PHOSP_SENDH
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 02-JUN-2021, entry version 113.
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; Orthoparamyxovirinae;
OC Respirovirus.
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 N(0).
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 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 320-433.
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 [14]
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 component of the RNA polymerase transcription and
CC replication complex. Binds the viral ribonucleocapsid and positions the
CC L polymerase on the template.
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.
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. {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}.
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DR PIR; A28985; RRNZHS.
DR PDB; 1EZJ; X-ray; 1.90 A; A=320-433.
DR PDB; 1R4G; NMR; -; A=516-568.
DR PDBsum; 1EZJ; -.
DR PDBsum; 1R4G; -.
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 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0039689; P:negative stranded viral RNA replication; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR DisProt; DP00939; -.
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 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="N(0) binding"
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 REGION 413..445
FT /note="L protein binding"
FT REGION 479..568
FT /note="Bipartite nucleocapsid binding domain 2"
FT REGION 496..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 364..429
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: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 N(0) binding."
FT /evidence="ECO:0000269|PubMed:11739672"
FT MUTAGEN 487..489
FT /note="RDE->AAA: Complete loss of N(0) 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 N(0) binding."
FT /evidence="ECO:0000269|PubMed:11739672"
FT MUTAGEN 533..536
FT /note="RAEK->AAAA: 50% loss of transcription. Completely
FT abolishes N(0) 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 N(0) 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
