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PROSITE documentation PDOC00195 [for PROSITE entry PS00223]

Annexins repeated domain signature





Description

Annexins [1,2,3,4,5,6] are a group of calcium-binding proteins that associate reversibly with membranes. They bind to phospholipid bilayers in the presence of micromolar free calcium concentration. The binding is specific for calcium and for acidic phospholipids. Annexins have been claimed to be involved in cytoskeletal interactions, phospholipase inhibition, intracellular signalling, anticoagulation, and membrane fusion.

Each of these proteins consist of an N-terminal domain of variable length followed by four or eight copies of a conserved segment of sixty one residues. The repeat (sometimes known as an 'endonexin fold') consists of five α-helices that are wound into a right-handed superhelix [7].

The proteins known to belong to the annexin family are listed below:

  • Annexin I (Lipocortin 1) (Calpactin 2) (p35) (Chromobindin 9).
  • Annexin II (Lipocortin 2) (Calpactin 1) (Protein I) (p36) (Chromobindin 8).
  • Annexin III (Lipocortin 3) (PAP-III).
  • Annexin IV (Lipocortin 4) (Endonexin I) (Protein II) (Chromobindin 4).
  • Annexin V (Lipocortin 5) (Endonexin 2) (VAC-α) (Anchorin CII) (PAP-I).
  • Annexin VI (Lipocortin 6) (Protein III) (Chromobindin 20) (p68) (p70). This is the only known annexin that contains 8 (instead of 4) repeats.
  • Annexin VII (Synexin).
  • Annexin VIII (Vascular anticoagulant-β) (VAC-β).
  • Annexin IX from Drosophila.
  • Annexin X from Drosophila.
  • Annexin XI (Calcyclin-associated annexin) (CAP-50).
  • Annexin XII from Hydra vulgaris.
  • Annexin XIII (Intestine-specific annexin) (ISA).

The signature pattern for this domain spans positions 9 to 61 of the repeat and includes the only perfectly conserved residue (an arginine in position 22).

Note:

A sequence similar to the annexin domain has been found in the N-terminal of α-giardins of Giardia lamblia [8].

Last update:

December 2004 / Pattern and text revised.

Technical section

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

ANNEXIN, PS00223; Annexins repeated domain signature  (PATTERN)


References

1AuthorsRaynal P. Pollard H.B.
TitleAnnexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins.
SourceBiochim. Biophys. Acta 1197:63-93(1994).
PubMed ID8155692

2AuthorsBarton G.J. Newman R.H. Freemont P.S. Crumpton M.J.
TitleAmino acid sequence analysis of the annexin super-gene family of proteins.
SourceEur. J. Biochem. 198:749-760(1991).
PubMed ID1646719

3AuthorsBurgoyne R.D. Geisow M.J.
TitleThe annexin family of calcium-binding proteins. Review article.
SourceCell Calcium 10:1-10(1989).
PubMed ID2659190

4AuthorsHaigler H.T. Fitch J.M. Jones J.M. Schlaepfer D.D.
TitleTwo lipocortin-like proteins, endonexin II and anchorin CII, may be alternate splices of the same gene.
SourceTrends Biochem. Sci. 14:48-50(1989).
PubMed ID2539661

5AuthorsKlee C.B.
TitleCa2+-dependent phospholipid- (and membrane-) binding proteins.
SourceBiochemistry 27:6645-6653(1988).
PubMed ID2973805

6AuthorsSmith P.D. Moss S.E.
TitleStructural evolution of the annexin supergene family.
SourceTrends Genet. 10:241-246(1994).
PubMed ID8091504

7AuthorsHuber R. Roemisch J. Paques E.-P.
TitleThe crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes.
SourceEMBO J. 9:3867-3874(1990).
PubMed ID2147412

8AuthorsFiedler K. Simons K.
TitleAnnexin homologues in Giardia lamblia.
SourceTrends Biochem. Sci. 20:177-178(1995).
PubMed ID7610478



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