PROSITE documentation PDOC00362

Dynamin family signature

Description

Dynamin [1,2] is a microtubule-associated force-producing protein of 100 Kd which is involved in the production of microtubule bundles and which is able to bind and hydrolyze GTP. Dynamin is structurally related to the following proteins:

  • Drosophila shibire protein (gene shi) [3]. Shibire is, very probably, the Drosophila cognate of mammalian dynamin. It seems to provide the motor for vesicular transport during endocytosis.
  • Yeast vacuolar sorting protein VPS1 (or SPO15) [4], a protein which could also be involved in microtubule-associated motility.
  • Yeast protein MGM1 [5], which is required for mitochondrial genome maintenance.
  • Yeast protein DNM1, which is involved in endocytosis.
  • Interferon induced Mx proteins [6,7]. Interferon α or β induce the synthesis of a family of closely related proteins. Most of these proteins are known to confer resistance to influenza viruses and/or rhabdoviruses on transfected mammalian cell in culture.

The three motifs found in all GTP-binding proteins are located in the N-terminal part of these proteins. The signature pattern that we developed for these proteins is based on a highly conserved region downstream of the ATP/GTP-binding motif 'A' (P-loop) (see <PDOC00017>).

Last update:

April 2006 / Pattern revised.

Technical section

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

DYNAMIN, PS00410Dynamin family signature  (PATTERN)
Consensus pattern: L-P-[RKT]-[GD]-[STNKEA]-[GND]-[LIVMG]-[VICA]-T-R
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE
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Matching PDB structures: 2AKA 2X2E 2X2F 3T34 ... [ALL]

References

1 Authors Vallee R.B., Shpetner H.S.
Title Motor proteins of cytoplasmic microtubules.
Source Annu. Rev. Biochem. 59:909-932(1990).
PubMed ID 2142876
DOI 10.1146/annurev.bi.59.070190.004401
2 Authors Obar R.A., Collins C.A., Hammarback J.A., Shpetner H.S., Vallee R.B.
Title Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins.
Source Nature 347:256-261(1990).
PubMed ID 2144893
DOI 10.1038/347256a0
3 Authors van der Bliek A., Meyerowitz E.M.
Source Nature 351:411-414(1991).
4 Authors Rothman J.H., Raymond C.K., Gilbert T., O'Hara P.J., Stevens T.H.
Title A putative GTP binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting.
Source Cell 61:1063-1074(1990).
PubMed ID 2112425
5 Authors Jones B.A., Fangman W.L.
Title Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin.
Source Genes Dev. 6:380-389(1992).
PubMed ID 1532158
6 Authors Arnheiter H., Meier E.
Title Mx proteins: antiviral proteins by chance or by necessity?
Source New Biol. 2:851-857(1990).
PubMed ID 1706623
7 Authors Staeheli P., Pitossi F., Pavlovic J.
Title Mx proteins: GTPases with antiviral activity.
Source Trends Cell Biol. 3:268-272(1993).
PubMed ID 14731745

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