ID CACB3_MOUSE Reviewed; 484 AA. AC P54285; G5E821; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 02-SEP-2026, entry version 188. DE RecName: Full=Voltage-dependent L-type calcium channel subunit beta-3; DE Short=CAB3; DE AltName: Full=Calcium channel voltage-dependent subunit beta 3; DE Short=CCHB3; GN Name=Cacnb3; Synonyms=Cacnlb3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3A). RX PubMed=7490102; DOI=10.1006/geno.1995.1196; RA Chin H., Kwon O.-J., Jung H.H., Kim D.S., Kozak C.A.; RT "Genetic mapping of the mouse genes encoding the voltage-sensitive calcium RT channel subunits."; RL Genomics 28:592-595(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RC STRAIN=129/SvJ; RX PubMed=8617257; DOI=10.1111/j.1432-1033.1996.t01-1-00138.x; RA Murakami M., Wissenbach U., Flockerzi V.; RT "Gene structure of the murine calcium channel beta3 subunit, cDNA and RT characterization of alternative splicing and transcription products."; RL Eur. J. Biochem. 236:138-143(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=21831364; DOI=10.1016/j.brainres.2011.07.033; RA Ball S.L., McEnery M.W., Yunker A.M., Shin H.S., Gregg R.G.; RT "Distribution of voltage gated calcium channel beta subunits in the mouse RT retina."; RL Brain Res. 1412:1-8(2011). RN [6] RP INTERACTION WITH CBARP, AND FUNCTION. RX PubMed=24751537; DOI=10.1083/jcb.201304101; RA Beguin P., Nagashima K., Mahalakshmi R.N., Vigot R., Matsunaga A., Miki T., RA Ng M.Y., Ng Y.J., Lim C.H., Tay H.S., Hwang L.A., Firsov D., Tang B.L., RA Inagaki N., Mori Y., Seino S., Launey T., Hunziker W.; RT "BARP suppresses voltage-gated calcium channel activity and Ca2+-evoked RT exocytosis."; RL J. Cell Biol. 205:233-249(2014). CC -!- FUNCTION: Regulatory subunit of the voltage-gated calcium channel that CC gives rise to L-type calcium currents (PubMed:24751537). Increases CC CACNA1B peak calcium current and shifts the voltage dependencies of CC channel activation and inactivation (By similarity). Increases CACNA1C CC peak calcium current and shifts the voltage dependencies of channel CC activation and inactivation (By similarity). CC {ECO:0000250|UniProtKB:P54287, ECO:0000250|UniProtKB:Q9MZL3, CC ECO:0000269|PubMed:24751537}. CC -!- SUBUNIT: Component of a calcium channel complex consisting of a pore- CC forming alpha subunit (CACNA1C) and the ancillary subunits CACNB3 and CC CACNA2D1. The channel complex contains alpha, beta, gamma and delta CC subunits in a 1:1:1:1 ratio. Interacts with CACNA2D4. Interacts with CC FASLG (By similarity). Interacts with CBARP; prevents the interaction CC of CACNB3 with the alpha subunit CACNA1C thereby negatively regulating CC the activity of the corresponding calcium channel (PubMed:24751537). CC {ECO:0000250|UniProtKB:P54284, ECO:0000269|PubMed:24751537}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21831364}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=3A; CC IsoId=P54285-1; Sequence=Displayed; CC Name=3B; CC IsoId=P54285-2; Sequence=Not described; CC -!- TISSUE SPECIFICITY: Detected in the inner plexiform layer in the retina CC (at protein level). {ECO:0000269|PubMed:21831364}. CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U20372; AAA91105.1; -; mRNA. DR EMBL; X94404; CAB61648.1; -; Genomic_DNA. DR EMBL; X94406; CAB61648.1; JOINED; Genomic_DNA. DR EMBL; X94405; CAB61648.1; JOINED; Genomic_DNA. DR EMBL; AC156543; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466550; EDL04179.1; -; Genomic_DNA. DR CCDS; CCDS27800.1; -. [P54285-1] DR PIR; S62185; S62185. DR RefSeq; NP_031607.2; NM_007581.4. [P54285-1] DR RefSeq; XP_036014990.1; XM_036159097.1. [P54285-1] DR AlphaFoldDB; P54285; -. DR SMR; P54285; -. DR BioGRID; 198441; 7. DR FunCoup; P54285; 859. DR IntAct; P54285; 3. DR MINT; P54285; -. DR STRING; 10090.ENSMUSP00000155514; -. DR GlyGen; P54285; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P54285; -. DR PhosphoSitePlus; P54285; -. DR jPOST; P54285; -. DR PaxDb; 10090-ENSMUSP00000155514; -. DR ProteomicsDB; 265488; -. [P54285-1] DR Pumba; P54285; -. DR ABCD; P54285; 1 sequenced antibody. DR Antibodypedia; 13690; 211 antibodies from 30 providers. DR DNASU; 12297; -. DR Ensembl; ENSMUST00000230490.2; ENSMUSP00000155514.2; ENSMUSG00000003352.15. DR GeneID; 12297; -. DR KEGG; mmu:12297; -. DR UCSC; uc007xnc.2; mouse. [P54285-1] DR AGR; MGI:103307; -. DR CTD; 784; -. DR MGI; MGI:103307; Cacnb3. DR VEuPathDB; HostDB:ENSMUSG00000003352; -. DR eggNOG; KOG3812; Eukaryota. DR GeneTree; ENSGT00950000182837; -. DR HOGENOM; CLU_021995_0_1_1; -. DR InParanoid; P54285; -. DR OMA; MGEHESE; -. DR OrthoDB; 5962384at2759; -. DR PhylomeDB; P54285; -. DR Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening. DR Reactome; R-MMU-422356; Regulation of insulin secretion. DR BioGRID-ORCS; 12297; 4 hits in 79 CRISPR screens. DR CD-CODE; CE726F99; Postsynaptic density. DR PRO; PR:P54285; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; P54285; protein. DR Bgee; ENSMUSG00000003352; Expressed in habenula and 238 other cell types or tissues. DR ExpressionAtlas; P54285; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISO:GO_Central. DR GO; GO:0005737; C:cytoplasm; ISO:GO_Central. DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:BHF-UCL. DR GO; GO:0016020; C:membrane; ISO:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI. DR GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB. DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; ISO:GO_Central. DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:GO_Central. DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:BHF-UCL. DR GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:BHF-UCL. DR GO; GO:0006816; P:calcium ion transport; ISO:GO_Central. DR GO; GO:0060402; P:calcium ion transport into cytosol; ISS:BHF-UCL. DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:GO_Central. DR GO; GO:1905788; P:negative regulation of detection of mechanical stimulus involved in sensory perception of touch; ISO:GO_Central. DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISO:GO_Central. DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:GO_Central. DR GO; GO:1901843; P:positive regulation of high voltage-gated calcium channel activity; ISS:UniProtKB. DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISO:GO_Central. DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; ISO:GO_Central. DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL. DR GO; GO:1902630; P:regulation of membrane hyperpolarization; ISO:GO_Central. DR GO; GO:0098903; P:regulation of membrane repolarization during action potential; ISS:BHF-UCL. DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI. DR CDD; cd12042; SH3_CACNB3; 1. DR FunFam; 3.40.50.300:FF:000023; Voltage-dependent L-type calcium channel subunit beta-2; 1. DR FunFam; 2.30.30.40:FF:000049; Voltage-dependent L-type calcium channel subunit beta-3; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR046937; CAB1-4_N_A-dom. DR InterPro; IPR035760; CACNB3_SH3. 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; IPR008079; VDCC_L_b3su. DR InterPro; IPR000584; VDCC_L_bsu. DR PANTHER; PTHR11824; VOLTAGE-DEPENDENT CALCIUM CHANNEL BETA SUBUNIT; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF12052; VGCC_beta4Aa_N; 1. DR PRINTS; PR01626; LCACHANNELB. DR PRINTS; PR01696; LCACHANNELB3. DR SMART; SM00072; GuKc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Calcium channel; Calcium transport; KW Cytoplasm; Ion channel; Ion transport; Phosphoprotein; Reference proteome; KW SH3 domain; Transport; Voltage-gated channel. FT CHAIN 1..484 FT /note="Voltage-dependent L-type calcium channel subunit FT beta-3" FT /id="PRO_0000144057" FT DOMAIN 59..128 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 1..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 129..170 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 195..345 FT /note="Mediates interaction with the alpha subunit" FT /evidence="ECO:0000250|UniProtKB:P54287" FT REGION 390..484 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 390..399 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 409..420 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 463..484 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54287" FT MOD_RES 393 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54287" FT CONFLICT 82 FT /note="G -> A (in Ref. 1; AAA91105)" FT /evidence="ECO:0000305" FT CONFLICT 114 FT /note="D -> A (in Ref. 1; AAA91105)" FT /evidence="ECO:0000305" FT CONFLICT 149 FT /note="N -> F (in Ref. 1; AAA91105)" FT /evidence="ECO:0000305" FT CONFLICT 335 FT /note="V -> A (in Ref. 1; AAA91105)" FT /evidence="ECO:0000305" FT CONFLICT 384 FT /note="L -> Q (in Ref. 1; AAA91105)" FT /evidence="ECO:0000305" FT CONFLICT 409 FT /note="S -> T (in Ref. 2; CAB61648)" FT /evidence="ECO:0000305" FT CONFLICT 421 FT /note="S -> T (in Ref. 2; CAB61648)" FT /evidence="ECO:0000305" SQ SEQUENCE 484 AA; 54572 MW; 56871A0B563A567E CRC64; MYDDSYVPGF EDSEAGSADS YTSRPSLDSD VSLEEDRESA RREVESQAQQ QLERAKHKPV AFAVRTNVSY CGVLDEECPV QGSGVNFEAK DFLHIKEKYS NDWWIGRLVK EGGDIAFIPS PQRLESIRLK QEQKARRSGN PSSLGDIGNR RSPPPSLAKQ KQKQAEHVPP YDVVPSMRPV VLVGPSLKGY EVTDMMQKAL FDFLKHRFDG RISITRVTAD LSLAKRSVLN NPGKRTIIER SSARSSIAEV QSEIERIFEL AKSLQLVVLD ADTINHPAQL AKTSLAPIIV FVKVSSPKVL QRLIRSRGKS QMKHLTVQMM AYDKLVQCPP ESFDVILDEN QLEDACEHLA EYLEVYWRAT HHPAPGPGLL GPPSAIPGLQ NQQLLGERVE EHSPLERDSL MPSDEASESS RQAWTGSSQR SSRHLEEDYA DAYQDLYQPH RQHTSGLPSA NGHDPQDRLL AQDSEHDHND RNWQRNRPWP KDSY //