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PR01579

Identifier
KCNAB2CHANEL  [View Relations]  [View Alignment]  
Accession
PR01579
No. of Motifs
5
Creation Date
12-SEP-2001
Title
KCNAB voltage-gated K+ channel beta-2 subunit signature
Database References
PRINTS; PR01577 KCNABCHANNEL
Literature References
1. MILLER, C.
An overview of the potassium channel family.
GENOME BIOL. 1(4) 1-5 (2000).
 
2. BAHRING, R., MILLIGAN, C.J., VARDANYAN, V., ENGELAND, B., YOUNG, B.A.,
DANNENBERG, J., WALDSCHUTZ, R., EDWARDS, J.P., WRAY, D. AND PONGS, O.
Coupling of voltage-dependent potassium channel inactivation and
oxidoreductase active site of Kvbeta subunits.
J.BIOL.CHEM. 276 22923-22929 (2001).
 
3. GULBIS, J.M., MANN, S. AND MACKINNON, R.
Structure of a voltage-dependent potassium channel beta subunit.
CELL 97 943-952 (2001).

Documentation
Potassium ion (K+) channels are a structurally diverse group of proteins
that facilitate the flow of K+ ions across cell membranes. They are
ubiquitous, being present in virtually all cell types. Activation of K+
channels tends to hyperpolarise cells, reducing the membrane's electrical
resistance, dampening nervous activity. In eukaryotic cells, K+ channels
are involved in neural signalling and generation of the cardiac rhythm, and
act as effectors in signal transduction pathways involving G protein-
coupled receptors (GPCRs). In prokaryotic cells, they play a role in the
maintenance of ionic homeostasis [1].
 
Some types of K+ channel are closed at the resting potential of the cell,
but open on membrane depolarisation, and are thus known as voltage-gated 
channels. Each of these types of channel typically comprises 4 pore-forming
alpha subunits that may associate with one of a number of different types of
beta subunit. 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 KCNAB family of K+ channel beta subunits form tetramers arranged in
a similar manner to the pore forming alpha subunits. KCNAB subunits are
oxidoreductase enzymes, complete with nicotinamide (NADPH)-cofactors in 
their active sites. Changes in the oxidoreductase activity appear to 
markedly influence the gating mode of Kv channels, since mutations to the
catalytic residues in the active site lessen the inactivating activity of
KCNAB [2]. The KCNAB family is further divided into 3 subfamilies: KCNAB1
(Kvbeta3), KCNAB2 (Kvbeta2) and KCNAB3.
 
KCNAB2 associates with Kv1.4 alpha subunits; however, association has only
very modest effects on the gating of this channel [3]. Two isoforms of KCNAB2
exist, which are produced by alternative splicing of amino acids 26-39.
 
KCNAB2CHANEL is a 5-element fingerprint that provides a signature for the
KCNAB voltage-gated K+ channel beta-2 subunit. The fingerprint was derived 
from an initial alignment of 5 sequences: the motifs were drawn from 
conserved regions spanning the N- and C-terminal portions of the alignment.
A single iteration on SPTR39.22_17.3f was required to reach convergence, no
further sequences being identified beyond the starting set.
Summary Information
5 codes involving  5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
555555
400000
300000
200000
12345
True Positives
Q13303        Q27955        Q64284        Q9N0V9        
Q9PTM5
Sequence Titles
Q13303      VOLTAGE-GATED POTASSIUM CHANNEL BETA-2 SUBUNIT - Homo sapiens (Human). 
Q27955 VOLTAGE-GATED POTASSIUM CHANNEL BETA-2 SUBUNIT - Bos taurus (Bovine).
Q64284 VOLTAGE GATED POTASSIUM CHANNEL BETA-2 SUBUNIT - Mus musculus (Mouse), and Rattus norvegicus (Rat).
Q9N0V9 VOLTAGE-GATED POTASSIUM CHANNEL BETA-2 SUBUNIT - Oryctolagus cuniculus (Rabbit).
Q9PTM5 VOLTAGE-GATED POTASSIUM CHANNEL BETA-2 SUBUNIT - Xenopus laevis (African clawed frog).
Scan History
SPTR39.22_17.3f 1  50   NSINGLE    
Initial Motifs
Motif 1  width=13
Element Seqn Id St Int Rpt
MYPESTTGSPARL Q13303 1 1 -
MYPESTTGSPARL Q9N0V9 1 1 -
MYPESTTGSPARL Q27955 1 1 -
MYPESTTGSPARL Q64284 1 1 -
MYPESTTDSPARL Q9PTM5 1 1 -

Motif 2 width=12
Element Seqn Id St Int Rpt
SLRQTGSPGMIY Q13303 14 0 -
SLRQTGSPGMIY Q9N0V9 14 0 -
SLRQTGSPGMIY Q27955 14 0 -
SLRQTGSPGMIY Q64284 14 0 -
SLRQTGSPGMIY Q9PTM5 14 0 -

Motif 3 width=13
Element Seqn Id St Int Rpt
STRYGSPKRQLQF Q13303 26 0 -
STRYGSPKRQLQF Q9N0V9 26 0 -
STRYGSPKRQLQF Q27955 26 0 -
STRYGSPKRQLQF Q64284 26 0 -
SARYGSPKRQLQF Q9PTM5 26 0 -

Motif 4 width=13
Element Seqn Id St Int Rpt
SGIPPYSRASLKG Q13303 257 218 -
SGIPPYSRASLKG Q9N0V9 257 218 -
SGIPPYSRASLKG Q27955 257 218 -
SGIPPYSRASLKG Q64284 257 218 -
GGIPPYSRASLKG Q9PTM5 257 218 -

Motif 5 width=11
Element Seqn Id St Int Rpt
LSSSIIHEIDS Q13303 343 73 -
LSSSIIHEIDS Q9N0V9 343 73 -
LSSSIIHEIDS Q27955 343 73 -
LSSSIVHEIDS Q64284 343 73 -
LSSSIIHEIDG Q9PTM5 343 73 -
Final Motifs
Motif 1  width=13
Element Seqn Id St Int Rpt
MYPESTTGSPARL Q13303 1 1 -
MYPESTTGSPARL Q9N0V9 1 1 -
MYPESTTGSPARL Q27955 1 1 -
MYPESTTGSPARL Q64284 1 1 -
MYPESTTDSPARL Q9PTM5 1 1 -

Motif 2 width=12
Element Seqn Id St Int Rpt
SLRQTGSPGMIY Q13303 14 0 -
SLRQTGSPGMIY Q9N0V9 14 0 -
SLRQTGSPGMIY Q27955 14 0 -
SLRQTGSPGMIY Q64284 14 0 -
SLRQTGSPGMIY Q9PTM5 14 0 -

Motif 3 width=13
Element Seqn Id St Int Rpt
STRYGSPKRQLQF Q13303 26 0 -
STRYGSPKRQLQF Q9N0V9 26 0 -
STRYGSPKRQLQF Q27955 26 0 -
STRYGSPKRQLQF Q64284 26 0 -
SARYGSPKRQLQF Q9PTM5 26 0 -

Motif 4 width=13
Element Seqn Id St Int Rpt
SGIPPYSRASLKG Q13303 257 218 -
SGIPPYSRASLKG Q9N0V9 257 218 -
SGIPPYSRASLKG Q27955 257 218 -
SGIPPYSRASLKG Q64284 257 218 -
GGIPPYSRASLKG Q9PTM5 257 218 -

Motif 5 width=11
Element Seqn Id St Int Rpt
LSSSIIHEIDS Q13303 343 73 -
LSSSIIHEIDS Q9N0V9 343 73 -
LSSSIIHEIDS Q27955 343 73 -
LSSSIVHEIDS Q64284 343 73 -
LSSSIIHEIDG Q9PTM5 343 73 -