshida T., Moyer S.A., RA Nagai Y., Gupta K.C.; RT "Role of primary constitutive phosphorylation of Sendai virus P and V RT proteins in viral replication and pathogenesis."; RL Virology 263:195-208(1999). RN [11] RP MUTAGENESIS OF 408-LYS-ARG-409; 412-GLU--GLU-416; SER-419; LEU-421; RP LEU-425; SER-426; LEU-428; ILE-430; 433-ASP--LYS-437; GLY-436; LYS-453; RP 455-LYS-GLU-456; 460-LYS--ASP-465 AND 469-GLU--ASP-473. RX PubMed=10400742; DOI=10.1128/jvi.73.8.6474-6483.1999; RA Bowman M.C., Smallwood S., Moyer S.A.; RT "Dissection of individual functions of the Sendai virus phosphoprotein in RT transcription."; RL J. Virol. 73:6474-6483(1999). RN [12] RP PHOSPHORYLATION AT SER-68; SER-125; SER-192; SER-257; SER-260; SER-447 AND RP SER-449, AND MUTAGENESIS OF SER-68; SER-125; SER-192; SER-257; SER-260; RP SER-447 AND SER-449. RX PubMed=10704359; DOI=10.1006/viro.1999.0176; RA Hu C.-J., Gupta K.C.; RT "Functional significance of alternate phosphorylation in Sendai virus P RT protein."; RL Virology 268:517-532(2000). RN [13] RP MUTAGENESIS OF 482-ARG--GLU-485; 487-ARG--GLU-489; 497-GLU--ASP-499; RP 506-ASN-ARG-509; 514-LYS--LYS-516; 524-LEU--ILE-526; 533-ARG--LYS-536; RP 549-ASP--LYS-533 AND 560-GLU--ASP-562. RX PubMed=11739672; DOI=10.1128/jvi.76.1.68-77.2002; RA Tuckis J., Smallwood S., Feller J.A., Moyer S.A.; RT "The C-terminal 88 amino acids of the Sendai virus P protein have multiple RT functions separable by mutation."; RL J. Virol. 76:68-77(2002). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 320-433, SUBUNIT, COILED COIL, RP DOMAIN, AND INTERACTION WITH POLYMERASE L. RX PubMed=10966649; DOI=10.1038/79013; RA Tarbouriech N., Curran J., Ruigrok R.W.H., Burmeister W.P.; RT "Tetrameric coiled coil domain of Sendai virus phosphoprotein."; RL Nat. Struct. Biol. 7:777-781(2000). RN [15] RP STRUCTURE BY NMR OF 516-568. RX PubMed=14980481; DOI=10.1016/j.virol.2003.10.029; RA Blanchard L., Tarbouriech N., Blackledge M., Timmins P., Burmeister W.P., RA Ruigrok R.W.H., Marion D.; RT "Structure and dynamics of the nucleocapsid-binding domain of the Sendai RT virus phosphoprotein in solution."; RL Virology 319:201-211(2004). CC -!- FUNCTION: Essential cofactor of the RNA polymerase L that plays a CC central role in the transcription and replication by forming the CC polymerase complex with RNA polymerase L and recruiting L to the CC genomic N-RNA template for RNA synthesis. Also plays a central role in CC the encapsidation of nascent RNA chains by forming the encapsidation CC complex with the nucleocapsid protein N (N-P complex). Acts as a CC chaperone for newly synthesized free N protein, so-called N0, allowing CC encapsidation of nascent RNA chains during replication (By similarity). CC The nucleoprotein protein N prevents excessive phosphorylation of P, CC which leads to down-regulation of viral transcription/ replication. CC Participates, together with N, in the formation of viral factories CC (viroplasms), which are large inclusions in the host cytoplasm where CC replication takes place (By similarity). Recruits host PI4KB and CC remodel the host endoplasmic reticulum membrane to form viral CC replication factories (By similarity). {ECO:0000250|UniProtKB:P06162, CC ECO:0000250|UniProtKB:Q77M42}. CC -!- SUBUNIT: Homotetramer (PubMed:10966649). Interacts (via multimerization CC domain) with polymerase L; this interaction forms the polymerase CC complex (PubMed:10966649, PubMed:8030249). Interacts (via N-terminus) CC with N0; this interaction allows P to chaperon N0 before encapsidation CC and form the N-P complex (Probable). Interacts (via C-terminus) with N- CC RNA template; this interaction positions the polymerase on the template CC (Probable). {ECO:0000269|PubMed:10966649, ECO:0000269|PubMed:8030249, CC ECO:0000305|PubMed:2154886, ECO:0000305|PubMed:7815552}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm. CC -!- DOMAIN: The N-terminus consists of a long intrinsically disordered tail CC (By similarity). The central part contains the coiled-coil CC multimerization domain (PMD) (PubMed:10966649). Forms a four-stranded CC coiled coil structure (PubMed:10966649). The C-terminus constitutes the CC alpha-helical domain that binds to the nucleocapsid (N-RNA complex) CC (PubMed:10966649, PubMed:11739672). {ECO:0000250|UniProtKB:P06162, CC ECO:0000269|PubMed:10966649, ECO:0000269|PubMed:11739672}. 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. {ECO:0000269|PubMed:10544094, ECO:0000269|PubMed:10704359, CC ECO:0000269|PubMed:8614993, ECO:0000269|PubMed:9195969}. CC -!- RNA EDITING: Modified_positions=318 {ECO:0000269|PubMed:9034340}; 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 P69280), and the W protein (+2G) CC (AC P69281).; 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 PIR; A28985; RRNZHS. DR PDB; 1EZJ; X-ray; 1.90 A; A=320-433. DR PDB; 1R4G; NMR; -; A=516-568. DR BMRB; P04859; -. DR SMR; P04859; -. DR iPTMnet; P04859; -. DR EvolutionaryTrace; P04859; -. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA. DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:InterPro. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0039689; P:negative stranded viral RNA replication; IDA:UniProtKB. DR CDD; cd21031; MEV_P-protein-C_like; 1. DR DisProt; DP00939; -. DR Gene3D; 1.10.287.340; -; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 1.10.287.320; Viral phosphoprotein oligmorisation site domain; 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; SSF58034; Multimerization domain of the phosphoprotein from sendai virus; 1. DR SUPFAM; SSF101089; Phosphoprotein XD domain; 1. DR PDBsum; 1EZJ; -. DR PDBsum; 1R4G; -. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Coiled coil; Host cytoplasm; Phosphoprotein; KW RNA editing; Viral RNA replication. FT CHAIN 1..568 FT /note="Phosphoprotein" FT /id="PRO_0000142714" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 33..41 FT /note="N0 binding" FT /evidence="ECO:0000269|PubMed:10966649, FT ECO:0000269|PubMed:7815552" FT REGION 38..320 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 344..411 FT /note="Multimerization" FT /evidence="ECO:0000250|UniProtKB:P06162" FT REGION 412..445 FT /note="L protein binding" FT /evidence="ECO:0000269|PubMed:10966649, FT ECO:0000269|PubMed:8525609" FT REGION 479..568 FT /note="Interaction with the nucleocapsid (N-RNA)" FT /evidence="ECO:0000269|PubMed:8525609" FT REGION 496..516 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 547..566 FT /note="Formation of N-RNA complex involved in transcription FT and replication" FT /evidence="ECO:0000250|UniProtKB:P06162" FT COILED 364..429 FT /evidence="ECO:0000269|PubMed:10966649" FT COMPBIAS 7..20 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 50..59 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 83..101 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 150..168 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 191..206 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 68 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000269|PubMed:10704359" FT MOD_RES 125 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000269|PubMed:10704359" FT MOD_RES 192 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000269|PubMed:10704359" FT MOD_RES 249 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000269|PubMed:10544094, FT ECO:0000269|PubMed:8614993" FT MOD_RES 257 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000269|PubMed:10704359" FT MOD_RES 260 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000269|PubMed:10704359" FT MOD_RES 447 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000269|PubMed:10704359" FT MOD_RES 449 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000269|PubMed:10704359" FT VARIANT 311 FT /note="S -> T" FT MUTAGEN 68 FT /note="S->A: Complete loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:10704359" FT MUTAGEN 125 FT /note="S->A: Complete loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:10704359" FT MUTAGEN 192 FT /note="S->A: Complete loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:10704359" FT MUTAGEN 249 FT /note="S->A: No effect." FT /evidence="ECO:0000269|PubMed:10544094" FT MUTAGEN 249 FT /note="S->D: No effect." FT /evidence="ECO:0000269|PubMed:10544094" FT MUTAGEN 250 FT /note="P->A: Prevents S-249 phosphorylation. No effect on P FT protein functions." FT /evidence="ECO:0000269|PubMed:10544094" FT MUTAGEN 257 FT /note="S->A: Complete loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:10704359" FT MUTAGEN 260 FT /note="S->A: Complete loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:10704359" FT MUTAGEN 408..409 FT /note="KR->AA: 80% loss of in vitro transcription." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 412..416 FT /note="EYQKE->AYQAA: 60% loss of in vitro transcription." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 419 FT /note="S->A: No effect." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 421 FT /note="L->A: 80% loss of in vitro transcription." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 425 FT /note="L->A: 80% loss of in vitro transcription." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 426 FT /note="S->A: No effect." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 428 FT /note="L->A: 60% loss of in vitro transcription." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 430 FT /note="I->A: No effect." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 433..437 FT /note="DRGGK->AAGGA: 80% loss of in vitro transcription." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 436 FT /note="G->A: No effect." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 447 FT /note="S->A: Complete loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:10704359" FT MUTAGEN 449 FT /note="S->A: Complete loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:10704359" FT MUTAGEN 453 FT /note="K->A: 60% loss of in vitro transcription." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 455..456 FT /note="KE->AA: 40% loss of in vitro transcription." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 460..465 FT /note="KATRFD->AATAFA: 80% loss of in vitro transcription." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 469..473 FT /note="ETLED->ATLAA: 60% loss of in vitro transcription." FT /evidence="ECO:0000269|PubMed:10400742" FT MUTAGEN 482..485 FT /note="REDE->AAAA: Complete loss of in vitro replication FT and N0 binding." FT /evidence="ECO:0000269|PubMed:11739672" FT MUTAGEN 487..489 FT /note="RDE->AAA: Complete loss of N0 binding." FT /evidence="ECO:0000269|PubMed:11739672" FT MUTAGEN 497..499 FT /note="ERD->AAA: No effect." FT /evidence="ECO:0000269|PubMed:11739672" FT MUTAGEN 506..509 FT /note="NASR->AASA: Complete loss of transcription and FT replication." FT /evidence="ECO:0000269|PubMed:11739672" FT MUTAGEN 514..516 FT /note="KEK->AAA: 56% loss of transcription." FT /evidence="ECO:0000269|PubMed:11739672" FT MUTAGEN 524..526 FT /note="LVI->AAA: Complete loss of transcription, FT replication and N0 binding." FT /evidence="ECO:0000269|PubMed:11739672" FT MUTAGEN 533..536 FT /note="RAEK->AAAA: 50% loss of transcription. Completely FT abolishes N0 binding." FT /evidence="ECO:0000269|PubMed:11739672" FT MUTAGEN 549..553 FT /note="DQEVK->AQAVA: 50% loss of transcription." FT MUTAGEN 560..562 FT /note="EED->AAA: Complete loss of transcription, in vitro FT replication and N0 binding." FT /evidence="ECO:0000269|PubMed:11739672" FT HELIX 322..334 FT /evidence="ECO:0007829|PDB:1EZJ" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:1EZJ" FT HELIX 341..344 FT /evidence="ECO:0007829|PDB:1EZJ" FT HELIX 350..359 FT /evidence="ECO:0007829|PDB:1EZJ" FT HELIX 364..424 FT /evidence="ECO:0007829|PDB:1EZJ" FT HELIX 425..428 FT /evidence="ECO:0007829|PDB:1EZJ" FT HELIX 519..526 FT /evidence="ECO:0007829|PDB:1R4G" FT HELIX 534..544 FT /evidence="ECO:0007829|PDB:1R4G" FT HELIX 550..566 FT /evidence="ECO:0007829|PDB:1R4G" SQ SEQUENCE 568 AA; 62004 MW; 494B675A55045C93 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 SDSTKKGIGE NTSSMKEMAT LLTSLGVIQS AQEFESSRDA SYVFARRALK SANYAEMTFN VCGLILSAEK SSARKVDENK QLLKQIQESV ESFRDIYKRF SEYQKEQNSL LMSNLSTLHI ITDRGGKTDN TDSLTRSPSV FAKSKENKTK ATRFDPSMET LEDMKYKPDL IREDEFRDEI RNPVYQERDT EPRASNASRL LPSKEKPTMH SLRLVIESSP LSRAEKAAYV KSLSKCKTDQ EVKAVMELVE EDIESLTN //