The domain within your query sequence starts at position 6 and ends at position 64; the E-value for the ISK_Channel domain shown below is 2.5e-7.



PFAM accession number:PF02060
Interpro abstract (IPR000369):

Two types of beta subunit (KCNE and KCNAB) are presently known to associate with voltage-gated alpha subunits (Kv, KCNQ and eag-like). However, not all combinations of alpha and beta subunits are possible. The KCNE family of K+ channel subunits are membrane glycoproteins that possess a single transmembrane (TM) domain. They share no structural relationship with the alpha subunit proteins, which possess pore forming domains. The subunits appear to have a regulatory function, modulating the kinetics and voltage dependence of the alpha subunits of voltage-dependent K+ channels. KCNE subunits are formed from short polypeptides of ~130 amino acids, and are divided into five subfamilies: KCNE1 (MinK/IsK), KCNE2 (MiRP1), KCNE3 (MiRP2), KCNE4 (MiRP3) and KCNE1L (AMMECR2).

Potassium channels are the most diverse group of the ion channel family [ (PUBMED:1772658) (PUBMED:1879548) ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ (PUBMED:2451788) ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ (PUBMED:2555158) ]: the practically non-inactivating 'delayed' group and the rapidly inactivating 'transient' group.

These are all highly similar proteins, with only small amino acid changes causing the diversity of the voltage-dependent gating mechanism, channel conductance and toxin binding properties. Each type of K + channel is activated by different signals and conditions depending on their type of regulation: some open in response to depolarisation of the plasma membrane; others in response to hyperpolarisation or an increase in intracellular calcium concentration; some can be regulated by binding of a transmitter, together with intracellular kinases; while others are regulated by GTP-binding proteins or other second messengers [ (PUBMED:2448635) ]. In eukaryotic cells, K + channels are involved in neural signalling and generation of the cardiac rhythm, act as effectors in signal transduction pathways involving G protein-coupled receptors (GPCRs) and may have a role in target cell lysis by cytotoxic T-lymphocytes [ (PUBMED:1373731) ]. In prokaryotic cells, they play a role in the maintenance of ionic homeostasis [ (PUBMED:11178249) ].

All K + channels discovered so far possess a core of alpha subunits, each comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG), which has been termed the K + selectivity sequence. In families that contain one P-domain, four subunits assemble to form a selective pathway for K + across the membrane. However, it remains unclear how the 2 P-domain subunits assemble to form a selective pore. The functional diversity of these families can arise through homo- or hetero-associations of alpha subunits or association with auxiliary cytoplasmic beta subunits. K + channel subunits containing one pore domain can be assigned into one of two superfamilies: those that possess six transmembrane (TM) domains and those that possess only two TM domains. The six TM domain superfamily can be further subdivided into conserved gene families: the voltage-gated (Kv) channels; the KCNQ channels (originally known as KvLQT channels); the EAG-like K + channels; and three types of calcium (Ca)-activated K + channels (BK, IK and SK) [ (PUBMED:11178249) ]. The 2TM domain family comprises inward-rectifying K + channels. In addition, there are K + channel alpha-subunits that possess two P-domains. These are usually highly regulated K + selective leak channels.

GO process:ion transport (GO:0006811)
GO component:membrane (GO:0016020)
GO function:voltage-gated potassium channel activity (GO:0005249)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ISK_Channel