Ankyrin

From Wikipedia, the free encyclopedia

ankyrin 1, erythrocytic
Identifiers
Symbol(s)	ANK1 ANK
Entrez	286
OMIM	182900
RefSeq	NM_000037
UniProt	P16157
Other data
Locus	Chr. 8 p21.1-11.2

ankyrin 2, neuronal
Identifiers
Symbol(s)	ANK2 LQT4
Entrez	287
OMIM	106410
RefSeq	NM_001148
UniProt	Q01484
Other data
Locus	Chr. 4 q25-q27

ankyrin 3, node of Ranvier (ankyrin G)
Identifiers
Symbol(s)	ANK3
Entrez	288
OMIM	600465
RefSeq	NM_020987
UniProt	Q12955
Other data
Locus	Chr. 10 q21

Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate.

Ankyrin contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain.

The ankyrin repeat is a common 33-residue motif consisting of two alpha helices separated by loops. Ankyrin repeats occur in a huge variety of different proteins, such as gankyrin, virtually all of which are eukaryotic. The majority of proteins contain six or fewer repeats,though the motif is named for ankyrin, which contains up to 24. The record holder is a protein from Giardia lamblia which contains 34 repeats. The repeats are thought to be involved in protein-protein interaction.

[edit] References

Singleton PA, Bourguignon LY. CD44 interaction with ankyrin and IP3 receptor in lipid rafts promotes hyaluronan-mediated Ca2+ signaling leading to nitric oxide production and endothelial cell adhesion and proliferation. Exp Cell Res. 2004 Apr 15;295(1):102-18.

Mosavi LK, Cammett TJ, Desrosiers DC, Peng Z The ankyrin repeat as molecular architecture for protein recognition Protein Science 2004 13:1435-1448 http://www.proteinscience.org/cgi/content/full/13/6/1435