SPRINT Home UMBER Home Contents Standard Search Advanced Search Relation Search

==SPRINT==> PRINTS View



  selected as


PR01696

Identifier
LCACHANNELB3  [View Relations]  [View Alignment]  
Accession
PR01696
No. of Motifs
4
Creation Date
13-MAR-2002
Title
L-type calcium channel beta-3 subunit signature
Database References
PRINTS; PR00167 CACHANNEL; PR01626 LCACHANNELB
Literature References
1. PICHLER, M., CASSIDY, T.N., REIMER, D., HAASE, H., KRAUS, R., OSTLER, D.
AND STRIESSNIG, J.
Beta subunit heterogeneity in neuronal L-type calcium channels.
J.BIOL.CHEM. 272(21) 13877-13882 (1997).
 
2. BRAMMAR, W.J.
VLG Ca.
IN THE ION CHANNEL FACTSBOOK, VOLUME IV, ACADEMIC PRESS, 1999, PP.22-153.
 
3. NEUHUBER, B., GERSTER, U., DORING, F., GLOSSMANN, H., TANABE, T. AND
FLUCHER, B.E.
Association of calcium channel alpha-1s and beta-1a subunits is required for
gr; 
the targeting of beta-1a but not of alpha-1s into skeletal muscle triads.
PROC.NATL.ACAD.SCI.U.S.A. 95 5015-5020 (1998).
 
4. CASTELLANO, A., WEI, X., BIRNBAUMER, L. AND PEREZ-REYES, E.
Cloning and expression of a third calcium channel beta subunit.
J.BIOL.CHEM. 15 268(5) 3450-3455 (1993).
 
5. SMITH, S.M., PIEDRAS-RENTERA, E.S., NAMKUNG, Y., SHIN, H.S. AND
TSIEN, R.W.
Neuronal voltage-activated calcium channels: on the roles of the alpha 1E
and beta-3 subunits.
ANN.NY.ACAD.SCI. 30 868 175-198 (1999).

Documentation
Calcium channels are generally discriminated by their biophysical and/or
pharmacological sensitivity. L-type calcium channels are distinguished by
their modulation by compounds such as dihydropyridines. These channels
tend to be localised mainly around the neuronal cell body, where they
influence calcium-dependent modulation and excitation-transcription coupling,
but are also found in skeletal and cardiac muscle, where they play a role in
excitation-contraction coupling and action potential shaping, respectively.
                  
L-type calcium channnels are formed from different alpha-1 subunit isoforms
that determine the pharmacological properties of the channel, since they
form the drug binding domain. Other properties, such as gating voltage-
dependence, G protein modulation and kinase susceptibility, are influenced 
by alpha-2, delta and beta subunits [1].
                  
Co-expression of beta subunit mRNA with alpha-1 subunit mRNA in Xenopus
oocytes produces increased calcium currents, which are accompanied by a
shift in the voltage-dependence of activation to more negative membrane
potentials. Conversely, microinjection of antisense oligonucleotides to 
beta subunit mRNA produces decreased calcium currents and shifts voltage-
dependent activation to more positive membrane potentials. There are
four distinct beta subunits: beta-1, beta-2, beta-3 and beta-4; and the
magnitude of these effects varies with the particular subtype [2].
 
Beta-3 subunits are most abundant in the brain, but are also present in
aorta, trachea, lung, heart, skeletal muscle and pancreatic islets, where
they play a role in the regulation of insulin secretion [4]. The beta-3
subunits regulate the activation (opening) and inactivation (closing)
kinetics through phosphorylation and dephosphorylation. However, it is noted
that no single channel is dependent on the beta-3 subunit [5].
 
LCACHANNELB3 is a 4-element fingerprint that provides a signature for the
L-type calcium channel beta-3 subunit. The fingerprint was derived from an
initial alignment of 6 sequences: the motifs were drawn from conserved
regions spanning virtually the full alignment length, focusing on those
sections that characterise the beta-3 subunits but distinguish them from the
rest of the L-type calcium channel beta subunits - motifs 1 and 2 reside at
the N-terminus; and motifs 3 and 4 at the C-terminus. Two iterations on
SPTR40_18f were required to reach convergence, at which point a true set
comprising 8 sequences was identified. A single partial match was also
found, O57653, a beta-3 subunit from Fugu rubripes that matches motifs 2-4.
Summary Information
   8 codes involving  4 elements
1 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
48888
30111
20000
1234
True Positives
CCB3_HUMAN    CCB3_MOUSE    CCB3_RABIT    CCB3_RAT      
Q91629 Q91630 Q9MZL3 Q9QVV3
True Positive Partials
Codes involving 3 elements
O57653
Sequence Titles
CCB3_HUMAN  Dihydropyridine-sensitive L-type, calcium channel beta-3 subunit (CAB3A/CAB3B) - Homo sapiens (Human). 
CCB3_MOUSE Dihydropyridine-sensitive L-type, calcium channel beta-3 subunit (CAB3A/CAB3B) (CCHB3) - Mus musculus (Mouse).
CCB3_RABIT Dihydropyridine-sensitive L-type, calcium channel beta-3 subunit (CAB3) - Oryctolagus cuniculus (Rabbit).
CCB3_RAT Dihydropyridine-sensitive L-type, calcium channel beta-3 subunit - Rattus norvegicus (Rat).
Q91629 DIHYDROPYRIDINE-SENSITIVE L-TYPE, CALCIUM CHANNEL BETA-3 XO28 SUBUNIT - Xenopus laevis (African clawed frog).
Q91630 DIHYDROPYRIDINE-SENSITIVE L-TYPE, CALCIUM CHANNEL BETA-3 XO32 SUBUNIT - Xenopus laevis (African clawed frog).
Q9MZL3 VOLTAGE-DEPENDENT CALCIUM CHANNEL BETA3A SUBUNIT - Bos taurus (Bovine).
Q9QVV3 CA2+ CHANNEL BETA SUBUNIT 3B - Rattus sp.

O57653 CALCIUM CHANNEL BETA3 SUBUNIT - Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
Scan History
SPTR40_18f 2  300  NSINGLE    
Initial Motifs
Motif 1  width=18
Element Seqn Id St Int Rpt
MYDDSYVPGFEDSEAGSA CCB3_HUMAN 1 1 -
MYDDSYVPGFEDSEAGSA CCB3_MOUSE 1 1 -
MYDDSYVPGFEDSEAGSA CCB3_RAT 1 1 -
MYDDSYVPGFEDSEAGSA Q9MZL3 1 1 -
MYEDSYVPGFEDSEAGSA CCB3_RABIT 1 1 -
MYDDLYLHGFEDSEVGSA Q91629 1 1 -

Motif 2 width=14
Element Seqn Id St Int Rpt
ESARREVESQAQQQ CCB3_HUMAN 38 19 -
ESARREVESQAQQQ CCB3_MOUSE 38 19 -
ESARREVESQAQQQ CCB3_RAT 38 19 -
ESARREVESQAQQQ Q9MZL3 38 19 -
ESARREVESQAQQQ CCB3_RABIT 38 19 -
ETARREVERQAQQQ Q91629 38 19 -

Motif 3 width=21
Element Seqn Id St Int Rpt
GPGLLGPPSAIPGLQNQQLLG CCB3_HUMAN 366 314 -
GPGLLGPPSAIPGLQNQQQLG CCB3_MOUSE 366 314 -
GPGMLGPPSAIPGLQNQQLLG CCB3_RAT 366 314 -
ALGLLGPPSAIPGLQNQQLLG Q9MZL3 366 314 -
GPGLLGPPSAIPGLQSQQLLG CCB3_RABIT 366 314 -
SQNLITPPTAIPGLQNQELLS Q91629 366 314 -

Motif 4 width=19
Element Seqn Id St Int Rpt
HRQHTSGLPSANGHDPQDR CCB3_HUMAN 440 53 -
HRQHTSGLPSANGHDPQDR CCB3_MOUSE 440 53 -
HRQHTSGLPSANGHDPQDR CCB3_RAT 440 53 -
HRQHTSGLPSANGHDPQDR Q9MZL3 440 53 -
HRQHTSGLPSANGHDPQDR CCB3_RABIT 433 46 -
HRHHNSGLNSTNGHDSQDR Q91629 440 53 -
Final Motifs
Motif 1  width=18
Element Seqn Id St Int Rpt
MYDDSYVPGFEDSEAGSA CCB3_HUMAN 1 1 -
MYDDSYVPGFEDSEAGSA CCB3_MOUSE 1 1 -
MYDDSYVPGFEDSEAGSA CCB3_RAT 1 1 -
MYDDSYVPGFEDSEAGSA Q9QVV3 1 1 -
MYDDSYVPGFEDSEAGSA Q9MZL3 1 1 -
MYEDSYVPGFEDSEAGSA CCB3_RABIT 1 1 -
MYDDLYLHGFEDSEVGSA Q91629 1 1 -
MYEDLYLHGIEDSEVGSA Q91630 1 1 -

Motif 2 width=14
Element Seqn Id St Int Rpt
ESARREVESQAQQQ CCB3_HUMAN 38 19 -
ESARREVESQAQQQ CCB3_MOUSE 38 19 -
ESARREVESQAQQQ CCB3_RAT 38 19 -
ESARREVESQAQQQ Q9QVV3 38 19 -
ESARREVESQAQQQ Q9MZL3 38 19 -
ESARREVESQAQQQ CCB3_RABIT 38 19 -
ETARREVERQAQQQ Q91629 38 19 -
EAARREVERQAQEQ Q91630 38 19 -

Motif 3 width=21
Element Seqn Id St Int Rpt
GPGLLGPPSAIPGLQNQQLLG CCB3_HUMAN 366 314 -
GPGLLGPPSAIPGLQNQQQLG CCB3_MOUSE 366 314 -
GPGMLGPPSAIPGLQNQQLLG CCB3_RAT 366 314 -
GPGMLGPPSAIPGLQNQQLLG Q9QVV3 359 307 -
ALGLLGPPSAIPGLQNQQLLG Q9MZL3 366 314 -
GPGLLGPPSAIPGLQSQQLLG CCB3_RABIT 366 314 -
SQNLITPPTAIPGLQNQELLS Q91629 366 314 -
SPNLITPPTVIPGLQNQQPVS Q91630 366 314 -

Motif 4 width=19
Element Seqn Id St Int Rpt
HRQHTSGLPSANGHDPQDR CCB3_HUMAN 440 53 -
HRQHTSGLPSANGHDPQDR CCB3_MOUSE 440 53 -
HRQHTSGLPSANGHDPQDR CCB3_RAT 440 53 -
HRQHTSGLPSANGHDPQDR Q9QVV3 433 53 -
HRQHTSGLPSANGHDPQDR Q9MZL3 440 53 -
HRQHTSGLPSANGHDPQDR CCB3_RABIT 433 46 -
HRHHNSGLNSTNGHDSQDR Q91629 440 53 -
HRHHNSGLNSTNGHDSQDR Q91630 440 53 -