CACB4_HUMAN
ID CACB4_HUMAN Reviewed; 520 AA.
AC O00305; A7BJ74; A8K1Y4; B4DG40; O60515; Q6B000; Q96L40;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit beta-4 {ECO:0000305};
DE Short=CAB4 {ECO:0000305};
DE AltName: Full=Calcium channel voltage-dependent subunit beta 4 {ECO:0000305};
GN Name=CACNB4 {ECO:0000312|HGNC:HGNC:1404}; Synonyms=CACNLB4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9254841; DOI=10.1007/pl00008704;
RA Taviaux S., Williams M.E., Harpold M.M., Nargeot J., Lory P.;
RT "Assignment of human genes for beta 2 and beta 4 subunits of voltage-
RT dependent Ca2+ channels to chromosomes 10p12 and 2q22-q23.";
RL Hum. Genet. 100:151-154(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, FUNCTION, AND
RP SUBUNIT.
RC TISSUE=Spinal cord;
RX PubMed=11880487; DOI=10.1523/jneurosci.22-05-01573.2002;
RA Helton T.D., Horne W.A.;
RT "Alternative splicing of the beta 4 subunit has alpha 1 subunit subtype-
RT specific effects on Ca2+ channel gating.";
RL J. Neurosci. 22:1573-1582(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=17618603; DOI=10.1016/j.bbrc.2007.06.112;
RA Kobayashi T., Yamada Y., Fukao M., Shiratori K., Tsutsuura M., Tanimoto K.,
RA Tohse N.;
RT "The GK domain of the voltage-dependent calcium channel beta subunit is
RT essential for binding to the alpha subunit.";
RL Biochem. Biophys. Res. Commun. 360:679-683(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Amygdala, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-520 (ISOFORM 1).
RX PubMed=9628818; DOI=10.1006/geno.1998.5311;
RA Escayg A., Jones J.M., Kearney J.A., Hitchcock P.F., Meisler M.H.;
RT "Calcium channel beta4 (CACNB4): human ortholog of the mouse epilepsy gene
RT lethargic.";
RL Genomics 50:14-22(1998).
RN [9]
RP INVOLVEMENT IN EJM6 AND EIG9, AND VARIANT EA5 PHE-104.
RX PubMed=10762541; DOI=10.1086/302909;
RA Escayg A., De Waard M., Lee D.D., Bichet D., Wolf P., Mayer T.,
RA Johnston J., Baloh R., Sander T., Meisler M.H.;
RT "Coding and noncoding variation of the human calcium-channel beta4-subunit
RT gene CACNB4 in patients with idiopathic generalized epilepsy and episodic
RT ataxia.";
RL Am. J. Hum. Genet. 66:1531-1539(2000).
RN [10]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [11]
RP STRUCTURE BY NMR OF 50-92.
RX PubMed=16385006; DOI=10.1110/ps.051894506;
RA Vendel A.C., Rithner C.D., Lyons B.A., Horne W.A.;
RT "Solution structure of the N-terminal A domain of the human voltage-gated
RT Ca2+channel beta4a subunit.";
RL Protein Sci. 15:378-383(2006).
CC -!- FUNCTION: The beta subunit of voltage-dependent calcium channels
CC contributes to the function of the calcium channel by increasing peak
CC calcium current, shifting the voltage dependencies of activation and
CC inactivation, modulating G protein inhibition and controlling the
CC alpha-1 subunit membrane targeting. {ECO:0000269|PubMed:11880487}.
CC -!- SUBUNIT: The L-type calcium channel is composed of four subunits:
CC alpha-1, alpha-2, beta and gamma (PubMed:11880487). Interacts with
CC FASLG (PubMed:19807924). Interacts with CBARP (By similarity).
CC {ECO:0000250|UniProtKB:Q8R0S4, ECO:0000269|PubMed:11880487,
CC ECO:0000269|PubMed:19807924}.
CC -!- INTERACTION:
CC O00305; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-714838, EBI-10171570;
CC O00305; P56545-3: CTBP2; NbExp=3; IntAct=EBI-714838, EBI-10171902;
CC O00305; Q5JST6: EFHC2; NbExp=6; IntAct=EBI-714838, EBI-2349927;
CC O00305-2; P21579: SYT1; NbExp=2; IntAct=EBI-714855, EBI-524909;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=4b;
CC IsoId=O00305-1; Sequence=Displayed;
CC Name=2; Synonyms=4a;
CC IsoId=O00305-2; Sequence=VSP_000635;
CC Name=3;
CC IsoId=O00305-3; Sequence=VSP_043192;
CC Name=4; Synonyms=4d;
CC IsoId=O00305-4; Sequence=VSP_043193;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the cerebellum and
CC kidney.
CC -!- DISEASE: Epilepsy, idiopathic generalized 9 (EIG9) [MIM:607682]: A
CC disorder characterized by recurring generalized seizures in the absence
CC of detectable brain lesions and/or metabolic abnormalities. Generalized
CC seizures arise diffusely and simultaneously from both hemispheres of
CC the brain. {ECO:0000269|PubMed:10762541}. Note=Disease susceptibility
CC is associated with variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Juvenile myoclonic epilepsy 6 (EJM6) [MIM:607682]: A subtype
CC of idiopathic generalized epilepsy. Patients have afebrile seizures
CC only, with onset in adolescence (rather than in childhood) and
CC myoclonic jerks which usually occur after awakening and are triggered
CC by sleep deprivation and fatigue. {ECO:0000269|PubMed:10762541}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- DISEASE: Episodic ataxia 5 (EA5) [MIM:613855]: A disorder characterized
CC by episodes of vertigo and ataxia that last for several hours.
CC Interictal examination show spontaneous downbeat and gaze-evoked
CC nystagmus, mild dysarthria and truncal ataxia.
CC {ECO:0000269|PubMed:10762541}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 4]: Unable to interact with the alpha-1
CC subunit. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; U95020; AAB53333.1; -; mRNA.
DR EMBL; AY054985; AAL14351.1; -; mRNA.
DR EMBL; AB302276; BAF73808.1; -; mRNA.
DR EMBL; AK290049; BAF82738.1; -; mRNA.
DR EMBL; AK294398; BAG57651.1; -; mRNA.
DR EMBL; AK316045; BAH14416.1; -; mRNA.
DR EMBL; AC068547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC097448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX11494.1; -; Genomic_DNA.
DR EMBL; BC075049; AAH75049.1; -; mRNA.
DR EMBL; AF038852; AAC24206.1; -; mRNA.
DR CCDS; CCDS46426.1; -. [O00305-1]
DR CCDS; CCDS46427.1; -. [O00305-3]
DR CCDS; CCDS46428.1; -. [O00305-2]
DR CCDS; CCDS54409.1; -. [O00305-4]
DR RefSeq; NP_000717.2; NM_000726.4. [O00305-1]
DR RefSeq; NP_001005746.1; NM_001005746.3. [O00305-3]
DR RefSeq; NP_001005747.1; NM_001005747.3. [O00305-2]
DR RefSeq; NP_001139270.1; NM_001145798.2. [O00305-4]
DR RefSeq; NP_001307651.1; NM_001320722.2.
DR PDB; 2D46; NMR; -; A=50-92.
DR PDBsum; 2D46; -.
DR AlphaFoldDB; O00305; -.
DR SMR; O00305; -.
DR BioGRID; 107239; 15.
DR IntAct; O00305; 12.
DR STRING; 9606.ENSP00000438949; -.
DR ChEMBL; CHEMBL2363032; -.
DR DrugBank; DB01118; Amiodarone.
DR DrugBank; DB09231; Benidipine.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugBank; DB09232; Cilnidipine.
DR DrugBank; DB04855; Dronedarone.
DR DrugBank; DB06751; Drotaverine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB00153; Ergocalciferol.
DR DrugBank; DB13961; Fish oil.
DR DrugBank; DB09236; Lacidipine.
DR DrugBank; DB00825; Levomenthol.
DR DrugBank; DB00653; Magnesium sulfate.
DR DrugBank; DB09238; Manidipine.
DR DrugBank; DB01388; Mibefradil.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB00393; Nimodipine.
DR DrugBank; DB00252; Phenytoin.
DR DrugBank; DB00243; Ranolazine.
DR DrugBank; DB00421; Spironolactone.
DR DrugBank; DB00273; Topiramate.
DR DrugBank; DB09089; Trimebutine.
DR TCDB; 8.A.22.1.4; the ca(2+) channel auxiliary subunit Beta types 1-4 (cca-Beta) family.
DR GlyGen; O00305; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00305; -.
DR PhosphoSitePlus; O00305; -.
DR BioMuta; CACNB4; -.
DR jPOST; O00305; -.
DR MassIVE; O00305; -.
DR MaxQB; O00305; -.
DR PaxDb; O00305; -.
DR PeptideAtlas; O00305; -.
DR PRIDE; O00305; -.
DR ProteomicsDB; 47831; -. [O00305-1]
DR ProteomicsDB; 47832; -. [O00305-2]
DR ProteomicsDB; 47833; -. [O00305-3]
DR ProteomicsDB; 47834; -. [O00305-4]
DR ABCD; O00305; 1 sequenced antibody.
DR Antibodypedia; 2810; 359 antibodies from 39 providers.
DR DNASU; 785; -.
DR Ensembl; ENST00000201943.10; ENSP00000201943.5; ENSG00000182389.20. [O00305-4]
DR Ensembl; ENST00000534999.6; ENSP00000443893.1; ENSG00000182389.20. [O00305-2]
DR Ensembl; ENST00000539935.7; ENSP00000438949.1; ENSG00000182389.20. [O00305-1]
DR Ensembl; ENST00000638005.1; ENSP00000489677.1; ENSG00000182389.20. [O00305-3]
DR GeneID; 785; -.
DR KEGG; hsa:785; -.
DR MANE-Select; ENST00000539935.7; ENSP00000438949.1; NM_000726.5; NP_000717.2.
DR UCSC; uc002txy.5; human. [O00305-1]
DR CTD; 785; -.
DR DisGeNET; 785; -.
DR GeneCards; CACNB4; -.
DR HGNC; HGNC:1404; CACNB4.
DR HPA; ENSG00000182389; Group enriched (brain, skin).
DR MalaCards; CACNB4; -.
DR MIM; 601949; gene.
DR MIM; 607682; phenotype.
DR MIM; 613855; phenotype.
DR neXtProt; NX_O00305; -.
DR OpenTargets; ENSG00000182389; -.
DR Orphanet; 211067; Episodic ataxia type 5.
DR Orphanet; 307; Juvenile myoclonic epilepsy.
DR PharmGKB; PA26014; -.
DR VEuPathDB; HostDB:ENSG00000182389; -.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_0_1_1; -.
DR InParanoid; O00305; -.
DR OMA; DYRADRP; -.
DR OrthoDB; 926074at2759; -.
DR PhylomeDB; O00305; -.
DR TreeFam; TF316195; -.
DR PathwayCommons; O00305; -.
DR Reactome; R-HSA-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR SignaLink; O00305; -.
DR BioGRID-ORCS; 785; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; CACNB4; human.
DR EvolutionaryTrace; O00305; -.
DR GeneWiki; CACNB4; -.
DR GenomeRNAi; 785; -.
DR Pharos; O00305; Tbio.
DR PRO; PR:O00305; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O00305; protein.
DR Bgee; ENSG00000182389; Expressed in cerebellar vermis and 146 other tissues.
DR ExpressionAtlas; O00305; baseline and differential.
DR Genevisible; O00305; HS.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; IEA:Ensembl.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0046058; P:cAMP metabolic process; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; IEA:Ensembl.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
DR GO; GO:0055001; P:muscle cell development; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:0019227; P:neuronal action potential propagation; IEA:Ensembl.
DR GO; GO:0048541; P:Peyer's patch development; IEA:Ensembl.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IEA:Ensembl.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IEA:Ensembl.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IMP:UniProtKB.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR000584; VDCC_L_bsu.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR PRINTS; PR01626; LCACHANNELB.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Disease variant; Epilepsy; Ion channel; Ion transport;
KW Methylation; Phosphoprotein; Reference proteome; SH3 domain; Transport;
KW Voltage-gated channel.
FT CHAIN 1..520
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-4"
FT /id="PRO_0000144060"
FT DOMAIN 92..161
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A055"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S4"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S4"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A055"
FT MOD_RES 506
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S4"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A055"
FT VAR_SEQ 1..49
FT /note="MSSSSYAKNGTADGPHSPTSQVARGTTTRRSRLKRSDGSTTSTSFILRQ ->
FT MYDNLYLHGIEDSEA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11880487,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_000635"
FT VAR_SEQ 1..21
FT /note="MSSSSYAKNGTADGPHSPTSQ -> MDV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043192"
FT VAR_SEQ 373..434
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17618603"
FT /id="VSP_043193"
FT VARIANT 104
FT /note="C -> F (in EA5; associated with susceptibility to
FT EIG9; dbSNP:rs1805031)"
FT /evidence="ECO:0000269|PubMed:10762541"
FT /id="VAR_013669"
FT CONFLICT 245
FT /note="F -> S (in Ref. 1; AAB53333 and 2; AAL14351)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="L -> V (in Ref. 2; AAL14351)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="S -> T (in Ref. 2; AAL14351)"
FT /evidence="ECO:0000305"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:2D46"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2D46"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2D46"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2D46"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:2D46"
FT CONFLICT O00305-2:12
FT /note="D -> N (in Ref. 2; AAL14351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 58169 MW; 21025FA9782347FA CRC64;
MSSSSYAKNG TADGPHSPTS QVARGTTTRR SRLKRSDGST TSTSFILRQG SADSYTSRPS
DSDVSLEEDR EAIRQEREQQ AAIQLERAKS KPVAFAVKTN VSYCGALDED VPVPSTAISF
DAKDFLHIKE KYNNDWWIGR LVKEGCEIGF IPSPLRLENI RIQQEQKRGR FHGGKSSGNS
SSSLGEMVSG TFRATPTSTA KQKQKVTEHI PPYDVVPSMR PVVLVGPSLK GYEVTDMMQK
ALFDFLKHRF DGRISITRVT ADISLAKRSV LNNPSKRAII ERSNTRSSLA EVQSEIERIF
ELARSLQLVV LDADTINHPA QLIKTSLAPI IVHVKVSSPK VLQRLIKSRG KSQSKHLNVQ
LVAADKLAQC PPEMFDVILD ENQLEDACEH LGEYLEAYWR ATHTTSSTPM TPLLGRNLGS
TALSPYPTAI SGLQSQRMRH SNHSTENSPI ERRSLMTSDE NYHNERARKS RNRLSSSSQH
SRDHYPLVEE DYPDSYQDTY KPHRNRGSPG GYSHDSRHRL
