Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoprotein

Gene

P/V/C

Organism
Sendai virus (strain Harris) (SeV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

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.

GO - Molecular functioni

GO - Biological processi

  • negative stranded viral RNA replication Source: UniProtKB
  • transcription, DNA-templated Source: InterPro

Keywordsi

Molecular functionChaperone
Biological processViral RNA replication

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoprotein
Short name:
Protein P
Gene namesi
Name:P/V/C
OrganismiSendai virus (strain Harris) (SeV)
Taxonomic identifieri11196 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeRespirovirus
Virus hostiCavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]
Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]

Subcellular locationi

GO - Cellular componenti

  • host cell cytoplasm Source: UniProtKB-SubCell
  • protein complex Source: CAFA

Keywords - Cellular componenti

Host cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi68S → A: Complete loss of phosphorylation. 1 Publication1
Mutagenesisi125S → A: Complete loss of phosphorylation. 1 Publication1
Mutagenesisi192S → A: Complete loss of phosphorylation. 1 Publication1
Mutagenesisi249S → A: No effect. 1 Publication1
Mutagenesisi249S → D: No effect. 1 Publication1
Mutagenesisi250P → A: Prevents S-249 phosphorylation. No effect on P protein functions. 1 Publication1
Mutagenesisi257S → A: Complete loss of phosphorylation. 1 Publication1
Mutagenesisi260S → A: Complete loss of phosphorylation. 1 Publication1
Mutagenesisi408 – 409KR → AA: 80% loss of in vitro transcription. 1 Publication2
Mutagenesisi412 – 416EYQKE → AYQAA: 60% loss of in vitro transcription. 1 Publication5
Mutagenesisi419S → A: No effect. 1 Publication1
Mutagenesisi421L → A: 80% loss of in vitro transcription. 1 Publication1
Mutagenesisi425L → A: 80% loss of in vitro transcription. 1 Publication1
Mutagenesisi426S → A: No effect. 1 Publication1
Mutagenesisi428L → A: 60% loss of in vitro transcription. 1 Publication1
Mutagenesisi430I → A: No effect. 1 Publication1
Mutagenesisi433 – 437DRGGK → AAGGA: 80% loss of in vitro transcription. 1 Publication5
Mutagenesisi436G → A: No effect. 1 Publication1
Mutagenesisi447S → A: Complete loss of phosphorylation. 1 Publication1
Mutagenesisi449S → A: Complete loss of phosphorylation. 1 Publication1
Mutagenesisi453K → A: 60% loss of in vitro transcription. 1 Publication1
Mutagenesisi455 – 456KE → AA: 40% loss of in vitro transcription. 1 Publication2
Mutagenesisi460 – 465KATRFD → AATAFA: 80% loss of in vitro transcription. 1 Publication6
Mutagenesisi469 – 473ETLED → ATLAA: 60% loss of in vitro transcription. 1 Publication5
Mutagenesisi482 – 485REDE → AAAA: Complete loss of in vitro replication and N(0) binding. 1 Publication4
Mutagenesisi487 – 489RDE → AAA: Complete loss of N(0) binding. 1 Publication3
Mutagenesisi497 – 499ERD → AAA: No effect. 1 Publication3
Mutagenesisi506 – 509NASR → AASA: Complete loss of transcription and replication. 1 Publication4
Mutagenesisi514 – 516KEK → AAA: 56% loss of transcription. 1 Publication3
Mutagenesisi524 – 526LVI → AAA: Complete loss of transcription, replication and N(0) binding. 1 Publication3
Mutagenesisi533 – 536RAEK → AAAA: 50% loss of transcription. Completely abolishes N(0) binding. 1 Publication4
Mutagenesisi549 – 553DQEVK → AQAVA: 50% loss of transcription. 5
Mutagenesisi560 – 562EED → AAA: Complete loss of transcription, in vitro replication and N(0) binding. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001427141 – 568PhosphoproteinAdd BLAST568

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68Phosphoserine; by host1 Publication1
Modified residuei125Phosphoserine; by host1 Publication1
Modified residuei192Phosphoserine; by host1 Publication1
Modified residuei249Phosphoserine; by host2 Publications1
Modified residuei257Phosphoserine; by host1 Publication1
Modified residuei260Phosphoserine; by host1 Publication1
Modified residuei447Phosphoserine; by host1 Publication1
Modified residuei449Phosphoserine; by host1 Publication1

Post-translational modificationi

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.4 Publications

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiP04859.

Interactioni

Subunit structurei

Homotetramer. Binds to the L protein, N0 and to the C-terminal domain of N in ribonucleocapsid.

GO - Molecular functioni

  • disordered domain specific binding Source: CAFA

Structurei

Secondary structure

1568
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi322 – 334Combined sources13
Beta strandi337 – 339Combined sources3
Helixi341 – 344Combined sources4
Helixi350 – 359Combined sources10
Helixi364 – 424Combined sources61
Helixi425 – 428Combined sources4
Helixi519 – 526Combined sources8
Helixi534 – 544Combined sources11
Helixi550 – 566Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EZJX-ray1.90A320-433[»]
1R4GNMR-A516-568[»]
DisProtiDP00939.
ProteinModelPortaliP04859.
SMRiP04859.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04859.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 41N(0) binding9
Regioni345 – 412Bipartite nucleocapsid binding domain 1Add BLAST68
Regioni413 – 445L protein bindingAdd BLAST33
Regioni479 – 568Bipartite nucleocapsid binding domain 2Add BLAST90

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili364 – 429Add BLAST66

Domaini

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.

Sequence similaritiesi

Belongs to the respirovirus P protein family.Curated

Keywords - Domaini

Coiled coil

Family and domain databases

InterProiView protein in InterPro
IPR002693. Paramyxo_PProtein_C.
IPR016075. RNA_pol_Pprot-P_XD_paramyxovir.
PfamiView protein in Pfam
PF01806. Paramyxo_P. 1 hit.
SUPFAMiSSF101089. SSF101089. 1 hit.

Sequencei

Sequence statusi: Complete.

P04859-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQDAFILKE DSEVEREAPG GRESLSDVIG FLDAVLSSEP TDIGGDRSWL
60 70 80 90 100
HNTINTPQGP GSAHRAKSEG EGEVSTPSTQ DNRSGEESRV SGRTSKPEAE
110 120 130 140 150
AHAGNLDKQN IHRAFGGRTG TNSVSQDLGD GGDSGILENP PNERGYPRSG
160 170 180 190 200
IEDENREMAA HPDKRGEDQA EGLPEEVRGG TSLPDEGEGG ASNNGRSMEP
210 220 230 240 250
GSSHSARVTG VLVIPSPELE EAVLRRNKRR PTNSGSKPLT PATVPGTRSP
260 270 280 290 300
PLNRYNSTGS PPGKPPSTQD EHINSGDTPA VRVKDRKPPI GTRSVSDCPA
310 320 330 340 350
NGRPIHPGLE SDSTKKGIGE NTSSMKEMAT LLTSLGVIQS AQEFESSRDA
360 370 380 390 400
SYVFARRALK SANYAEMTFN VCGLILSAEK SSARKVDENK QLLKQIQESV
410 420 430 440 450
ESFRDIYKRF SEYQKEQNSL LMSNLSTLHI ITDRGGKTDN TDSLTRSPSV
460 470 480 490 500
FAKSKENKTK ATRFDPSMET LEDMKYKPDL IREDEFRDEI RNPVYQERDT
510 520 530 540 550
EPRASNASRL LPSKEKPTMH SLRLVIESSP LSRAEKAAYV KSLSKCKTDQ
560
EVKAVMELVE EDIESLTN
Length:568
Mass (Da):62,004
Last modified:August 13, 1987 - v1
Checksum:i494B675A55045C93
GO

RNA editingi

Edited at position 318.1 Publication
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).

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti311S → T. 1

Sequence databases

PIRiA28985. RRNZHS.

Keywords - Coding sequence diversityi

RNA editing

Similar proteinsi

Entry informationi

Entry nameiPHOSP_SENDH
AccessioniPrimary (citable) accession number: P04859
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 10, 2017
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families