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Phosphoprotein (Protein P)

 PHOSP_SENDH             Reviewed;         568 AA.
P04859;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
10-MAY-2017, entry version 101.
RecName: Full=Phosphoprotein;
Short=Protein P;
Name=P/V/C;
Sendai virus (strain Harris) (SeV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Respirovirus.
NCBI_TaxID=11196;
NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
NCBI_TaxID=36483; Cricetidae sp. (Hamster).
NCBI_TaxID=10090; Mus musculus (Mouse).
NCBI_TaxID=10116; Rattus norvegicus (Rat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6317203; DOI=10.1016/0092-8674(83)90115-0;
Giorgi C., Blumberg B.M., Kolakofsky D.;
"Sendai virus contains overlapping genes expressed from a single
mRNA.";
Cell 35:829-836(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Kolakofsky D.;
Submitted (JAN-2005) to UniProtKB.
[3]
INTERACTION WITH THE NUCLEOCAPSID.
PubMed=2154886; DOI=10.1016/0042-6822(90)90105-Z;
Ryan K.W., Portner A.;
"Separate domains of Sendai virus P protein are required for binding
to viral nucleocapsids.";
Virology 174:515-521(1990).
[4]
INTERACTION WITH L PROTEIN.
PubMed=8030249; DOI=10.1006/viro.1994.1409;
Curran J., Pelet T., Kolakofsky D.;
"An acidic activation-like domain of the Sendai virus P protein is
required for RNA SYnthesis and encapsidation.";
Virology 202:875-884(1994).
[5]
INTERACTION WITH NUCLEOPROTEIN N(0).
PubMed=7815552;
Curran J., Marq J.-B., Kolakofsky D.;
"An N-terminal domain of the Sendai paramyxovirus P protein acts as a
chaperone for the NP protein during the nascent chain assembly step of
genome replication.";
J. Virol. 69:849-855(1995).
[6]
PHOSPHORYLATION AT SER-249.
PubMed=8614993; DOI=10.1006/viro.1996.0052;
Byrappa S., Pan Y.-B., Gupta K.C.;
"Sendai virus P protein is constitutively phosphorylated at serine249:
high phosphorylation potential of the P protein.";
Virology 216:228-234(1996).
[7]
RNA EDITING.
PubMed=9034340; DOI=10.1093/emboj/16.3.578;
Kato A., Kiyotani K., Sakai Y., Yoshida T., Nagai Y.;
"The paramyxovirus, Sendai virus, V protein encodes a luxury function
required for viral pathogenesis.";
EMBO J. 16:578-587(1997).
[8]
PHOSPHORYLATION BY PKC ZETA.
PubMed=9195969; DOI=10.1074/jbc.272.26.16578;
Huntley C.C., De B.P., Banerjee A.K.;
"Phosphorylation of Sendai virus phosphoprotein by cellular protein
kinase C zeta.";
J. Biol. Chem. 272:16578-16584(1997).
[9]
PHOSPHORYLATION AT SER-249, AND MUTAGENESIS OF SER-249 AND PRO-250.
PubMed=10544094; DOI=10.1006/viro.1999.9953;
Hu C.-J., Kato A., Bowman M.C., Kiyotani K., Yoshida T., Moyer S.A.,
Nagai Y., Gupta K.C.;
"Role of primary constitutive phosphorylation of Sendai virus P and V
proteins in viral replication and pathogenesis.";
Virology 263:195-208(1999).
[10]
MUTAGENESIS OF 408-LYS-ARG-409; 412-GLU--GLU-416; SER-419; LEU-421;
LEU-425; SER-426; LEU-428; ILE-430; 433-ASP--LYS-437; GLY-436;
LYS-453; 455-LYS-GLU-456; 460-LYS--ASP-465 AND 469-GLU--ASP-473.
PubMed=10400742;
Bowman M.C., Smallwood S., Moyer S.A.;
"Dissection of individual functions of the Sendai virus phosphoprotein
in transcription.";
J. Virol. 73:6474-6483(1999).
[11]
PHOSPHORYLATION AT SER-68; SER-125; SER-192; SER-257; SER-260; SER-447
AND SER-449, AND MUTAGENESIS OF SER-68; SER-125; SER-192; SER-257;
SER-260; SER-447 AND SER-449.
PubMed=10704359; DOI=10.1006/viro.1999.0176;
Hu C.-J., Gupta K.C.;
"Functional significance of alternate phosphorylation in Sendai virus
P protein.";
Virology 268:517-532(2000).
[12]
MUTAGENESIS OF 482-ARG--GLU-485; 487-ARG--GLU-489; 497-GLU--ASP-499;
506-ASN-ARG-509; 514-LYS--LYS-516; 524-LEU--ILE-526; 533-ARG--LYS-536;
549-ASP--LYS-533 AND 560-GLU--ASP-562.
PubMed=11739672; DOI=10.1128/JVI.76.1.68-77.2002;
Tuckis J., Smallwood S., Feller J.A., Moyer S.A.;
"The C-terminal 88 amino acids of the Sendai virus P protein have
multiple functions separable by mutation.";
J. Virol. 76:68-77(2002).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 320-433.
PubMed=10966649; DOI=10.1038/79013;
Tarbouriech N., Curran J., Ruigrok R.W.H., Burmeister W.P.;
"Tetrameric coiled coil domain of Sendai virus phosphoprotein.";
Nat. Struct. Biol. 7:777-781(2000).
[14]
STRUCTURE BY NMR OF 516-568.
PubMed=14980481; DOI=10.1016/j.virol.2003.10.029;
Blanchard L., Tarbouriech N., Blackledge M., Timmins P.,
Burmeister W.P., Ruigrok R.W.H., Marion D.;
"Structure and dynamics of the nucleocapsid-binding domain of the
Sendai virus phosphoprotein in solution.";
Virology 319:201-211(2004).
-!- FUNCTION: Essential component of the RNA polymerase transcription
and replication complex. Binds the viral ribonucleocapsid and
positions the L polymerase on the template.
-!- FUNCTION: Acts as a chaperone for newly synthesized free N
protein, so-called N(0). Stabilizes the L protein upon binding it.
-!- SUBUNIT: Homotetramer. Binds to the L protein, N(0) and to the C-
terminal domain of N in ribonucleocapsid.
-!- SUBCELLULAR LOCATION: Host cytoplasm.
-!- DOMAIN: The L protein binding domain is necessary for viral RNA
synthesis, whereas the N(0) binding domain is not. Two separate
regions are required for binding to the nucleocapsid.
-!- PTM: Phosphorylated by PKC/PRKCZ, and other unknown kinases.
Phosphorylation is necessary for viral transcription and
replication. The N-terminus contains the majority of
phosphorylated sites. Ser-249 is the major site of
phosphorylation, but is not necessary for most functions.
{ECO:0000269|PubMed:10544094, ECO:0000269|PubMed:10704359,
ECO:0000269|PubMed:8614993, ECO:0000269|PubMed:9195969}.
-!- RNA EDITING: Modified_positions=318 {ECO:0000269|PubMed:9034340};
Note=Partially edited. RNA editing at this position consists of an
insertion of one or two guanine nucleotides. The sequence
displayed here is the P protein, derived from the unedited RNA.
The edited RNA gives rise to the V protein (+1G) (AC P69280), and
the W protein (+2G) (AC P69281).;
-!- MISCELLANEOUS: The P/V/C gene has two overlapping open reading
frames. One encodes the P/V/W proteins and the other the C/Y
proteins.
-!- SIMILARITY: Belongs to the respirovirus P protein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
PIR; A28985; RRNZHS.
PDB; 1EZJ; X-ray; 1.90 A; A=320-433.
PDB; 1R4G; NMR; -; A=516-568.
PDBsum; 1EZJ; -.
PDBsum; 1R4G; -.
DisProt; DP00939; -.
ProteinModelPortal; P04859; -.
SMR; P04859; -.
iPTMnet; P04859; -.
EvolutionaryTrace; P04859; -.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
GO; GO:0039689; P:negative stranded viral RNA replication; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
InterPro; IPR002693; Paramyxo_PProtein_C.
InterPro; IPR016075; RNA_pol_Pprot-P_XD_paramyxovir.
Pfam; PF01806; Paramyxo_P; 1.
SUPFAM; SSF101089; SSF101089; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Coiled coil; Host cytoplasm; Phosphoprotein;
RNA editing; Viral RNA replication.
CHAIN 1 568 Phosphoprotein.
/FTId=PRO_0000142714.
REGION 33 41 N(0) binding.
REGION 345 412 Bipartite nucleocapsid binding domain 1.
REGION 413 445 L protein binding.
REGION 479 568 Bipartite nucleocapsid binding domain 2.
COILED 364 429
MOD_RES 68 68 Phosphoserine; by host.
{ECO:0000269|PubMed:10704359}.
MOD_RES 125 125 Phosphoserine; by host.
{ECO:0000269|PubMed:10704359}.
MOD_RES 192 192 Phosphoserine; by host.
{ECO:0000269|PubMed:10704359}.
MOD_RES 249 249 Phosphoserine; by host.
{ECO:0000269|PubMed:10544094,
ECO:0000269|PubMed:8614993}.
MOD_RES 257 257 Phosphoserine; by host.
{ECO:0000269|PubMed:10704359}.
MOD_RES 260 260 Phosphoserine; by host.
{ECO:0000269|PubMed:10704359}.
MOD_RES 447 447 Phosphoserine; by host.
{ECO:0000269|PubMed:10704359}.
MOD_RES 449 449 Phosphoserine; by host.
{ECO:0000269|PubMed:10704359}.
VARIANT 311 311 S -> T.
MUTAGEN 68 68 S->A: Complete loss of phosphorylation.
{ECO:0000269|PubMed:10704359}.
MUTAGEN 125 125 S->A: Complete loss of phosphorylation.
{ECO:0000269|PubMed:10704359}.
MUTAGEN 192 192 S->A: Complete loss of phosphorylation.
{ECO:0000269|PubMed:10704359}.
MUTAGEN 249 249 S->A: No effect.
{ECO:0000269|PubMed:10544094}.
MUTAGEN 249 249 S->D: No effect.
{ECO:0000269|PubMed:10544094}.
MUTAGEN 250 250 P->A: Prevents S-249 phosphorylation. No
effect on P protein functions.
{ECO:0000269|PubMed:10544094}.
MUTAGEN 257 257 S->A: Complete loss of phosphorylation.
{ECO:0000269|PubMed:10704359}.
MUTAGEN 260 260 S->A: Complete loss of phosphorylation.
{ECO:0000269|PubMed:10704359}.
MUTAGEN 408 409 KR->AA: 80% loss of in vitro
transcription.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 412 416 EYQKE->AYQAA: 60% loss of in vitro
transcription.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 419 419 S->A: No effect.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 421 421 L->A: 80% loss of in vitro transcription.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 425 425 L->A: 80% loss of in vitro transcription.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 426 426 S->A: No effect.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 428 428 L->A: 60% loss of in vitro transcription.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 430 430 I->A: No effect.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 433 437 DRGGK->AAGGA: 80% loss of in vitro
transcription.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 436 436 G->A: No effect.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 447 447 S->A: Complete loss of phosphorylation.
{ECO:0000269|PubMed:10704359}.
MUTAGEN 449 449 S->A: Complete loss of phosphorylation.
{ECO:0000269|PubMed:10704359}.
MUTAGEN 453 453 K->A: 60% loss of in vitro transcription.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 455 456 KE->AA: 40% loss of in vitro
transcription.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 460 465 KATRFD->AATAFA: 80% loss of in vitro
transcription.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 469 473 ETLED->ATLAA: 60% loss of in vitro
transcription.
{ECO:0000269|PubMed:10400742}.
MUTAGEN 482 485 REDE->AAAA: Complete loss of in vitro
replication and N(0) binding.
{ECO:0000269|PubMed:11739672}.
MUTAGEN 487 489 RDE->AAA: Complete loss of N(0) binding.
{ECO:0000269|PubMed:11739672}.
MUTAGEN 497 499 ERD->AAA: No effect.
{ECO:0000269|PubMed:11739672}.
MUTAGEN 506 509 NASR->AASA: Complete loss of
transcription and replication.
{ECO:0000269|PubMed:11739672}.
MUTAGEN 514 516 KEK->AAA: 56% loss of transcription.
{ECO:0000269|PubMed:11739672}.
MUTAGEN 524 526 LVI->AAA: Complete loss of transcription,
replication and N(0) binding.
{ECO:0000269|PubMed:11739672}.
MUTAGEN 533 536 RAEK->AAAA: 50% loss of transcription.
Completely abolishes N(0) binding.
{ECO:0000269|PubMed:11739672}.
MUTAGEN 549 553 DQEVK->AQAVA: 50% loss of transcription.
MUTAGEN 560 562 EED->AAA: Complete loss of transcription,
in vitro replication and N(0) binding.
{ECO:0000269|PubMed:11739672}.
HELIX 322 334 {ECO:0000244|PDB:1EZJ}.
STRAND 337 339 {ECO:0000244|PDB:1EZJ}.
HELIX 341 344 {ECO:0000244|PDB:1EZJ}.
HELIX 350 359 {ECO:0000244|PDB:1EZJ}.
HELIX 364 424 {ECO:0000244|PDB:1EZJ}.
HELIX 425 428 {ECO:0000244|PDB:1EZJ}.
HELIX 519 526 {ECO:0000244|PDB:1R4G}.
HELIX 534 544 {ECO:0000244|PDB:1R4G}.
HELIX 550 566 {ECO:0000244|PDB:1R4G}.
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


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