Protein Details: Potassium voltage-gated channel subfamily B member 2

Protein ID

ICDB_Pro_0056

Protein Name

Potassium voltage-gated channel subfamily B member 2

Gene Name

Kcnb2

Organism

Mus musculus (Mouse)

Length

907 amino acids

AlphaFoldDB

AF-A6H8H5-F1-model_v4.pdb

Function

Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes; primarily in the brain and smooth muscle cells. Channels open or close in response to the voltage difference across the membrane; letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone; such as KCNS1 and KCNS2; creating a functionally diverse range of channel complexes. In vivo; membranes probably contain a mixture of heteromeric potassium channel complexes; making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells

Sequence

MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMREREGEEFDNTCCPEKRKKLWDLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQENDEFGQPSDNRKLAHVEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDATKFTSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVAVEKAGESANTKDSVDDNHLSPSRWKWARKALSETSSNKSYENKYQEVSQNDSHEHLNNTSSSSPQHLSAQKLEMLYNEITKTQPHSHPNPDCQEQPERPCVYEEEIEMEEVICPQEQLAVAQTEVIVDMKSTSSIDSFTSCATDFTETERSPLPPPSASHLQMKFPTDLPGTDEHQRARAPPFLTLSRDKGPAAREAAVDYAPIDITVNLDAGASHGPLQPDSASDSPKSSLKGSNPLKSRSLKVNFQENRASAPQTPPSTARPLPVTTADFPLTTPQHMSTILLEEALPQGQPPLLEADDSAHCQGPSKGFSPRFPKQKLFPFSSRERRSFTEIDTGEDEDFLDLQRSRPDKQADPSPNCLADKPGDARDSLREEGCVGSSSPQNTDHNCRQDIYQAVGEVKKDSSQEGYKMENHLFAPEIHSNPGDTGHCPTRETSM

PDB Structures

Ligand Binding

1. DICL_CP

2. DICL_Pep

Binding Site

Disease

Location

DOI ID

10.1371/journal.pbio.1000112; 10.1101/gr.2596504; 10.1111/j.1749-6632.1999.tb11293.x; 10.1016/j.cell.2010.12.001

RefSeq

NP_001091998.1; XP_006495658.1

Feature