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Protein

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

Gene

Cacnb4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • high voltage-gated calcium channel activity Source: MGI
  • voltage-gated calcium channel activity Source: MGI

GO - Biological processi

  • adult walking behavior Source: MGI
  • calcium ion transmembrane transport Source: MGI
  • calcium ion transport Source: MGI
  • cAMP metabolic process Source: MGI
  • cellular calcium ion homeostasis Source: MGI
  • detection of light stimulus involved in visual perception Source: MGI
  • gamma-aminobutyric acid secretion Source: MGI
  • gamma-aminobutyric acid signaling pathway Source: MGI
  • muscle fiber development Source: MGI
  • neurological system process Source: MGI
  • neuromuscular junction development Source: MGI
  • neuronal action potential propagation Source: MGI
  • Peyer's patch development Source: MGI
  • regulation of membrane potential Source: MGI
  • regulation of voltage-gated calcium channel activity Source: MGI
  • spleen development Source: MGI
  • synaptic transmission, glutamatergic Source: MGI
  • T cell receptor signaling pathway Source: MGI
  • thymus development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-MMU-112308. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
R-MMU-419037. NCAM1 interactions.
R-MMU-5576892. Phase 0 - rapid depolarisation.
R-MMU-5576893. Phase 2 - plateau phase.
R-MMU-5576894. Phase 1 - inactivation of fast Na+ channels.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Cacnb4
Synonyms:Cacnlb4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:103301. Cacnb4.

Subcellular locationi

GO - Cellular componenti

  • plasma membrane Source: MGI
  • synapse Source: MGI
  • voltage-gated calcium channel complex Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519Voltage-dependent L-type calcium channel subunit beta-4PRO_0000144061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei182 – 1821PhosphoserineCombined sources
Modified residuei410 – 4101PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8R0S4.
PaxDbiQ8R0S4.
PeptideAtlasiQ8R0S4.
PRIDEiQ8R0S4.

PTM databases

iPTMnetiQ8R0S4.
PhosphoSiteiQ8R0S4.

Expressioni

Gene expression databases

BgeeiQ8R0S4.
ExpressionAtlasiQ8R0S4. baseline and differential.
GenevisibleiQ8R0S4. MM.

Interactioni

Subunit structurei

The L-type calcium channel is composed of four subunits: alpha-1, alpha-2, beta and gamma. Interacts with FASLG (By similarity). Interacts with CBARP.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ERC1Q8IUD2-22EBI-3647752,EBI-6920871From a different organism.
Ppp2r5dQ91V892EBI-3647752,EBI-8028449

Protein-protein interaction databases

BioGridi198442. 3 interactions.
IntActiQ8R0S4. 9 interactions.
STRINGi10090.ENSMUSP00000077438.

Structurei

Secondary structure

1
519
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi72 – 8817
Beta strandi94 – 1007
Beta strandi124 – 1329
Beta strandi135 – 1428
Beta strandi148 – 1514
Helixi153 – 1619
Turni162 – 1643
Beta strandi211 – 2155
Beta strandi221 – 2244
Helixi232 – 24817
Turni249 – 2513
Beta strandi252 – 2587
Helixi262 – 2643
Helixi288 – 30215
Beta strandi307 – 3126
Helixi318 – 3214
Beta strandi329 – 3335
Helixi338 – 3469
Helixi350 – 3534
Helixi356 – 36712
Helixi371 – 3733
Beta strandi375 – 3784
Beta strandi380 – 3823
Helixi383 – 40119

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VYVX-ray3.00A49-407[»]
ProteinModelPortaliQ8R0S4.
SMRiQ8R0S4. Positions 49-402.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8R0S4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 16063SH3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiKOG3812. Eukaryota.
ENOG410XRDI. LUCA.
GeneTreeiENSGT00390000002740.
HOGENOMiHOG000230979.
HOVERGENiHBG050765.
InParanoidiQ8R0S4.
KOiK04865.
OrthoDBiEOG7966G4.
PhylomeDBiQ8R0S4.
TreeFamiTF316195.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
IPR000584. VDCC_L_bsu.
[Graphical view]
PANTHERiPTHR11824. PTHR11824. 1 hit.
PfamiPF00625. Guanylate_kin. 1 hit.
PF12052. VGCC_beta4Aa_N. 1 hit.
[Graphical view]
PRINTSiPR01626. LCACHANNELB.
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: Q8R0S4-3) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSSSYGKNGA ADGPHSPSSQ VARGTTTRRS RLKRSDGSTT STSFILRQGS
60 70 80 90 100
ADSYTSRPSD SDVSLEEDRE AIRQEREQQA AIQLERAKSK PVAFAVKTNV
110 120 130 140 150
SYCGALDEDV PVPSTAISFD AKDFLHIKEK YNNDWWIGRL VKEGCEIGFI
160 170 180 190 200
PSPLRLENIR IQQEQKRGRF HGGKSSGNSS SSLGEMVSGT FRATPTTTAK
210 220 230 240 250
QKQKVTEHIP PYDVVPSMRP VVLVGPSLKG YEVTDMMQKA LFDFLKHRFD
260 270 280 290 300
GRISITRVTA DISLAKRSVL NNPSKRAIIE RSNTRSSLAE VQSEIERIFE
310 320 330 340 350
LARSLQLVVL DADTINHPAQ LIKTSLAPII VHVKVSSPKV LQRLIKSRGK
360 370 380 390 400
SQSKHLNVQL VAADKLAQCP PEMFDVILDE NQLEDACEHL GEYLEAYWRA
410 420 430 440 450
THTSSSTPMT PLLGRNVGST ALSPYPTAIS GLQSQRMRHS NHSTENSPIE
460 470 480 490 500
RRSLMTSDEN YHNERARKSR NRLSSSSQHS RDHYPLVEED YPDSYQDTYK
510
PHRNRGSPGG CSHDSRHRL
Length:519
Mass (Da):57,950
Last modified:January 23, 2007 - v2
Checksum:i663A88C7BCF7E90C
GO
Isoform 1 (identifier: Q8R0S4-1) [UniParc]FASTAAdd to basket

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

Show »
Length:486
Mass (Da):54,619
Checksum:iF4FCDD8810D75696
GO
Isoform 2 (identifier: Q8R0S4-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:473
Mass (Da):53,084
Checksum:i1EA0EE1CA4264A65
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti492 – 4921P → A in BAC31681 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4848MSSSY…FILRQ → MYDNLYLHGVEDSEA in isoform 1. 2 PublicationsVSP_022599Add
BLAST
Alternative sequencei1 – 4848MSSSY…FILRQ → MA in isoform 2. 1 PublicationVSP_010737Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16034.1. [Q8R0S4-3]
CCDS16035.1. [Q8R0S4-1]
CCDS71052.1. [Q8R0S4-2]
RefSeqiNP_001032176.1. NM_001037099.2. [Q8R0S4-3]
NP_001272356.1. NM_001285427.1. [Q8R0S4-2]
NP_666235.1. NM_146123.3. [Q8R0S4-1]
XP_006497704.1. XM_006497641.2. [Q8R0S4-2]
XP_011237317.1. XM_011239015.1. [Q8R0S4-2]
UniGeneiMm.330223.

Genome annotation databases

EnsembliENSMUST00000078324; ENSMUSP00000077438; ENSMUSG00000017412. [Q8R0S4-3]
ENSMUST00000102760; ENSMUSP00000099821; ENSMUSG00000017412. [Q8R0S4-1]
ENSMUST00000102761; ENSMUSP00000099822; ENSMUSG00000017412. [Q8R0S4-2]
GeneIDi12298.
KEGGimmu:12298.
UCSCiuc008jra.2. mouse. [Q8R0S4-1]
uc008jrb.2. mouse. [Q8R0S4-2]
uc008jrc.1. mouse. [Q8R0S4-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16034.1. [Q8R0S4-3]
CCDS16035.1. [Q8R0S4-1]
CCDS71052.1. [Q8R0S4-2]
RefSeqiNP_001032176.1. NM_001037099.2. [Q8R0S4-3]
NP_001272356.1. NM_001285427.1. [Q8R0S4-2]
NP_666235.1. NM_146123.3. [Q8R0S4-1]
XP_006497704.1. XM_006497641.2. [Q8R0S4-2]
XP_011237317.1. XM_011239015.1. [Q8R0S4-2]
UniGeneiMm.330223.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VYVX-ray3.00A49-407[»]
ProteinModelPortaliQ8R0S4.
SMRiQ8R0S4. Positions 49-402.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198442. 3 interactions.
IntActiQ8R0S4. 9 interactions.
STRINGi10090.ENSMUSP00000077438.

PTM databases

iPTMnetiQ8R0S4.
PhosphoSiteiQ8R0S4.

Proteomic databases

MaxQBiQ8R0S4.
PaxDbiQ8R0S4.
PeptideAtlasiQ8R0S4.
PRIDEiQ8R0S4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000078324; ENSMUSP00000077438; ENSMUSG00000017412. [Q8R0S4-3]
ENSMUST00000102760; ENSMUSP00000099821; ENSMUSG00000017412. [Q8R0S4-1]
ENSMUST00000102761; ENSMUSP00000099822; ENSMUSG00000017412. [Q8R0S4-2]
GeneIDi12298.
KEGGimmu:12298.
UCSCiuc008jra.2. mouse. [Q8R0S4-1]
uc008jrb.2. mouse. [Q8R0S4-2]
uc008jrc.1. mouse. [Q8R0S4-3]

Organism-specific databases

CTDi785.
MGIiMGI:103301. Cacnb4.

Phylogenomic databases

eggNOGiKOG3812. Eukaryota.
ENOG410XRDI. LUCA.
GeneTreeiENSGT00390000002740.
HOGENOMiHOG000230979.
HOVERGENiHBG050765.
InParanoidiQ8R0S4.
KOiK04865.
OrthoDBiEOG7966G4.
PhylomeDBiQ8R0S4.
TreeFamiTF316195.

Enzyme and pathway databases

ReactomeiR-MMU-112308. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
R-MMU-419037. NCAM1 interactions.
R-MMU-5576892. Phase 0 - rapid depolarisation.
R-MMU-5576893. Phase 2 - plateau phase.
R-MMU-5576894. Phase 1 - inactivation of fast Na+ channels.

Miscellaneous databases

ChiTaRSiCacnb4. mouse.
EvolutionaryTraceiQ8R0S4.
PROiQ8R0S4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R0S4.
ExpressionAtlasiQ8R0S4. baseline and differential.
GenevisibleiQ8R0S4. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
IPR000584. VDCC_L_bsu.
[Graphical view]
PANTHERiPTHR11824. PTHR11824. 1 hit.
PfamiPF00625. Guanylate_kin. 1 hit.
PF12052. VGCC_beta4Aa_N. 1 hit.
[Graphical view]
PRINTSiPR01626. LCACHANNELB.
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye.
  4. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND THR-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. Cited for: INTERACTION WITH CBARP.

Entry informationi

Entry nameiCACB4_MOUSE
AccessioniPrimary (citable) accession number: Q8R0S4
Secondary accession number(s): Q3UHK2, Q8BRN6, Q8CAJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.