CACB2_MOUSE
ID CACB2_MOUSE Reviewed; 655 AA.
AC Q8CC27; A2ASJ8; Q8C5J5; Q9CTQ6;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit beta-2;
DE Short=CAB2;
DE AltName: Full=Calcium channel voltage-dependent subunit beta 2;
GN Name=Cacnb2; Synonyms=Cacnlb2;
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 (ISOFORM 3), AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=14674701; DOI=10.1023/a:1027316017156;
RA Murakami M., Aoyama M., Suzuki T., Sasano H., Nakayama S., Iijima T.;
RT "Genetic characterization of a new splice variant of the beta2 subunit of
RT the voltage-dependent calcium channel.";
RL Mol. Cell. Biochem. 254:217-225(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Olfactory bulb, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-214; SER-545 AND
RP THR-549, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH CBARP.
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: 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:0000250,
CC ECO:0000269|PubMed:14674701}.
CC -!- SUBUNIT: Component of a calcium channel complex consisting of a pore-
CC forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or
CC CACNB2, CACNG1 and CACNA2D1. The channel complex contains alpha, beta,
CC gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either
CC CACNB1 or CACNB2. Interacts with CACNA1C (By similarity). Interacts
CC with RRAD. Interaction with RRAD regulates the trafficking of CACNA1C
CC to the cell membrane. Interacts with TMIGD2 (By similarity). Interacts
CC with CAMK2D (By similarity). Interacts with CBARP (PubMed:24751537).
CC Interacts with CAMK2A (By similarity). {ECO:0000250|UniProtKB:Q08289,
CC ECO:0000250|UniProtKB:Q8VGC3, ECO:0000269|PubMed:24751537}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8CC27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CC27-2; Sequence=VSP_010730;
CC Name=3; Synonyms=Beta-2g;
CC IsoId=Q8CC27-3; Sequence=VSP_010731;
CC Name=4;
CC IsoId=Q8CC27-4; Sequence=VSP_010731, VSP_010732;
CC -!- PTM: Regulated through phosphorylation at Thr-549 by CaMK2D.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AB109465; BAD01474.1; -; Genomic_DNA.
DR EMBL; AK020806; BAB32216.1; -; mRNA.
DR EMBL; AK034054; BAC28562.1; -; mRNA.
DR EMBL; AK078220; BAC37179.1; -; mRNA.
DR EMBL; AL928632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15702.1; -. [Q8CC27-1]
DR CCDS; CCDS84473.1; -. [Q8CC27-3]
DR RefSeq; NP_001296448.1; NM_001309519.1. [Q8CC27-3]
DR RefSeq; NP_075605.1; NM_023116.4. [Q8CC27-1]
DR RefSeq; XP_006497383.1; XM_006497320.1. [Q8CC27-2]
DR AlphaFoldDB; Q8CC27; -.
DR SMR; Q8CC27; -.
DR BioGRID; 198440; 9.
DR ComplexPortal; CPX-3194; Cardiac muscle VGCC complex.
DR IntAct; Q8CC27; 4.
DR STRING; 10090.ENSMUSP00000110371; -.
DR iPTMnet; Q8CC27; -.
DR PhosphoSitePlus; Q8CC27; -.
DR MaxQB; Q8CC27; -.
DR PaxDb; Q8CC27; -.
DR PRIDE; Q8CC27; -.
DR ProteomicsDB; 265484; -. [Q8CC27-1]
DR ProteomicsDB; 265485; -. [Q8CC27-2]
DR ProteomicsDB; 265486; -. [Q8CC27-3]
DR ProteomicsDB; 265487; -. [Q8CC27-4]
DR ABCD; Q8CC27; 1 sequenced antibody.
DR Antibodypedia; 12067; 579 antibodies from 35 providers.
DR DNASU; 12296; -.
DR Ensembl; ENSMUST00000114719; ENSMUSP00000110367; ENSMUSG00000057914. [Q8CC27-3]
DR Ensembl; ENSMUST00000114723; ENSMUSP00000110371; ENSMUSG00000057914. [Q8CC27-1]
DR GeneID; 12296; -.
DR KEGG; mmu:12296; -.
DR UCSC; uc008ikm.2; mouse. [Q8CC27-1]
DR UCSC; uc008iks.2; mouse. [Q8CC27-3]
DR UCSC; uc056zla.1; mouse. [Q8CC27-4]
DR CTD; 783; -.
DR MGI; MGI:894644; Cacnb2.
DR VEuPathDB; HostDB:ENSMUSG00000057914; -.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_3_0_1; -.
DR InParanoid; Q8CC27; -.
DR OrthoDB; 926074at2759; -.
DR PhylomeDB; Q8CC27; -.
DR TreeFam; TF316195; -.
DR Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-MMU-422356; Regulation of insulin secretion.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-MMU-5576893; Phase 2 - plateau phase.
DR BioGRID-ORCS; 12296; 3 hits in 60 CRISPR screens.
DR ChiTaRS; Cacnb2; mouse.
DR PRO; PR:Q8CC27; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CC27; protein.
DR Bgee; ENSMUSG00000057914; Expressed in retinal neural layer and 135 other tissues.
DR ExpressionAtlas; Q8CC27; baseline and differential.
DR Genevisible; Q8CC27; MM.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IMP:SynGO.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:BHF-UCL.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:MGI.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; 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:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; ISO:MGI.
DR GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; IMP:SynGO.
DR GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; ISS:BHF-UCL.
DR GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISS:BHF-UCL.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:BHF-UCL.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR GO; GO:1901843; P:positive regulation of high voltage-gated calcium channel activity; ISS:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:BHF-UCL.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd12040; SH3_CACNB2; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR035605; CACNB2_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; IPR005444; VDCC_L_b2su.
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; PR01628; LCACHANNELB2.
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 Cell membrane; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain; Transport; Voltage-gated channel.
FT CHAIN 1..655
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-2"
FT /id="PRO_0000144052"
FT DOMAIN 110..179
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 544
FT /note="Required for CaMK2D-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VGC3"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 549
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..67
FT /note="MVQSDTSKSPPVAAVAQESQMELLESAAPAGALGAQSYGKGARRKNRFKGSD
FT GSTSSDTTSNSFVRQ -> MQCCGLVHRRRVRVSY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010730"
FT VAR_SEQ 1..67
FT /note="MVQSDTSKSPPVAAVAQESQMELLESAAPAGALGAQSYGKGARRKNRFKGSD
FT GSTSSDTTSNSFVRQ -> MKATWIRLLKRAKGGRLKSSDIC (in isoform 3
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010731"
FT VAR_SEQ 221..264
FT /note="IDIDATGLDAEENDIPANHRSPKPSANSVTSPHSKEKRMPFFKK -> KQKQ
FT KS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010732"
FT CONFLICT 124
FT /note="A -> R (in Ref. 1; BAD01474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 73149 MW; 77841E9C2613843D CRC64;
MVQSDTSKSP PVAAVAQESQ MELLESAAPA GALGAQSYGK GARRKNRFKG SDGSTSSDTT
SNSFVRQGSA DSYTSRPSDS DVSLEEDREA VRREAERQAQ AQLEKAKTKP VAFAVRTNVR
YSAAQEDDVP VPGMAISFEA KDFLHVKEKF NNDWWIGRLV KEGCEIGFIP SPVKLENMRL
QHEQRAKQGK FYSSKSGGNS SSSLGDIVPS SRKSTPPSSA IDIDATGLDA EENDIPANHR
SPKPSANSVT SPHSKEKRMP FFKKTEHTPP YDVVPSMRPV VLVGPSLKGY EVTDMMQKAL
FDFLKHRFEG RISITRVTAD ISLAKRSVLN NPSKHAIIER SNTRSSLAEV QSEIERIFEL
ARTLQLVVLD ADTINHPAQL SKTSLAPIIV YVKISSPKVL QRLIKSRGKS QAKHLNVQMV
AADKLAQCPP QESFDVILDE NQLEDACEHL ADYLEAYWKA THPPSGNLPN PLLSRTLASS
TLPLSPTLAS NSQGSQGDQR PDRSAPRSAS QAEEEPCLEP VKKSQHRSSS ATHQNHRSGT
GRGLSRQETF DSETQESRDS AYVEPKEDYS HEHVDRYVPH REHNHREETH SSNGHRHRES
RHRSRDMGRD QDHNECIKQR SRHKSKDRYC DKEGEVISKR RNEAGEWNRD VYIRQ
