CACB3_MOUSE
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 03-AUG-2022, entry version 169.
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}.
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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_007581.3. [P54285-1]
DR AlphaFoldDB; P54285; -.
DR SMR; P54285; -.
DR BioGRID; 198441; 7.
DR IntAct; P54285; 3.
DR MINT; P54285; -.
DR STRING; 10090.ENSMUSP00000003442; -.
DR iPTMnet; P54285; -.
DR PhosphoSitePlus; P54285; -.
DR MaxQB; P54285; -.
DR PaxDb; P54285; -.
DR PRIDE; P54285; -.
DR ProteomicsDB; 265488; -. [P54285-1]
DR Antibodypedia; 13690; 212 antibodies from 30 providers.
DR DNASU; 12297; -.
DR Ensembl; ENSMUST00000230490; ENSMUSP00000155514; ENSMUSG00000003352. [P54285-1]
DR GeneID; 12297; -.
DR KEGG; mmu:12297; -.
DR UCSC; uc007xnc.2; mouse. [P54285-1]
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; PCQGSAD; -.
DR OrthoDB; 926074at2759; -.
DR PhylomeDB; P54285; -.
DR TreeFam; TF316195; -.
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 74 CRISPR screens.
DR ChiTaRS; Cacnb3; mouse.
DR PRO; PR:P54285; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P54285; protein.
DR Bgee; ENSMUSG00000003352; Expressed in habenula and 234 other tissues.
DR ExpressionAtlas; P54285; baseline and differential.
DR Genevisible; P54285; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:BHF-UCL.
DR GO; GO:0016020; C:membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:MGI.
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:MGI.
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:MGI.
DR GO; GO:1905788; P:negative regulation of detection of mechanical stimulus involved in sensory perception of touch; ISO:MGI.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
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:MGI.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:1902630; P:regulation of membrane hyperpolarization; ISO:MGI.
DR GO; GO:0098903; P:regulation of membrane repolarization during action potential; ISS:BHF-UCL.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
DR CDD; cd12042; SH3_CACNB3; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 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; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 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 29..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..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
