WPP domain


title: "WPP domain" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["protein-domains"] topic_path: "general/protein-domains" source: "https://en.wikipedia.org/wiki/WPP_domain" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::data[format=table title="Infobox protein family"]

FieldValue
SymbolWPP
NameWPP domain
PfamPF13943
::

| Symbol = WPP | Name = WPP domain | image = | width = | caption = | Pfam = PF13943 | Pfam_clan = | InterPro = | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = The WPP domain is a protein domain thought to be exclusively found in plants, first identified in 2000. The domain is about 90 amino acid residues long.

The domain is known to direct RanGAP to the nuclear envelope. Non-RanGAP nuclear envelope proteins are also known to encode WPP domains, such as MFP1 attachment factor 1 (MAF1), and WPP2.

The WPP stands for a tryptophan-proline-proline motif that is highly conserved in the domain. Either deletion of the WPP domain or mutation of both the namesake tryptophan and first proline residues into alanine in the Arabidopsis thaliana protein RanGAP1 leads to mis-targeting in the majority of cells.

::figure[src="https://upload.wikimedia.org/wikipedia/commons/a/a7/WPP_domain_alignment.PNG" caption="A [[multiple sequence alignment]] of proteins containing a WPP domain showing the conserved WPP sequence motif to the left."] ::

References

References

  1. Meier I. (December 2000). "A novel link between ran signal transduction and nuclear envelope proteins in plants". [[Plant Physiology (journal).
  2. (December 2001). "A domain unique to plant RanGAP is responsible for its targeting to the plant nuclear rim". [[Proceedings of the National Academy of Sciences of the United States of America]].
  3. (December 2004). "Arabidopsis WPP-domain proteins are developmentally associated with the nuclear envelope and promote cell division". [[The Plant Cell]].

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