Reviewed, UniProtKB/Swiss-Prot P04859 (PHOSP_SENDH)

Names and origin

Protein names

Recommended name:
    Phosphoprotein
      Short name=Protein P

Gene names

Name:

P/V/C

Organism

Sendai virus (strain Harris) (SeV)

Taxonomic identifier

11196 [NCBI]

Taxonomic lineage

Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Respirovirus

Virus host

Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]
Cavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]

Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. Acts as a chaperone for newly synthesized free N protein, so-called N0. Stabilizes the L protein upon binding it.
Subunit structure	Homotetramer. Binds to the L protein, N0 and to the C-terminal domain of N in ribonucleocapsid. Ref.3 Ref.4 Ref.5
Subcellular location	Host cytoplasm.
Domain	The L protein binding domain is necessary for viral RNA synthesis, whereas the N0 binding domain is not. Two separate regions are required for binding to the nucleocapsid.
Post-translational modification	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. Ref.6 Ref.8 Ref.9 Ref.11
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.
Sequence similarities	Belongs to the respirovirus P protein family.
RNA editing	Edited at position 318. 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). Ref.7

Ontologies

Keywords
Biological process	RNA replication
Cellular component	Host cytoplasm
Coding sequence diversity	RNA editing
Domain	Coiled coil
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	transcription, RNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 568

568

Phosphoprotein

PRO_0000142714

Regions

Region

33 – 41

9

N(0) binding

Region

345 – 412

68

Bipartite nucleocapsid binding domain 1

Region

413 – 445

33

L protein binding

Region

479 – 568

90

Bipartite nucleocapsid binding domain 2

Coiled coil

364 – 429

66

Amino acid modifications

Modified residue

68

1

Phosphoserine; by host Ref.11

Modified residue

125

1

Phosphoserine; by host Ref.11

Modified residue

192

1

Phosphoserine; by host Ref.11

Modified residue

249

1

Phosphoserine; by host Ref.6 Ref.9

Modified residue

257

1

Phosphoserine; by host Ref.11

Modified residue

260

1

Phosphoserine; by host Ref.11

Modified residue

447

1

Phosphoserine; by host Ref.11

Modified residue

449

1

Phosphoserine; by host Ref.11

Natural variations

Natural variant

311

1

S → T

Experimental info

Mutagenesis

68

1

S → A: Complete loss of phosphorylation. Ref.11

Mutagenesis

125

1

S → A: Complete loss of phosphorylation. Ref.11

Mutagenesis

192

1

S → A: Complete loss of phosphorylation. Ref.11

Mutagenesis

249

1

S → A: No effect. Ref.9

Mutagenesis

249

1

S → D: No effect. Ref.9

Mutagenesis

250

1

P → A: Prevents S-249 phosphorylation. No effect on P protein functions. Ref.9

Mutagenesis

257

1

S → A: Complete loss of phosphorylation. Ref.11

Mutagenesis

260

1

S → A: Complete loss of phosphorylation. Ref.11

Mutagenesis

408 – 409

2

KR → AA: 80% loss of in vitro transcription.

Mutagenesis

412 – 416

5

EYQKE → AYQAA: 60% loss of in vitro transcription.

Mutagenesis

419

1

S → A: No effect. Ref.10

Mutagenesis

421

1

L → A: 80% loss of in vitro transcription. Ref.10

Mutagenesis

425

1

L → A: 80% loss of in vitro transcription. Ref.10

Mutagenesis

426

1

S → A: No effect. Ref.10

Mutagenesis

428

1

L → A: 60% loss of in vitro transcription. Ref.10

Mutagenesis

430

1

I → A: No effect. Ref.10

Mutagenesis

433 – 437

5

DRGGK → AAGGA: 80% loss of in vitro transcription. Ref.10

Mutagenesis

436

1

G → A: No effect. Ref.10

Mutagenesis

447

1

S → A: Complete loss of phosphorylation. Ref.11

Mutagenesis

449

1

S → A: Complete loss of phosphorylation. Ref.11

Mutagenesis

453

1

K → A: 60% loss of in vitro transcription. Ref.10

Mutagenesis

455 – 456

2

KE → AA: 40% loss of in vitro transcription.

Mutagenesis

460 – 465

6

KATRFD → AATAFA: 80% loss of in vitro transcription. Ref.10

Mutagenesis

469 – 473

5

ETLED → ATLAA: 60% loss of in vitro transcription. Ref.10

Mutagenesis

482 – 485

4

REDE → AAAA: Complete loss of in vitro replication and N(0) binding.

Mutagenesis

487 – 489

3

RDE → AAA: Complete loss of N(0) binding.

Mutagenesis

497 – 499

3

ERD → AAA: No effect.

Mutagenesis

506 – 509

4

NASR → AASA: Complete loss of transcription and replication.

Mutagenesis

514 – 516

3

KEK → AAA: 56% loss of transcription.

Mutagenesis

524 – 526

3

LVI → AAA: Complete loss of transcription, replication and N(0) binding.

Mutagenesis

533 – 536

4

RAEK → AAAA: 50% loss of transcription. Completely abolishes N(0) binding.

Mutagenesis

549 – 553

5

DQEVK → AQAVA: 50% loss of transcription.

Mutagenesis

560 – 562

3

EED → AAA: Complete loss of transcription, in vitro replication and N(0) binding. Ref.12

Secondary structure

1

.

.

.

.

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.

.

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.

.

.

.

.

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568

Helix Strand Turn

Details...

Helix

322 – 334

13

Beta strand

337 – 339

3

Helix

341 – 344

4

Helix

350 – 359

10

Helix

364 – 424

61

Helix

425 – 428

4

Helix

519 – 526

8

Helix

534 – 544

11

Helix

550 – 566

17

Sequences

	Sequence		Length	Mass (Da)
	P04859-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 494B675A55045C93	FASTA	568	62,004
	10 20 30 40 50 60 MDQDAFILKE DSEVEREAPG GRESLSDVIG FLDAVLSSEP TDIGGDRSWL HNTINTPQGP 70 80 90 100 110 120 GSAHRAKSEG EGEVSTPSTQ DNRSGEESRV SGRTSKPEAE AHAGNLDKQN IHRAFGGRTG 130 140 150 160 170 180 TNSVSQDLGD GGDSGILENP PNERGYPRSG IEDENREMAA HPDKRGEDQA EGLPEEVRGG 190 200 210 220 230 240 TSLPDEGEGG ASNNGRSMEP GSSHSARVTG VLVIPSPELE EAVLRRNKRR PTNSGSKPLT 250 260 270 280 290 300 PATVPGTRSP PLNRYNSTGS PPGKPPSTQD EHINSGDTPA VRVKDRKPPI GTRSVSDCPA 310 320 330 340 350 360 NGRPIHPGLE SDSTKKGIGE NTSSMKEMAT LLTSLGVIQS AQEFESSRDA SYVFARRALK 370 380 390 400 410 420 SANYAEMTFN VCGLILSAEK SSARKVDENK QLLKQIQESV ESFRDIYKRF SEYQKEQNSL 430 440 450 460 470 480 LMSNLSTLHI ITDRGGKTDN TDSLTRSPSV FAKSKENKTK ATRFDPSMET LEDMKYKPDL 490 500 510 520 530 540 IREDEFRDEI RNPVYQERDT EPRASNASRL LPSKEKPTMH SLRLVIESSP LSRAEKAAYV 550 560 KSLSKCKTDQ EVKAVMELVE EDIESLTN

References

[1]	"Sendai virus contains overlapping genes expressed from a single mRNA." Giorgi C., Blumberg B.M., Kolakofsky D. Cell 35:829-836(1983) [PubMed: 6317203] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	Kolakofsky D. Submitted (JAN-2005) to UniProtKB Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]	"Separate domains of Sendai virus P protein are required for binding to viral nucleocapsids." Ryan K.W., Portner A. Virology 174:515-521(1990) [PubMed: 2154886] [Abstract] Cited for: INTERACTION WITH THE NUCLEOCAPSID.
[4]	"An acidic activation-like domain of the Sendai virus P protein is required for RNA SYnthesis and encapsidation." Curran J., Pelet T., Kolakofsky D. Virology 202:875-884(1994) [PubMed: 8030249] [Abstract] Cited for: INTERACTION WITH L PROTEIN.
[5]	"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." Curran J., Marq J.-B., Kolakofsky D. J. Virol. 69:849-855(1995) [PubMed: 7815552] [Abstract] Cited for: INTERACTION WITH NUCLEOPROTEIN N(0).
[6]	"Sendai virus P protein is constitutively phosphorylated at serine249: high phosphorylation potential of the P protein." Byrappa S., Pan Y.-B., Gupta K.C. Virology 216:228-234(1996) [PubMed: 8614993] [Abstract] Cited for: PHOSPHORYLATION AT SER-249.
[7]	"The paramyxovirus, Sendai virus, V protein encodes a luxury function required for viral pathogenesis." Kato A., Kiyotani K., Sakai Y., Yoshida T., Nagai Y. EMBO J. 16:578-587(1997) [PubMed: 9034340] [Abstract] Cited for: RNA EDITING.
[8]	"Phosphorylation of Sendai virus phosphoprotein by cellular protein kinase C zeta." Huntley C.C., De B.P., Banerjee A.K. J. Biol. Chem. 272:16578-16584(1997) [PubMed: 9195969] [Abstract] Cited for: PHOSPHORYLATION BY PKC ZETA.
[9]	"Role of primary constitutive phosphorylation of Sendai virus P and V proteins in viral replication and pathogenesis." Hu C.-J., Kato A., Bowman M.C., Kiyotani K., Yoshida T., Moyer S.A., Nagai Y., Gupta K.C. Virology 263:195-208(1999) [PubMed: 10544094] [Abstract] Cited for: PHOSPHORYLATION AT SER-249, MUTAGENESIS OF SER-249 AND PRO-250.
[10]	"Dissection of individual functions of the Sendai virus phosphoprotein in transcription." Bowman M.C., Smallwood S., Moyer S.A. J. Virol. 73:6474-6483(1999) [PubMed: 10400742] [Abstract] Cited for: 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.
[11]	"Functional significance of alternate phosphorylation in Sendai virus P protein." Hu C.-J., Gupta K.C. Virology 268:517-532(2000) [PubMed: 10704359] [Abstract] Cited for: PHOSPHORYLATION AT SER-68; SER-125; SER-192; SER-257; SER-260; SER-447 AND SER-449, MUTAGENESIS OF SER-68; SER-125; SER-192; SER-257; SER-260; SER-447 AND SER-449.
[12]	"The C-terminal 88 amino acids of the Sendai virus P protein have multiple functions separable by mutation." Tuckis J., Smallwood S., Feller J.A., Moyer S.A. J. Virol. 76:68-77(2002) [PubMed: 11739672] [Abstract] Cited for: 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.
[13]	"Tetrameric coiled coil domain of Sendai virus phosphoprotein." Tarbouriech N., Curran J., Ruigrok R.W.H., Burmeister W.P. Nat. Struct. Biol. 7:777-781(2000) [PubMed: 10966649] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 320-433.
[14]	"Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution." Blanchard L., Tarbouriech N., Blackledge M., Timmins P., Burmeister W.P., Ruigrok R.W.H., Marion D. Virology 319:201-211(2004) [PubMed: 14980481] [Abstract] Cited for: STRUCTURE BY NMR OF 516-568.

Cross-references

Sequence databases

PIR

RRNZHS. A28985.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EZJ	X-ray	1.90	A	320-433	[»]
1R4G	NMR	-	A	516-568	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR016075. RNA_pol_Pprot-P_XD_paramyxovir.
IPR002693. RNA_pol_PProtein_C_Sendai-typ.
[Graphical view]

Pfam

PF01806. Paramyxo_P. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PHOSP_SENDH

Accession

Primary (citable) accession number: P04859

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	November 24, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)