Cavβ3

Description: calcium channel, voltage-dependent, beta 3 subunit
Gene: cacnb3
Alias: cacnb3

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Introduction

Voltage dependent calcium channels (VDCC) auxiliary beta (Cavb1–4) and alpha2delta (Cava2d1–4) subunits associate with the alpha1 functional subunits (for review see Walker and De Waard, 1998 [1279]) and affect the biophysical properties of the alpha1 subunits as observed for the auxiliary subunits of voltage-dependent sodium and potassium channels (for review see Isom et al., 1994 [1247]; Trimmer, 1998 [1280]).

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Gene

CACNB3 (also known as CAB3; CACNLB3; FLJ58949) encodes beta 3 subunit of voltage dependent calcium channels.

http://www.ncbi.nlm.nih.gov/gene/784

Species	NCBI gene ID	Chromosome	Position
Human	784	12	14461
Mouse	12297	15	16100
Rat	25297	7	12275

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Transcript

Species	NCBI accession	Length (nt)
Human	NM_000725.4	2931
Mouse	NM_007581.3	2822
Rat	NM_012828.3	2521

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Protein Isoforms

Species	Uniprot ID	Length (aa)
Human	P54284	484
Mouse	P54285	484
Rat	P54287	484

Isoforms

Transcript

Length (nt)

Protein

Length (aa)

Variant

Isoform

Known

NM_001206917.2

2526

NP_001193846.1

471

transcript variant 4

isoform 4

NM_001206916.2

2607

NP_001193845.1

483

transcript variant 3

isoform 3

NM_000725.4

2931

NP_000716.2

484

transcript variant 1

isoform 1

NM_001206915.2

2808

NP_001193844.1

443

transcript variant 2

isoform 2

Predicted

XM_047429525.1

3758

XP_047285481.1

484

transcript variant X1

isoform X1

XM_047429527.1

2574

XP_047285483.1

308

transcript variant X3

isoform X2

XM_047429526.1

2541

XP_047285482.1

308

transcript variant X2

isoform X2

XM_047429529.1

1324

XP_047285485.1

271

transcript variant X6

isoform X3

XM_011538728.3

3349

XP_011537030.1

308

transcript variant X4

isoform X2

XM_047429528.1

2070

XP_047285484.1

308

transcript variant X5

isoform X2

XM_054373189.1

4634

XP_054229164.1

484

transcript variant X7

isoform X1

XM_054373191.1

2574

XP_054229166.1

308

transcript variant X3

isoform X2

XM_054373190.1

2541

XP_054229165.1

308

transcript variant X2

isoform X2

XM_054373194.1

1324

XP_054229169.1

271

transcript variant X6

isoform X3

XM_054373192.1

3349

XP_054229167.1

308

transcript variant X4

isoform X2

XM_054373193.1

2070

XP_054229168.1

308

transcript variant X5

isoform X2

Known

NM_001044741.2

2568

NP_001038206.1

483

transcript variant 2

isoform 2

NM_001356543.1

2565

NP_001343472.1

482

transcript variant 4

isoform 4

NM_007581.3

2822

NP_031607.2

484

transcript variant 1

isoform 1

NM_001286226.1

2741

NP_001273155.1

457

transcript variant 3

isoform 3

NM_001410382.1

2530

NP_001397311.1

489

isoform 5

NM_001410383.1

2527

NP_001397312.1

488

isoform 6

NM_001410384.1

2816

NP_001397313.1

483

isoform 7

Predicted

XM_017316418.3

2448

XP_017171907.1

477

transcript variant X16

isoform X10

XM_006520365.2

2508

XP_006520428.1

477

transcript variant X13

isoform X10

XM_036159101.1

2291

XP_036014994.1

471

transcript variant X15

isoform X12

XM_030248302.2

3334

XP_030104162.1

490

transcript variant X2

isoform X1

XM_030248304.2

3228

XP_030104164.1

490

transcript variant X4

isoform X1

XM_006520367.2

2411

XP_006520430.1

314

transcript variant X17

isoform X13

XM_006520360.2

2532

XP_006520423.1

489

transcript variant X5

isoform X2

XM_006520362.5

2400

XP_006520425.1

488

transcript variant X7

isoform X4

XM_017316415.3

3284

XP_017171904.1

490

transcript variant X1

isoform X1

XM_030248303.2

3214

XP_030104163.1

490

transcript variant X3

isoform X1

XM_036159097.1

3635

XP_036014990.1

484

transcript variant X8

isoform X5

XM_030248306.2

2374

XP_030104166.1

314

transcript variant X19

isoform X13

XM_036159102.1

2371

XP_036014995.1

314

transcript variant X20

isoform X13

XM_030248307.2

2350

XP_030104167.1

308

transcript variant X24

isoform X14

XM_036159104.1

3432

XP_036014997.1

308

transcript variant X22

isoform X14

XM_036159100.1

3208

XP_036014993.1

475

transcript variant X14

isoform X11

XM_006520361.4

3108

XP_006520424.1

489

transcript variant X6

isoform X3

XM_006520363.4

3217

XP_006520426.1

484

transcript variant X9

isoform X6

XM_006520364.4

3207

XP_006520427.1

481

transcript variant X11

isoform X8

XM_036159098.1

3084

XP_036014991.1

483

transcript variant X10

isoform X7

XM_036159106.1

2990

XP_036014999.1

245

transcript variant X25

isoform X15

XM_030248305.2

3077

XP_030104165.1

314

transcript variant X18

isoform X13

XM_036159105.1

3048

XP_036014998.1

308

transcript variant X23

isoform X14

XM_036159103.1

3247

XP_036014996.1

308

transcript variant X21

isoform X14

XM_036159099.1

2286

XP_036014992.1

478

transcript variant X12

isoform X9

Known

NM_012828.3

2521

NP_036960.1

484

Predicted

XM_006257329.4

2579

XP_006257391.1

483

transcript variant X2

isoform X2

XM_017594673.2

2590

XP_017450162.1

495

transcript variant X1

isoform X1

XM_039078460.1

1045

XP_038934388.1

282

transcript variant X3

isoform X3

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Post-Translational Modifications

PTM

Position

Type

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Structure

High-voltage–activated calcium channels are comprised of a pore-forming alpha1 subunit, auxiliary beta and alpha2delta subunits, and, in some cases, an auxiliary gamma subunit (for review see Catterall, 2000 [477]).

The b subunit has been shown to interact with alpha1 subunit interaction domain (AID) in the cytoplasmic I-II linker of alpha1 subunit (Pragnell et al., 1994 [1290]; Witcher et al., 1995 [1291]), and all four beta subunits interacted with AID of Cav2.2-alpha-1 in vitro with high affinity (Kd of 5nM; Scott et al., 1996 [1292]).

Cavβ3 predicted AlphaFold size

Species	Area (Å²)	Reference
Human	4902.29	source
Mouse	6701.49	source
Rat	6120.49	source

Methodology for AlphaFold size prediction and disclaimer are available here

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Function

It has been shown that b auxiliary subunits increase current amplitude in voltage-dependent calcium channels (Mori et al., 1991; Neely et al., 1993 [1241]; Wakamori et al., 1993 [1286]; Jones et al., 1998 [1266]; Klugbauer et al., 1999 [1289]). However, Yasuda et al. [92] found a novel inhibitory effect of b3 subunit on macroscopic Ba2+ currents through recombinant N- and R-type calcium channels expressed in Xenopus oocytes.

Coexpression of beta subunits enhanced the level of channel expression in the plasma membrane (Williams et al., 1992 [1281]; Brust et al., 1993 [1282]) by chaperoning the translocation of alpha1 subunits (Chien et al., 1995 [1261]; Yamaguchi et al., 1998 [238]; Gao et al., 1999 [1283]; Gerster et al., 1999 [1284]) from ER where beta subunits antagonize the binding between alpha1 and an ER retention protein (Bichet et al., 2000 [1285]). In addition, beta subunits also increased channel open probability without affecting single-channel conductance (Neely et al., 1993 [1221]; Wakamori et al., 1993 [1286], 1999 [1287]; Jones et al., 1998 [1266]; Gerster et al., 1999 [1284]; Hohaus et al., 2000 [1288]). A hyperpolarizing shift of I-V relationships by beta subunits (Neely et al., 1993 [1241]; Yamaguchi et al., 1998 [238]) also partially contributes to an increase in macroscopic current amplitude.

References

Yasuda T et al. Overexpressed Ca(v)beta3 inhibits N-type (Cav2.2) calcium channel currents through a hyperpolarizing shift of ultra-slow and closed-state inactivation.
J. Gen. Physiol., 2004 Apr , 123 (401-16).

238

Yamaguchi H et al. Multiple modulation pathways of calcium channel activity by a beta subunit. Direct evidence of beta subunit participation in membrane trafficking of the alpha1C subunit.
J. Biol. Chem., 1998 Jul 24 , 273 (19348-56).

477

Catterall WA Structure and regulation of voltage-gated Ca2+ channels.
Annu. Rev. Cell Dev. Biol., 2000 , 16 (521-55).

1221

Neely A et al. Potentiation by the beta subunit of the ratio of the ionic current to the charge movement in the cardiac calcium channel.
Science, 1993 Oct 22 , 262 (575-8).

1247

Isom LL et al. Auxiliary subunits of voltage-gated ion channels.
Neuron, 1994 Jun , 12 (1183-94).

1261

Chien AJ et al. Roles of a membrane-localized beta subunit in the formation and targeting of functional L-type Ca2+ channels.
J. Biol. Chem., 1995 Dec 15 , 270 (30036-44).

1266

Jones LP et al. Mechanism of auxiliary subunit modulation of neuronal alpha1E calcium channels.
J. Gen. Physiol., 1998 Aug , 112 (125-43).

1279

Walker D et al. Subunit interaction sites in voltage-dependent Ca2+ channels: role in channel function.
Trends Neurosci., 1998 Apr , 21 (148-54).

1280

Trimmer JS Regulation of ion channel expression by cytoplasmic subunits.
Curr. Opin. Neurobiol., 1998 Jun , 8 (370-4).

1281

Williams ME et al. Structure and functional expression of an omega-conotoxin-sensitive human N-type calcium channel.
Science, 1992 Jul 17 , 257 (389-95).

1282

Brust PF et al. Human neuronal voltage-dependent calcium channels: studies on subunit structure and role in channel assembly.
Neuropharmacology, 1993 Nov , 32 (1089-102).

1283

Gao B et al. Functional properties of a new voltage-dependent calcium channel alpha(2)delta auxiliary subunit gene (CACNA2D2).
J. Biol. Chem., 2000 Apr 21 , 275 (12237-42).

1284

Gerster U et al. Current modulation and membrane targeting of the calcium channel alpha1C subunit are independent functions of the beta subunit.
J. Physiol. (Lond.), 1999 Jun 1 , 517 ( Pt 2) (353-68).

1285

Bichet D et al. The I-II loop of the Ca2+ channel alpha1 subunit contains an endoplasmic reticulum retention signal antagonized by the beta subunit.
Neuron, 2000 Jan , 25 (177-90).

1286

Wakamori M et al. Auxiliary subunits operate as a molecular switch in determining gating behaviour of the unitary N-type Ca2+ channel current in Xenopus oocytes.
J. Physiol. (Lond.), 1999 Jun 15 , 517 ( Pt 3) (659-72).

1287

Wakamori M et al. Single-channel analysis of a cloned human heart L-type Ca2+ channel alpha 1 subunit and the effects of a cardiac beta subunit.
Biochem. Biophys. Res. Commun., 1993 Nov 15 , 196 (1170-6).

1288

Hohaus A et al. Modulation of the smooth-muscle L-type Ca2+ channel alpha1 subunit (alpha1C-b) by the beta2a subunit: a peptide which inhibits binding of beta to the I-II linker of alpha1 induces functional uncoupling.
Biochem. J., 2000 Jun 15 , 348 Pt 3 (657-65).

1289

Klugbauer N et al. Molecular diversity of the calcium channel alpha2delta subunit.
J. Neurosci., 1999 Jan 15 , 19 (684-91).

1290

Pragnell M et al. Calcium channel beta-subunit binds to a conserved motif in the I-II cytoplasmic linker of the alpha 1-subunit.
Nature, 1994 Mar 3 , 368 (67-70).

1291

Witcher DR et al. Association of native Ca2+ channel beta subunits with the alpha 1 subunit interaction domain.
J. Biol. Chem., 1995 Jul 28 , 270 (18088-93).

1292

Scott VE et al. Beta subunit heterogeneity in N-type Ca2+ channels.
J. Biol. Chem., 1996 Feb 9 , 271 (3207-12).

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Credits

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