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