ANO 2011

ANO 2011 is a centrist and populistpolitical party in the Czech Republic founded by Andrej Babiš, second wealthiest man in the Czech republic, owner of Agrofert and media publishing company MAFRA. It is based on the former movement Action of Dissatisfied Citizens (Czech: Akce nespokojených občanů, ANO). "Ano" means "yes" in Czech.

History

The idea of founding a new political party came after current leader and founder Andrej Babiš started talking about system corruption. His statements were supported by thousands of Czechs. ANO 2011 started as association in November 2011 and on 11 May 2012 ANO became official political party in the Czech Republic.

In 2013 Czech legislative election held on 25–26 October 2013, ANO gained 18.7% of the vote and 47 seats in the Chamber of Deputies, attaining second place behind the Czech Social Democratic Party (ČSSD).

On 29 January 2014 the Cabinet of Prime Minister Bohuslav Sobotka was sworn in, with ANO and the Christian Democratic Union (KDU–ČSL) participating as junior coalition partners to the ČSSD.

ANO

Ano or ANO may refer to:

See also

ANO3

ANO3 is a gene that in humans is located on chromosome 11 and encodes the protein anoctamin 3. It belongs to a family of genes (ANO1–ANO10) that appear to encode calcium-activated chloride channels.

Clinical signficance

Mutations in ANO3 have been linked to a form of autosomal dominant cranio-cervical dystonia (also known as DYT23), which presents as abnormal twisting or tremulous movements of the face, voice, head and upper limbs.

References

External links

ANO1

Anoctamin-1 (ANO1) also known as Transmembrane member 16A (TMEM16A) is a protein that, in humans, is encoded by the ANO1 gene. Anoctamin-1 is a voltage-sensitive calcium-activated chloride channel that is expressed in smooth muscle and epithelial cells; it is highly expressed in human interstitial cells of Cajal (ICC) throughout the gastrointestinal tract. Changes in ANO1 channel activity directly/positively correlate with ICC activity.

Function

ANO1 is a transmembrane protein that functions as a calcium-activated chloride channel.Ca²⁺, Sr²⁺, and Ba²⁺ activate the channel.

Structure

No atomic resolution structure of this channel has yet been obtained. However, biochemical evidence suggests that the channel assembles as a dimer of two ANO1 polypeptide subunits. From hydropathy plotting, each subunit is thought to encode a molecule with eight transmembrane domains, with a reentrant loop between the fifth and sixth transmembrane domains. The reentrant loop is thought to be a P loop-like structure responsible for the ion selectivity of the protein.