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PR01515

Identifier
KV22CHANNEL  [View Relations]  [View Alignment]  
Accession
PR01515
No. of Motifs
7
Creation Date
19-JUN-2001
Title
Kv2.2 voltage-gated K+ channel signature
Database References
PRINTS; PR00169 KCHANNEL; PR01491 KVCHANNEL; PR01495 SHABCHANNEL
Literature References
1. MILLER, C.
An overview of the potassium channel family.
GENOME BIOL. 1(4) 1-5 (2000).
 
2. ASHCROFT, F.M.
Voltage-gated K+ channels.
IN ION CHANNELS AND DISEASE, ACADEMIC PRESS, 2000, PP.97-123.
 
3. SANSOM, M.S.
Putting the parts together.
CURR.BIOL. 9(19) R738-R741 (1999).   
 
4. CONLEY, E.C. AND BRAMMAR, W.J.
Shab.
IN THE ION CHANNEL FACTSBOOK, VOLUME IV, ACADEMIC PRESS, 1999, PP.524-558.

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].
      
Structurally, Kv channels belong to the subfamily of K+ channels whose
subunits contain 6 transmembrane (TM) domains: these are the voltage-
gated K+ (Kv) channels, the KCNQ channels, the EAG-like K+ channels and
3 kinds of Ca2+-activated K+ channels (BK, IK and SK) [2]. All K+
channels share a characteristic sequence feature: a TMxTVGYG motif
that resides between the 2 C-terminal membrane spanning helices, and
forms the K+-selective pore domain [1-2].
     
The Kv family can be divided into 4 subfamilies on the basis of sequence
similarity and function: Shaker (Kv1), Shab (Kv2), Shaw (Kv3) and Shal 
(Kv4). All consist of pore-forming alpha subunits that associate with 
different types of beta subunit. To form a functional K+ channel pore,
4 alpha subunits and 4 beta subunits are required. The alpha subunits
have 6 well-conserved TM domains, a pore loop region and variable length
N- and C-termini. TM domains 5 and 6, and the loop region, form the K+ 
channel pore through which the K+ ions pass [3].
    
The Shab voltage-gated delayed rectifier K+ channels (also known as Kv2 
channels) are responsible for much of the delayed rectifier current in 
Drosophila nervous system and muscle. However, in vertebrates, Kv2 channels
have largely undetermined roles in the delayed rectifier currents of the 
heart and skeletal muscle. Kv2 channels can be further divided into 2
subtypes, designated Kv2.1 and Kv2.2 [4].
 
The first Kv2.2 channel was cloned from rat and was originally referred to
as the circumvillate papilla delayed rectifying K+ channel or cDRK. Several 
mammalian channels have subsequently been found and, together with the rat 
Kv2.2 channel, form a small subfamily. They are predominantly expressed in 
the interneurones; however, their roles are largely undetermined [4]. 
 
KV22CHANNEL is a 7-element fingerprint that provides a signature for the
Kv2.2 voltage-gated K+ channel. The fingerprint was derived from an initial
alignment of 4 sequences: the motifs were drawn from conserved regions
spanning the C-terminal third of the alignment, focusing on those sections
that characterise the Kv2.2 channel but distinguish it from other members of
the Shab channel family. A single iteration on SPTR39_15f was required to
reach convergence, no further sequences being identified beyond the starting
set. Several partial matches were found, all of which are closely related
members of the Shab family that match 2 or 3 motifs.
Summary Information
   4 codes involving  7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
3 codes involving 3 elements
5 codes involving 2 elements
Composite Feature Index
74444444
60000000
50000000
40000000
33030003
23020104
1234567
True Positives
CIKB_CANFA    CIKB_HUMAN    CIKB_RAT      Q91592        
True Positive Partials
Codes involving 3 elements
CIKA_HUMAN Q14193 Q9MZ19
Codes involving 2 elements
CIKA_RAT O18868 Q03717 Q91593
Q9S7T0
Sequence Titles
CIKB_CANFA  DELAYED RECTIFIER POTASSIUM CHANNEL PROTEIN - CANIS FAMILIARIS (DOG). 
CIKB_HUMAN VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN KV2.2 - Homo sapiens (Human).
CIKB_RAT VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN KV2.2 (CDRK) - Rattus norvegicus (Rat).
Q91592 POTASSIUM CHANNEL ALPHA SUBUNIT KV2.2 - Xenopus laevis (African clawed frog).

CIKA_HUMAN VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN KV2.1 (DHK1) - Homo sapiens (Human).
Q14193 H-DRK1 K(+) CHANNEL (DJ791K14.1) (POTASSIUM VOLTAGE-GATED CHANNEL, SHAB-RELATED SUBFAMILY, MEMBER 1) - Homo sapiens (Human).
Q9MZ19 VOLTAGE-GATED POTASSIUM CHANNEL KV2.1 - Oryctolagus cuniculus (Rabbit).

CIKA_RAT VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN KV2.1 (DRK1) - Rattus norvegicus (Rat).
O18868 DELAYED RECTIFIER POTASSIUM CHANNEL KV2.1 - Sus scrofa (Pig).
Q03717 POTASSIUM CHANNEL PROTEIN - Mus musculus (Mouse).
Q91593 POTASSIUM CHANNEL ALPHA SUBUNIT KV2.1 - Xenopus laevis (African clawed frog).
Q9S7T0 F28J7.11 PROTEIN - Arabidopsis thaliana (Mouse-ear cress).
Scan History
SPTR39_15f 1  80   NSINGLE    
Initial Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
KAGESANTKDSADDN CIKB_HUMAN 471 471 -
KAGESANIKDSVDDN CIKB_RAT 471 471 -
KAGESSSTKDSADDN CIKB_CANFA 471 471 -
KSEDGSNKMEKPSDN Q91592 471 471 -

Motif 2 width=16
Element Seqn Id St Int Rpt
YQEVSQKDSHEQLNNT CIKB_HUMAN 512 26 -
YQEVSQKDSHEQLNNT CIKB_RAT 512 26 -
YQEVSQKDSHEQLNNT CIKB_CANFA 512 26 -
YQEVSQHDSQEQLNNA Q91592 512 26 -

Motif 3 width=15
Element Seqn Id St Int Rpt
QKLEMLYNEITKTQP CIKB_HUMAN 538 10 -
QKLEMLYNEITKTQT CIKB_RAT 538 10 -
QKLEMLYNEITKTQP CIKB_CANFA 538 10 -
QKLEELYNEITKAQS Q91592 537 9 -

Motif 4 width=11
Element Seqn Id St Int Rpt
NPDCQEKPERP CIKB_HUMAN 557 4 -
NPDCQEQPERP CIKB_RAT 557 4 -
NPDGQEQPDRP CIKB_CANFA 557 4 -
NSSFQEQAAVP Q91592 556 4 -

Motif 5 width=15
Element Seqn Id St Int Rpt
EEEIEMEEVVCPQEQ CIKB_HUMAN 571 3 -
EEEIEMEEVVCPQEQ CIKB_RAT 571 3 -
EEEIEMEEVVCPQEQ CIKB_CANFA 571 3 -
EEEIEMEEVSTKKTQ Q91592 570 3 -

Motif 6 width=18
Element Seqn Id St Int Rpt
SPLPPPSASHLQMKFPTD CIKB_HUMAN 619 33 -
SPLPPPSASHLQMKFPTD CIKB_RAT 619 33 -
SPLPPLSASHLQMRFPPD CIKB_CANFA 619 33 -
SPLTPYPGSNLEIRFPSY Q91592 618 33 -

Motif 7 width=13
Element Seqn Id St Int Rpt
PLKSRSLKVNFKE CIKB_HUMAN 709 72 -
PLKSRSLKVNFQE CIKB_RAT 705 68 -
PLKSRSLRVNFKE CIKB_CANFA 709 72 -
PLRSRSLKVNFKN Q91592 705 69 -
Final Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
KAGESANTKDSADDN CIKB_HUMAN 471 471 -
KAGESANIKDSVDDN CIKB_RAT 471 471 -
KAGESSSTKDSADDN CIKB_CANFA 471 471 -
KSEDGSNKMEKPSDN Q91592 471 471 -

Motif 2 width=16
Element Seqn Id St Int Rpt
YQEVSQKDSHEQLNNT CIKB_HUMAN 512 26 -
YQEVSQKDSHEQLNNT CIKB_RAT 512 26 -
YQEVSQKDSHEQLNNT CIKB_CANFA 512 26 -
YQEVSQHDSQEQLNNA Q91592 512 26 -

Motif 3 width=15
Element Seqn Id St Int Rpt
QKLEMLYNEITKTQP CIKB_HUMAN 538 10 -
QKLEMLYNEITKTQT CIKB_RAT 538 10 -
QKLEMLYNEITKTQP CIKB_CANFA 538 10 -
QKLEELYNEITKAQS Q91592 537 9 -

Motif 4 width=11
Element Seqn Id St Int Rpt
NPDCQEKPERP CIKB_HUMAN 557 4 -
NPDCQEQPERP CIKB_RAT 557 4 -
NPDGQEQPDRP CIKB_CANFA 557 4 -
NSSFQEQAAVP Q91592 556 4 -

Motif 5 width=15
Element Seqn Id St Int Rpt
EEEIEMEEVVCPQEQ CIKB_HUMAN 571 3 -
EEEIEMEEVVCPQEQ CIKB_RAT 571 3 -
EEEIEMEEVVCPQEQ CIKB_CANFA 571 3 -
EEEIEMEEVSTKKTQ Q91592 570 3 -

Motif 6 width=18
Element Seqn Id St Int Rpt
SPLPPPSASHLQMKFPTD CIKB_HUMAN 619 33 -
SPLPPPSASHLQMKFPTD CIKB_RAT 619 33 -
SPLPPLSASHLQMRFPPD CIKB_CANFA 619 33 -
SPLTPYPGSNLEIRFPSY Q91592 618 33 -

Motif 7 width=13
Element Seqn Id St Int Rpt
PLKSRSLKVNFKE CIKB_HUMAN 709 72 -
PLKSRSLKVNFQE CIKB_RAT 705 68 -
PLKSRSLRVNFKE CIKB_CANFA 709 72 -
PLRSRSLKVNFKN Q91592 705 69 -