DP00144: Histone RNA hairpin-binding proteinFASTA viewXML view

General information
DisProt:DP00144
Name:Histone RNA hairpin-binding protein
Synonym(s):SLBP_DROME
Histone stem-loop-binding protein
Histone mRNA Binding Protein
SLBP
First appeared in release:Release 3.0 (02/17/2006)
UniProt:Q9VAN6
UniGene:Dm.4801
SwissProt: SLBP_DROME
TrEMBL:  
NCBI (GI): 9789800
Source organism:Drosophila melanogaster (Fruit fly)
Sequence length:276
Percent disordered:63%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MLCEDQHMSV ENTPQKGSGS LNSSASSISI DVKPTMQSWA QEVRAEFGHS DEASSSLNSS - 60
AASCGSLAKK ETADGNLESK DGEGREMAFE FLDGVNEVKF ERLVKEEKLK TPYKRRHSFT - 120
PPSNENSRSN SPNSSNSSAN GDAAAPKGGN NPHSRNSKKS GNFRAHKEEK RVRHNSYTSS - 180
TSSSSSYTEA DPAILSRRQK QIDYGKNTAA YERYVEMVPK DERTRDHPRT PNKYGKYSRR - 240
AFDGLVKIWR KSLHIYDPPT QARDTAKDSN SDSDSD



Functional narrative    

Stem-loop binding protein (SLBP) is a 31 kDa protein that is central to the regulation of histone mRNAs and is highly conserved in metazoans. It is involved in histone pre-mRNA 3' processing and couples histone mRNA production with the cell cycle. Both maternal and zygotic proteins play an essential and vital function for development. The SLBP, which binds the conserved 26 nucleotide hairpin at the 3' end of all metazoan replication-dependent histone mRNAs, is important for regulation of histone mRNA processing, translation, and degradation. In vertebrate and Drosophila SLBPs, the region required for RNA binding and pre-mRNA processing is located toward the C-terminal end. dSLBP has a two-domain structure with the RNA binding and processing domain (residues 175-276) in the C-terminal half of the molecule. Drosophila genetics suggests that dSLBP also shuttles between the nucleus and the cytoplasm implicating a cytoplasmic role for the N-terminal domain of dSLBP, but no function has yet been assigned to residues 1-173.

Region 1: 1-175

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
Name:N-terminal domain
Location:1 - 175
Length:175
Region sequence:

MLCEDQHMSVENTPQKGSGSLNSSASSISIDVKPTMQSWAQEVRAEFGHSDEASSSLNSS
AASCGSLAKKETADGNLESKDGEGREMAFEFLDGVNEVKFERLVKEEKLKTPYKRRHSFT
PPSNENSRSNSPNSSNSSANGDAAAPKGGNNPHSRNSKKSGNFRAHKEEKRVRHN

Modification type: Fragment
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 7; 2D (15N,1H) HSQC and 3D HNCA; 3D (13C, 1H) NOESY-HSQC (mixing time of 100 ms); 3D (15N,1H) NOESY-HSQC (mixing time of 75 ms); 3D HNHA; 600 MHz)

  2. Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7; 20 mM sodium phosphate; 50 microM protein)

References:
  1. Thapar R, Mueller GA, Marzluff WF. "The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure." 2004; 43(29): 9390-400. PubMed: 15260482

Comments:
The N-terminal domain of SLBP is intrinsically or natively unfolded but it has transient helical structure in four regions. The N-terminal domain of SLBP gives one cross-peak per residue indicating that, although unfolded, the different conformations are in fast exchange on the NMR time scale.




References

  1. Lanzotti DJ, Kupsco JM, Yang XC, Dominski Z, Marzluff WF, Duronio RJ. "Drosophila stem-loop binding protein intracellular localization is mediated by phosphorylation and is required for cell cycle-regulated histone mRNA expression." Mol Biol Cell. 2004; 15(3): 1112-23. PubMed: 14999087


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