Reviewed, UniProtKB/Swiss-Prot Q8R0S4 (CACB4_MOUSE)

Names and origin

Protein names

Recommended name:
    Voltage-dependent L-type calcium channel subunit beta-4
      Short name=CAB4
Alternative name(s):
    Calcium channel voltage-dependent subunit beta 4

Gene names

Name:	Cacnb4
Synonyms:	Cacnlb4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting By similarity.
Subunit structure	The L-type calcium channel is composed of four subunits: alpha-1, alpha-2, beta and gamma By similarity.
Sequence similarities	Belongs to the calcium channel beta subunit family. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Coding sequence diversity	Alternative splicing
Domain	SH3 domain
Ligand	Calcium
Molecular function	Calcium channel Ionic channel Voltage-gated channel
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	Peyer's patch development Inferred from mutant phenotype. Source: MGI T cell receptor signaling pathway Inferred from mutant phenotype. Source: MGI adult walking behavior Inferred from mutant phenotype. Source: MGI cAMP metabolic process Inferred from mutant phenotype. Source: MGI calcium ion transport Inferred from mutant phenotype. Source: MGI cellular calcium ion homeostasis Inferred from mutant phenotype. Source: MGI gamma-aminobutyric acid secretion Inferred from mutant phenotype. Source: MGI gamma-aminobutyric acid signaling pathway Inferred from mutant phenotype. Source: MGI neuromuscular junction development Inferred from mutant phenotype. Source: MGI neuronal action potential propagation Inferred from mutant phenotype. Source: MGI regulation of membrane potential Inferred from mutant phenotype. Source: MGI spleen development Inferred from mutant phenotype. Source: MGI synaptic transmission, glutamatergic Inferred from mutant phenotype. Source: MGI thymus development Inferred from mutant phenotype. Source: MGI
Cellular component	voltage-gated calcium channel complex Inferred from direct assay. Source: MGI
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW high voltage-gated calcium channel activity Traceable author statement. Source: MGI protein binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: Q8R0S4-3)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: Q8R0S4-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MSSSYGKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTSTSFILRQ → MYDNLYLHGVEDSEA

Isoform 2 (identifier: Q8R0S4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MSSSYGKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTSTSFILRQ → MA

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 519

519

Voltage-dependent L-type calcium channel subunit beta-4

PRO_0000144061

Regions

Domain

98 – 160

63

SH3

Amino acid modifications

Modified residue

38

1

Phosphoserine Ref.6

Modified residue

404

1

Phosphoserine Ref.4

Modified residue

405

1

Phosphoserine Ref.6

Modified residue

410

1

Phosphothreonine Ref.4

Modified residue

507

1

Phosphoserine Ref.5

Natural variations

Alternative sequence

1 – 48

48

MSSSY…FILRQ → MYDNLYLHGVEDSEA in isoform 1.

VSP_022599

Alternative sequence

1 – 48

48

MSSSY…FILRQ → MA in isoform 2.

VSP_010737

Experimental info

Sequence conflict

492

1

P → A in BAC31681. Ref.2

Secondary structure

1

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519

Helix Strand Turn

Details...

Helix

72 – 88

17

Beta strand

94 – 100

7

Beta strand

124 – 132

9

Beta strand

135 – 142

8

Beta strand

148 – 151

4

Helix

153 – 161

9

Turn

162 – 164

3

Beta strand

211 – 215

5

Beta strand

221 – 224

4

Helix

232 – 248

17

Turn

249 – 251

3

Beta strand

252 – 258

7

Helix

262 – 264

3

Helix

288 – 302

15

Beta strand

307 – 312

6

Helix

318 – 321

4

Beta strand

329 – 333

5

Helix

338 – 346

9

Helix

350 – 353

4

Helix

356 – 367

12

Helix

371 – 373

3

Beta strand

375 – 378

4

Beta strand

380 – 382

3

Helix

383 – 401

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 663A88C7BCF7E90C	FASTA	519	57,950
	10 20 30 40 50 60 MSSSYGKNGA ADGPHSPSSQ VARGTTTRRS RLKRSDGSTT STSFILRQGS ADSYTSRPSD 70 80 90 100 110 120 SDVSLEEDRE AIRQEREQQA AIQLERAKSK PVAFAVKTNV SYCGALDEDV PVPSTAISFD 130 140 150 160 170 180 AKDFLHIKEK YNNDWWIGRL VKEGCEIGFI PSPLRLENIR IQQEQKRGRF HGGKSSGNSS 190 200 210 220 230 240 SSLGEMVSGT FRATPTTTAK QKQKVTEHIP PYDVVPSMRP VVLVGPSLKG YEVTDMMQKA 250 260 270 280 290 300 LFDFLKHRFD GRISITRVTA DISLAKRSVL NNPSKRAIIE RSNTRSSLAE VQSEIERIFE 310 320 330 340 350 360 LARSLQLVVL DADTINHPAQ LIKTSLAPII VHVKVSSPKV LQRLIKSRGK SQSKHLNVQL 370 380 390 400 410 420 VAADKLAQCP PEMFDVILDE NQLEDACEHL GEYLEAYWRA THTSSSTPMT PLLGRNVGST 430 440 450 460 470 480 ALSPYPTAIS GLQSQRMRHS NHSTENSPIE RRSLMTSDEN YHNERARKSR NRLSSSSQHS 490 500 510 RDHYPLVEED YPDSYQDTYK PHRNRGSPGG CSHDSRHRL
	Isoform 1. Checksum: F4FCDD8810D75696	FASTA	486	54,619
	10 20 30 40 50 60 MYDNLYLHGV EDSEAGSADS YTSRPSDSDV SLEEDREAIR QEREQQAAIQ LERAKSKPVA 70 80 90 100 110 120 FAVKTNVSYC GALDEDVPVP STAISFDAKD FLHIKEKYNN DWWIGRLVKE GCEIGFIPSP 130 140 150 160 170 180 LRLENIRIQQ EQKRGRFHGG KSSGNSSSSL GEMVSGTFRA TPTTTAKQKQ KVTEHIPPYD 190 200 210 220 230 240 VVPSMRPVVL VGPSLKGYEV TDMMQKALFD FLKHRFDGRI SITRVTADIS LAKRSVLNNP 250 260 270 280 290 300 SKRAIIERSN TRSSLAEVQS EIERIFELAR SLQLVVLDAD TINHPAQLIK TSLAPIIVHV 310 320 330 340 350 360 KVSSPKVLQR LIKSRGKSQS KHLNVQLVAA DKLAQCPPEM FDVILDENQL EDACEHLGEY 370 380 390 400 410 420 LEAYWRATHT SSSTPMTPLL GRNVGSTALS PYPTAISGLQ SQRMRHSNHS TENSPIERRS 430 440 450 460 470 480 LMTSDENYHN ERARKSRNRL SSSSQHSRDH YPLVEEDYPD SYQDTYKPHR NRGSPGGCSH DSRHRL
	Isoform 2. Checksum: 1EA0EE1CA4264A65	FASTA	473	53,084
	10 20 30 40 50 60 MAGSADSYTS RPSDSDVSLE EDREAIRQER EQQAAIQLER AKSKPVAFAV KTNVSYCGAL 70 80 90 100 110 120 DEDVPVPSTA ISFDAKDFLH IKEKYNNDWW IGRLVKEGCE IGFIPSPLRL ENIRIQQEQK 130 140 150 160 170 180 RGRFHGGKSS GNSSSSLGEM VSGTFRATPT TTAKQKQKVT EHIPPYDVVP SMRPVVLVGP 190 200 210 220 230 240 SLKGYEVTDM MQKALFDFLK HRFDGRISIT RVTADISLAK RSVLNNPSKR AIIERSNTRS 250 260 270 280 290 300 SLAEVQSEIE RIFELARSLQ LVVLDADTIN HPAQLIKTSL APIIVHVKVS SPKVLQRLIK 310 320 330 340 350 360 SRGKSQSKHL NVQLVAADKL AQCPPEMFDV ILDENQLEDA CEHLGEYLEA YWRATHTSSS 370 380 390 400 410 420 TPMTPLLGRN VGSTALSPYP TAISGLQSQR MRHSNHSTEN SPIERRSLMT SDENYHNERA 430 440 450 460 470 RKSRNRLSSS SQHSRDHYPL VEEDYPDSYQ DTYKPHRNRG SPGGCSHDSR HRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structures of the murine genes for the beta1- and beta4-Subunits of the voltage-dependent calcium channel." Murakami M., Miyoshi I., Suzuki T., Sasano H., Iijima T. J. Mol. Neurosci. 21:13-22(2003) [PubMed: 14500989] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Strain: C57BL/6J. Tissue: Brain cortex, Hypothalamus and Spinal cord.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye.
[4]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed: 15572359] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404 AND THR-410, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-405, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB100402 Genomic DNA. Translation: BAC80139.1.
AK038633 mRNA. Translation: BAC30073.1.
AK043850 mRNA. Translation: BAC31681.1.
AK079616 mRNA. Translation: BAC37703.1.
AK147338 mRNA. Translation: BAE27855.1.
BC026479 mRNA. Translation: AAH26479.1.

IPI

IPI00131720.
IPI00473235.
IPI00626660.

RefSeq

NP_001032176.1.
NP_666235.1.

UniGene

Mm.330223

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VYV	X-ray	3.00	A	49-407	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q8R0S4.

Genome annotation databases

Ensembl

ENSMUSG00000017412. Mus musculus. [Contig view]

GeneID

12298.

KEGG

mmu:12298.

Organism-specific databases

MGI

MGI:103301. Cacnb4.

Phylogenomic databases

HOGENOM

Q8R0S4.

HOVERGEN

Q8R0S4.

OMA

Q8R0S4. TAKQKQK.

Gene expression databases

ArrayExpress

Q8R0S4.

Bgee

Q8R0S4.

GermOnline

ENSMUSG00000017412. Mus musculus.

Family and domain databases

InterPro

IPR008145. Guanylt/Ca.
IPR001452. SH3_domain.
IPR000584. VDCC_L_bsu.
[Graphical view]

PANTHER

PTHR11824. Ca_channel_B. 1 hit.

Pfam

PF00774. Ca_channel_B. 1 hit.
[Graphical view]

PRINTS

PR01626. LCACHANNELB.

SMART

SM00072. GuKc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

PROSITE

PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

280812.

SOURCE

Search...

Entry information

Entry name

CACB4_MOUSE

Accession

Primary (citable) accession number: Q8R0S4
Secondary accession number(s): Q3UHK2, Q8BRN6, Q8CAJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)