Protein Domain : IPR003271

Type:  Family Name:  Potassium channel, inwardly rectifying, Kir2.1
Description:  Potassium channels are the most diverse group of the ion channel family [, ]. They are important in shaping the action potential, and in neuronal excitability and plasticity []. The potassium channel family iscomposed of several functionally distinct isoforms, which can be broadly separated into 2 groups []: 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 []. 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 []. In prokaryotic cells, they play a role in themaintenance of ionic homeostasis [].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 hasbeen 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) []. 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.Inwardly-rectifying potassium channels (Kir) are the principal class of two-TM domain potassium channels. They are characterised by the property of inward-rectification, which is described as the ability to allow large inward currents and smaller outward currents. Inwardly rectifying potassium channels (Kir) are responsible for regulating diverse processes including: cellular excitability, vascular tone, heart rate, renal salt flow, and insulin release []. To date, around twenty members of this superfamily have been cloned, which can be grouped into six families by sequence similarity, and these are designated Kir1.x-6.x [, ].Cloned Kir channel cDNAs encode proteins of between ~370-500 residues, both N- and C-termini are thought to be cytoplasmic, and the N terminus lacks a signal sequence. Kir channel alpha subunits possess only 2TM domains linked with a P-domain. Thus, Kir channels share similarity with the fifth and sixth domains, and P-domain of the other families. It is thought that four Kir subunits assemble to form a tetrameric channel complex, which may be hetero- or homomeric [].Kir2.1 (also known as IRK1) is thought to play a role in controlling the excitability of brain and heart tissues. Immuno-localisation studies haverevealed it to be present on many cell types within the forebrain, including neurones, macroglia, endothelial, ependymal and vascular smooth musclecells. Phosphatidylinositol 4,5-bisphosphate (PIP2) is thought to interact with Kir2.1 (as well as several other Kir subunits) via a C-terminal motif,promoting channel activity. Recently it has been demonstrated that nicotine can block Kir2.1 channels, this likely contributing to its ability topromote the occurrence of cardiac arrhythmias []. Short Name:  K_chnl_inward-rec_Kir2.1

0 Child Features

2 Contains

DB identifier Type Name
IPR013518 Domain Potassium channel, inwardly rectifying, Kir, cytoplasmic
IPR013673 Domain Potassium channel, inwardly rectifying, Kir, N-terminal

1 Cross References

Identifier
PR01324

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0005242 IPR003271
GO:0006813 IPR003271
GO:0016020 IPR003271

3 Ontology Annotations

GO Term Gene Name
GO:0005242 IPR003271
GO:0006813 IPR003271
GO:0016020 IPR003271

1 Parent Features

DB identifier Type Name
IPR016449 Family Potassium channel, inwardly rectifying, Kir

0 Proteins

11 Publications

First Author Title Year Journal Volume Pages PubMed ID
            1772658
            1879548
            1373731
            2448635
            2451788
            2555158
            11178249
            7580148
            10102275
            10449331
            10739749