PROSITE documentation PDOC51472
RNA-recognition motif (RRM) Nup35-type domain profile


The nuclear pore complex (NPC) mediates the transport of macromolecules across the nuclear envelope (NE). The NPC is composed of a relatively small number of proteins (~30), termed nucleoporins or Nups. The vertebrate nuclear pore protein Nup35, the ortholog of Saccharomyces cerevisiae Nup53p, is suggested to interact with the NE membrane and to be required for nuclear morphology. The highly conserved region between vertebrate Nup35 and yeast Nup53p is predicted to contain an RNA-recognition motif (RRM) domain (see <PDOC00030>).

The sequences of the RRM Nup-35-type domain are highly conserved in all eucaryotes. The RRM Nup35-type domain adopts the characteristic βαβ βαβ topology of the secondary structure elements, with a four-stranded antiparallel β-sheet packed against two α helices (see <PDB:1WWH>). The RRM Nup35-type domain forms a homodimer and contains atypical rinonucleoprotein (RNP) motifs, which lack the conserved residues that typically bind RNA in canonical RRM domains. The dimer interface involves the β-sheet surface, with its atypical RNP motifs, which is generally used to bind RNA in typical RRM domains [1].

The profile we developed covers the entire RRM Nup35-type domain.

Last update:

December 2009 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

RRM_NUP35, PS51472; RNA-recognition motif (RRM) Nup35-type domain profile  (MATRIX)


1AuthorsHanda N. Kukimoto-Niino M. Akasaka R. Kishishita S. Murayama K. Terada T. Inoue M. Kigawa T. Kose S. Imamoto N. Tanaka A. Hayashizaki Y. Shirouzu M. Yokoyama S.
TitleThe crystal structure of mouse Nup35 reveals atypical RNP motifs and novel homodimerization of the RRM domain.
SourceJ. Mol. Biol. 363:114-124(2006).
PubMed ID16962612

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