Annotations for this protein have been verified by the authors of the corresponding papers



DP00699: PhosphoproteinFASTA viewXML view

General information
DisProt:DP00699
Name:Phosphoprotein
Synonym(s):PHOSP_NIPAV
Protein P
First appeared in release:Release 5.2 (08/07/2010)
UniProt:Q9IK91
UniGene: 
SwissProt: PHOSP_NIPAV
TrEMBL:  
NCBI (GI):  
Source organism:Nipah virus
Sequence length:709
Percent disordered:57%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MDKLELVNDG LNIIDFIQKN QKEIQKTYGR SSIQQPSIKD QTKAWEDFLQ CTSGESEQVE - 60
GGMSKDDGDV ERRNLEDLSS TSPTDGTIGK RVSNTRDWAE GSDDIQLDPV VTDVVYHDHG - 120
GECTGYGFTS SPERGWSDYT SGANNGNVCL VSDAKMLSYA PEIAVSKEDR ETDLVHLENK - 180
LSTTGLNPTA VPFTLRNLSD PAKDSPVIAE HYYGLGVKEQ NVGPQTSRNV NLDSIKLYTS - 240
DDEEADQLEF EDEFAGSSSE VIVGISPEDE EPSSVGGKPN ESIGRTIEGQ SIRDNLQAKD - 300
NKSTDVPGAG PKDSAVKEEP PQKRLPMLAE EFECSGSEDP IIRELLKENS LINCQQGKDA - 360
QPPYHWSIER SISPDKTEIV NGAVQTADRQ RPGTPMPKSR GIPIKKGTDA KYPSAGTENV - 420
PGSKSGATRH VRGSPPYQEG KSVNAENVQL NASTAVKETD KSEVNPVDDN DSLDDKYIMP - 480
SDDFSNTFFP HDTDRLNYHA DHLGDYDLET LCEESVLMGV INSIKLINLD MRLNHIEEQV - 540
KEIPKIINKL ESIDRVLAKT NTALSTIEGH LVSMMIMIPG KGKGERKGKN NPELKPVIGR - 600
DILEQQSLFS FDNVKNFRDG SLTNEPYGAA VQLREDLILP ELNFEETNAS QFVPMADDSS - 660
RDVIKTLIRT HIKDRELRSE LIGYLNKAEN DEEIQEIANT VNDIIDGNI



Functional narrative    

Function: Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template (By similarity). May play a role to prevent the establishment of cellular antiviral state by binding to host STAT1 in the cytoplasm. This activity is not as strong as that of V and W.
SUBUNIT: Interacts with host STAT1.


Subcellular Location: Virion. Host cytoplasm.
RNA EDITING: Modified_positions=406; 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 Q997F2), and the W protein (+2G) (AC P0C1C7).
MISCELLANEOUS: The P/V/C gene has two overlapping open reading frames. One encodes the P/V/W proteins and the other the C protein.
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Region 1: 1-406

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered - Pre-Molten Globule
Name:PNT
Location:1 - 406
Length:406
Region sequence:

MDKLELVNDGLNIIDFIQKNQKEIQKTYGRSSIQQPSIKDQTKAWEDFLQCTSGESEQVE
GGMSKDDGDVERRNLEDLSSTSPTDGTIGKRVSNTRDWAEGSDDIQLDPVVTDVVYHDHG
GECTGYGFTSSPERGWSDYTSGANNGNVCLVSDAKMLSYAPEIAVSKEDRETDLVHLENK
LSTTGLNPTAVPFTLRNLSDPAKDSPVIAEHYYGLGVKEQNVGPQTSRNVNLDSIKLYTS
DDEEADQLEFEDEFAGSSSEVIVGISPEDEEPSSVGGKPNESIGRTIEGQSIRDNLQAKD
NKSTDVPGAGPKDSAVKEEPPQKRLPMLAEEFECSGSEDPIIRELLKENSLINCQQGKDA
QPPYHWSIERSISPDKTEIVNGAVQTADRQRPGTPMPKSRGIPIKK

Modification type: Fragment
Monomeric
Native
PDB:  
Structural/functional type: Function arises via a pre-molten globule to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Sensitivity to proteolysis (299 K; pH: 8; thermolysin)

  2. Nuclear magnetic resonance (NMR) (300 K; pH: 7; D2O 10 %; NaCl 150 mM; PNT 0.1 mM; sodium phosphate 10 mM)

  3. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7; )

  4. Dynamic light scattering (298 K; pH: 8; )

  5. SDS-PAGE gel, Aberrant mobility on

References:
  1. Habchi J, Mamelli L, Darbon H, Longhi S. "Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment." PLoS ONE. 2010; 5(7): e11684. PubMed: 20657787

Comments:
The PNT region is shared by Proteins P, V and W. According to Habchi et al. (2010), the disorder found in the PNT region of Protein P is "a way of alleviating evolutionary constraints within overlapping reading frames."




References

  1. Habchi J, Mamelli L, Darbon H, Longhi S. "Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment." PLoS ONE. 2010; 5(7): e11684. PubMed: 20657787



Comments


[AV 08/06/2010 PMID 20657787]


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