PROSITE documentation PDOC50202 [for PROSITE entry PS50202]

Major sperm protein (MSP) domain profile





Description

Nematode sperm are unusual amoeboid cells in which motility is not based on actin, but instead on the major sperm protein (MSP) that polymerizes to form a cytoskeleton constructed from intermeshed filaments. MSP is a dimeric molecule that polymerizes to form non-polar filaments constructed from two helical subfilaments that wind round one another. The filaments then assemble into larger macromolecular assemblies called fibre complexes. MSP is a small (~14 kDa) basic protein typically encoded by a multigene family of up to 28 members [1,2,3,4]. An about 120-amino acid domain similar to MSP has been found in the following proteins:

  • Animal Vesicle-Associated Membrane Protein-associated (VAMP-associated) protein family of 33 kDa (VAP33). VAP33 is required for neurotransmitter release. It binds to the v-SNARE synaptobrevin/VAMP which is associated with vesicle fusion. VAP33 has a two-domain structure with its N-terminus being highly homologous to MSP, whereas its C-terminus is based on a putative α-helical coiled-coil combined with an extremly hydrophobic membrane-attachment region [5].
  • Nicotiana plumbaginifolia VAP27, a VAP33 homologue. It interacts with the resistance protein Cf9 [6].
  • Yeast inositol regulator SCS2, a VAP33 homologue. It is C-terminally anchored to the endoplasmic reticulum [7].

The MSP polypeptide chain has an immunoglobulin-like fold based on a seven-stranded β sandwich measuring approximately 15 A x 20 A x 45 A and having opposing three-stranded and four-stranded β sheets (see <PDB:1MSP>) [1].

The profile we developed covers the entire MSP domain.

Last update:

October 2002 / First entry.

Technical section

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

MSP, PS50202; Major sperm protein (MSP) domain profile  (MATRIX)


References

1AuthorsBullock T.L., Roberts T.M., Stewart M.
Title2.6 A resolution crystal structure of helices of the motile major sperm protein (MSP) of Caenorhabditis elegans.
SourceJ. Mol. Biol. 263:284-296(1996).
PubMed ID8913307

2AuthorsBaker A.M.E., Roberts T.M., Stewart M.
TitleThe crystal structure of aminoglycoside-3'-phosphotransferase-IIa, an enzyme responsible for antibiotic resistance.
SourceJ. Mol. Biol. 319:491-499(2002).
PubMed ID12051923

3AuthorsHaaf A., LeClaire L. III, Roberts G., Kent H.M., Roberts T.M., Stewart M., Neuhaus D.
TitleSolution structure of the motile major sperm protein (MSP) of Ascaris suum - evidence for two manganese binding sites and the possible role of divalent cations in filament formation.
SourceJ. Mol. Biol. 284:1611-1624(1998).
PubMed ID9878374

4AuthorsSmith H.E., Ward S.
TitleIdentification of protein-protein interactions of the major sperm protein (MSP) of Caenorhabditis elegans.
SourceJ. Mol. Biol. 279:605-619(1998).
PubMed ID9641981

5AuthorsNishimura Y., Hayashi M., Inada H., Tanaka T.
TitleMolecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins.
SourceBiochem. Biophys. Res. Commun. 254:21-26(1999).
PubMed ID9920726

6AuthorsLaurent F., Labesse G., de Wit P.
TitleMolecular cloning and partial characterization of a plant VAP33 homologue with a major sperm protein domain.
SourceBiochem. Biophys. Res. Commun. 270:286-292(2000).
PubMed ID10733941
DOI10.1006/bbrc.2000.2387

7AuthorsKagiwada S., Hosaka K., Murata M., Nikawa J.-I., Takatsuki A.
TitleThe Saccharomyces cerevisiae SCS2 gene product, a homolog of a synaptobrevin-associated protein, is an integral membrane protein of the endoplasmic reticulum and is required for inositol metabolism.
SourceJ. Bacteriol. 180:1700-1708(1998).
PubMed ID9537365



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