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PROSITE documentation PDOC50202
Major sperm protein (MSP) domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC50202

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.

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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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