|Name:||potassium voltage-gated channel, shaker-related subfamily, beta member 1|
|Aliases:||AKR6A3, KCNA1B, hKvBeta3, Kvb1.3, hKvb3|
|PubMed (8838324):|| Schultz D, Litt M, Smith L, Thayer M, McCormack K. Localization of two potassium channel beta subunit genes, KCNA1B and KCNA2B.Genomics. 1996 Feb 1;31(3):389-91. PMID: 8838324 [PubMed - indexed for MEDLINE]|
The gating properties and current amplitudes of mammalian voltage-activated Shaker potassium channels are modulated by at least two associated beta subunits (Kv beta 1.1 and Kv beta 1.2). The human Kv beta 1.1 gene (KCNA1B) resides on chromosome 3, as indicated by somatic cell hybrid mapping. More precise localization of KCNA1B to 3q26.1 was obtained with fluorescence in situ hybridization (FISH) and was corroborated by PCR screening of the CEPH YAC library. The human Kv beta 1.2 gene (KCNA2B) resides on chromosome 1, as indicated by somatic cell hybrid mapping, and has been localized by FISH to 1p36.3.
|PubMed (7499366):|| England SK, Uebele VN, Kodali J, Bennett PB, Tamkun MM. A novel K+ channel beta-subunit (hKv beta 1.3) is produced via alternative mRNAsplicing.J Biol Chem. 1995 Dec 1;270(48):28531-4. PMID: 7499366 [PubMed - indexed for MEDLINE]|
Voltage-gated K+ channels can form multimeric complexes with accessory beta-subunits. We report here a novel K+ channel beta-subunit cloned from human heart, hKv beta 1.3, that has 74-83% overall identity with previously cloned beta-subunits. Comparison of hKv beta 1.3 with the previously cloned hKv beta 3 and rKv beta 1 proteins indicates that the carboxyl-terminal 328 amino acids are identical, while unique variable length amino termini exist. Analysis of human beta-subunit cDNA and genomic nucleotide sequences confirm that these three beta-subunits are alternatively spliced from a common beta-subunit gene. Co-expression of hKv beta 1.3 in Xenopus oocytes with the delayed rectifier hKv1.5 indicated that hKv beta 1.3 has unique functional effects. This novel beta-subunit induced a time-dependent inactivation during membrane voltage steps to positive potentials, induced a 13-mV hyperpolarizing shift in the activation curve, and slowed deactivation (tau = 13 +/- 0.5 ms versus 35 +/- 1.7 ms at -40 mV). Most notably, hKv beta 1.3 converted the Kv1.5 outwardly rectifying current voltage relationship to one showing strong inward rectification. These data suggest that Kv channel current diversity may arise from association with alternatively spliced Kv beta-subunits. A simplified nomenclature for the K+ channel beta-subunit subfamilies is suggested.
>sp|Q14722|KVB1_HUMAN Voltage-gated potassium channel beta-1 subunit (K+ channel beta-1 subunit) (Kv-beta-1) - Homo sapiens (Human). MLAARTGAAGSQISEENTKLRRQSGFSVAGKDKSPKKASENAKDSSLSPSGESQLRARQLALLREVEMNWYLKLCDLSSE HTTVCTTGMPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGW RRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTS RWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLK CYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVV NEIDNILRNKPYSKKDYRS