CACB3_RAT
ID CACB3_RAT Reviewed; 484 AA.
AC P54287;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
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;
GN Name=Cacnb3; Synonyms=Cacnlb3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7679112; DOI=10.1016/s0021-9258(18)53715-7;
RA Castellano A., Wei X., Birnbaumer L., Perez-Reyes E.;
RT "Cloning and expression of a third calcium channel beta subunit.";
RL J. Biol. Chem. 268:3450-3455(1993).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10666413; DOI=10.1161/01.res.86.2.175;
RA Wei S.K., Colecraft H.M., DeMaria C.D., Peterson B.Z., Zhang R.,
RA Kohout T.A., Rogers T.B., Yue D.T.;
RT "Ca(2+) channel modulation by recombinant auxiliary beta subunits expressed
RT in young adult heart cells.";
RL Circ. Res. 86:175-184(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-393, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP INTERACTION WITH CBARP AND CACNA1C, 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).
RN [5]
RP FUNCTION, INTERACTION WITH CACNA1C, AND SUBUNIT.
RX PubMed=29742403; DOI=10.1016/j.bpj.2018.03.029;
RA Bartels P., Yu D., Huang H., Hu Z., Herzig S., Soong T.W.;
RT "Alternative Splicing at N Terminus and Domain I Modulates CaV1.2
RT Inactivation and Surface Expression.";
RL Biophys. J. 114:2095-2106(2018).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 16-366 ALONE AND IN COMPLEX WITH
RP CACNA1C, SUBUNIT, FUNCTION, AND REGION.
RX PubMed=15170217; DOI=10.1038/nature02641;
RA Chen Y.H., Li M.H., Zhang Y., He L.L., Yamada Y., Fitzmaurice A., Shen Y.,
RA Zhang H., Tong L., Yang J.;
RT "Structural basis of the alpha1-beta subunit interaction of voltage-gated
RT Ca2+ channels.";
RL Nature 429:675-680(2004).
CC -!- FUNCTION: Regulatory subunit of the voltage-gated calcium channel that
CC gives rise to L-type calcium currents (PubMed:7679112, PubMed:10666413,
CC PubMed:24751537, PubMed:29742403, PubMed:15170217). Increases CACNA1B
CC peak calcium current and shifts the voltage dependencies of channel
CC activation and inactivation (By similarity). Increases CACNA1C peak
CC calcium current and shifts the voltage dependencies of channel
CC activation and inactivation (PubMed:7679112, PubMed:10666413,
CC PubMed:24751537, PubMed:29742403, PubMed:15170217).
CC {ECO:0000250|UniProtKB:Q9MZL3, ECO:0000269|PubMed:10666413,
CC ECO:0000269|PubMed:15170217, ECO:0000269|PubMed:24751537,
CC ECO:0000269|PubMed:29742403, ECO:0000269|PubMed:7679112}.
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 (Probable). The channel complex contains alpha, beta, gamma
CC and delta subunits in a 1:1:1:1 ratio (Probable). Interacts with
CC CACNA2D4. Interacts with FASLG (By similarity). Interacts with CBARP;
CC prevents the interaction of CACNB3 with the alpha subunit CACNA1C
CC thereby negatively regulating the activity of the corresponding calcium
CC channel (PubMed:24751537). {ECO:0000250|UniProtKB:P54284,
CC ECO:0000269|PubMed:24751537, ECO:0000305|PubMed:10666413,
CC ECO:0000305|PubMed:24751537, ECO:0000305|PubMed:29742403,
CC ECO:0000305|PubMed:7679112}.
CC -!- INTERACTION:
CC P54287; P55040: GEM; Xeno; NbExp=2; IntAct=EBI-8028596, EBI-744104;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10666413}.
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:7679112}.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; M88751; AAA18486.1; -; mRNA.
DR PIR; A46608; A46608.
DR RefSeq; NP_036960.1; NM_012828.2.
DR PDB; 1VYT; X-ray; 2.60 A; A/B=16-366.
DR PDB; 1VYU; X-ray; 2.30 A; A/B=16-366.
DR PDBsum; 1VYT; -.
DR PDBsum; 1VYU; -.
DR AlphaFoldDB; P54287; -.
DR SMR; P54287; -.
DR BioGRID; 247336; 3.
DR DIP; DIP-59370N; -.
DR IntAct; P54287; 3.
DR MINT; P54287; -.
DR STRING; 10116.ENSRNOP00000017490; -.
DR BindingDB; P54287; -.
DR ChEMBL; CHEMBL3137269; -.
DR ChEMBL; CHEMBL3137270; -.
DR ChEMBL; CHEMBL4296086; -.
DR iPTMnet; P54287; -.
DR PhosphoSitePlus; P54287; -.
DR PaxDb; P54287; -.
DR PRIDE; P54287; -.
DR Ensembl; ENSRNOT00000081206; ENSRNOP00000073026; ENSRNOG00000054274.
DR GeneID; 25297; -.
DR KEGG; rno:25297; -.
DR UCSC; RGD:2248; rat.
DR CTD; 784; -.
DR RGD; 2248; Cacnb3.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_0_1_1; -.
DR InParanoid; P54287; -.
DR OMA; PCQGSAD; -.
DR OrthoDB; 926074at2759; -.
DR PhylomeDB; P54287; -.
DR TreeFam; TF316195; -.
DR Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-RNO-422356; Regulation of insulin secretion.
DR EvolutionaryTrace; P54287; -.
DR PRO; PR:P54287; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000054274; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; P54287; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
DR GO; GO:0005246; F:calcium channel regulator activity; IMP:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:BHF-UCL.
DR GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; IDA:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IDA:BHF-UCL.
DR GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEP:RGD.
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; IMP:RGD.
DR GO; GO:1905788; P:negative regulation of detection of mechanical stimulus involved in sensory perception of touch; IMP:RGD.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:1901843; P:positive regulation of high voltage-gated calcium channel activity; IMP:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:RGD.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:1902630; P:regulation of membrane hyperpolarization; IDA:RGD.
DR GO; GO:0098903; P:regulation of membrane repolarization during action potential; IDA: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; ISO:RGD.
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 3D-structure; Calcium; Calcium channel; Calcium transport; Cytoplasm;
KW Ion channel; Ion transport; Phosphoprotein; Reference proteome; SH3 domain;
KW Transport; Voltage-gated channel.
FT CHAIN 1..484
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-3"
FT /id="PRO_0000144059"
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:0000269|PubMed:15170217"
FT REGION 388..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 389..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:0007744|PubMed:22673903"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 40..55
FT /evidence="ECO:0007829|PDB:1VYU"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1VYU"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1VYU"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:1VYU"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:1VYU"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1VYU"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1VYU"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:1VYU"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1VYU"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1VYU"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1VYT"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:1VYT"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1VYT"
FT HELIX 247..262
FT /evidence="ECO:0007829|PDB:1VYU"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1VYU"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1VYU"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1VYU"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:1VYU"
FT HELIX 342..360
FT /evidence="ECO:0007829|PDB:1VYU"
SQ SEQUENCE 484 AA; 54564 MW; 18815828E9C5C9CA CRC64;
MYDDSYVPGF EDSEAGSADS YTSRPSLDSD VSLEEDRESA RREVESQAQQ QLERAKHKPV
AFAVRTNVSY CGVLDEECPV QGSGVNFEAK DFLHIKEKYS NDWWIGRLVK EGGDIAFIPS
PQRLESIRLK QEQKARRSGN PSSLSDIGNR RSPPPSLAKQ KQKQAEHVPP YDVVPSMRPV
VLVGPSLKGY EVTDMMQKAL FDFLKHRFDG RISITRVTAD LSLAKRSVLN NPGKRTIIER
SSARSSIAEV QSEIERIFEL AKSLQLVVLD ADTINHPAQL AKTSLAPIIV FVKVSSPKVL
QRLIRSRGKS QMKHLTVQMM AYDKLVQCPP ESFDVILDEN QLDDACEHLA EYLEVYWRAT
HHPAPGPGML GPPSAIPGLQ NQQLLGERGE EHSPLERDSL MPSDEASESS RQAWTGSSQR
SSRHLEEDYA DAYQDLYQPH RQHTSGLPSA NGHDPQDRLL AQDSEHDHND RNWQRNRPWP
KDSY
