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Voltage-dependent L-type calcium channel subunit beta-2 (CAB2) (Calcium channel voltage-dependent subunit beta 2)

 CACB2_MOUSE             Reviewed;         655 AA.
Q8CC27; A2ASJ8; Q8C5J5; Q9CTQ6;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 137.
RecName: Full=Voltage-dependent L-type calcium channel subunit beta-2;
Short=CAB2;
AltName: Full=Calcium channel voltage-dependent subunit beta 2;
Name=Cacnb2; Synonyms=Cacnlb2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE (ISOFORM 3), AND FUNCTION.
TISSUE=Heart;
PubMed=14674701; DOI=10.1023/A:1027316017156;
Murakami M., Aoyama M., Suzuki T., Sasano H., Nakayama S., Iijima T.;
"Genetic characterization of a new splice variant of the beta2 subunit
of the voltage-dependent calcium channel.";
Mol. Cell. Biochem. 254:217-225(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
STRAIN=C57BL/6J; TISSUE=Diencephalon, Olfactory bulb, and Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-214; SER-545
AND THR-549, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Heart;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
INTERACTION WITH CBARP.
PubMed=24751537; DOI=10.1083/jcb.201304101;
Beguin P., Nagashima K., Mahalakshmi R.N., Vigot R., Matsunaga A.,
Miki T., Ng M.Y., Ng Y.J., Lim C.H., Tay H.S., Hwang L.A., Firsov D.,
Tang B.L., Inagaki N., Mori Y., Seino S., Launey T., Hunziker W.;
"BARP suppresses voltage-gated calcium channel activity and Ca2+-
evoked exocytosis.";
J. Cell Biol. 205:233-249(2014).
-!- FUNCTION: The beta subunit of voltage-dependent calcium channels
contributes to the function of the calcium channel by increasing
peak calcium current, shifting the voltage dependencies of
activation and inactivation, modulating G protein inhibition and
controlling the alpha-1 subunit membrane targeting. {ECO:0000250,
ECO:0000269|PubMed:14674701}.
-!- SUBUNIT: Component of a calcium channel complex consisting of a
pore-forming alpha subunit (CACNA1S) and the ancillary subunits
CACNB1 or CACNB2, CACNG1 and CACNA2D1. The channel complex
contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio,
i.e. it contains either CACNB1 or CACNB2. Interacts with CACNA1C
(By similarity). Interacts with RRAD. Interaction with RRAD
regulates the trafficking of CACNA1C to the cell membrane.
Interacts with TMIGD2 (By similarity). Interacts with CAMK2D (By
similarity). Interacts with CBARP (PubMed:24751537). Interacts
with CAMK2A (By similarity). {ECO:0000250|UniProtKB:Q08289,
ECO:0000250|UniProtKB:Q8VGC3, ECO:0000269|PubMed:24751537}.
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8CC27-1; Sequence=Displayed;
Name=2;
IsoId=Q8CC27-2; Sequence=VSP_010730;
Note=No experimental confirmation available.;
Name=3; Synonyms=Beta-2g;
IsoId=Q8CC27-3; Sequence=VSP_010731;
Name=4;
IsoId=Q8CC27-4; Sequence=VSP_010731, VSP_010732;
Note=No experimental confirmation available.;
-!- PTM: Regulated through phosphorylation at Thr-549 by CaMK2D.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the calcium channel beta subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB109465; BAD01474.1; -; Genomic_DNA.
EMBL; AK020806; BAB32216.1; -; mRNA.
EMBL; AK034054; BAC28562.1; -; mRNA.
EMBL; AK078220; BAC37179.1; -; mRNA.
EMBL; AL928632; CAM20242.1; -; Genomic_DNA.
CCDS; CCDS15702.1; -. [Q8CC27-1]
CCDS; CCDS84473.1; -. [Q8CC27-3]
RefSeq; NP_001296448.1; NM_001309519.1. [Q8CC27-3]
RefSeq; NP_075605.1; NM_023116.4. [Q8CC27-1]
RefSeq; XP_006497383.1; XM_006497320.1. [Q8CC27-2]
UniGene; Mm.313930; -.
ProteinModelPortal; Q8CC27; -.
SMR; Q8CC27; -.
BioGrid; 198440; 4.
ComplexPortal; CPX-3194; Cardiac muscle VGCC complex.
IntAct; Q8CC27; 4.
STRING; 10090.ENSMUSP00000110371; -.
iPTMnet; Q8CC27; -.
PhosphoSitePlus; Q8CC27; -.
PaxDb; Q8CC27; -.
PRIDE; Q8CC27; -.
Ensembl; ENSMUST00000114719; ENSMUSP00000110367; ENSMUSG00000057914. [Q8CC27-3]
Ensembl; ENSMUST00000114723; ENSMUSP00000110371; ENSMUSG00000057914. [Q8CC27-1]
GeneID; 12296; -.
KEGG; mmu:12296; -.
UCSC; uc008ikm.2; mouse. [Q8CC27-1]
UCSC; uc008iks.2; mouse. [Q8CC27-3]
UCSC; uc056zla.1; mouse. [Q8CC27-4]
CTD; 783; -.
MGI; MGI:894644; Cacnb2.
eggNOG; KOG3812; Eukaryota.
eggNOG; ENOG410XRDI; LUCA.
GeneTree; ENSGT00390000002740; -.
HOGENOM; HOG000230979; -.
HOVERGEN; HBG050765; -.
InParanoid; Q8CC27; -.
KO; K04863; -.
OMA; NRDVYIR; -.
OrthoDB; EOG091G09C1; -.
PhylomeDB; Q8CC27; -.
TreeFam; TF316195; -.
Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
Reactome; R-MMU-422356; Regulation of insulin secretion.
Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
Reactome; R-MMU-5576893; Phase 2 - plateau phase.
ChiTaRS; Cacnb2; mouse.
PRO; PR:Q8CC27; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000057914; Expressed in 167 organ(s), highest expression level in lumbar subsegment of spinal cord.
ExpressionAtlas; Q8CC27; baseline and differential.
Genevisible; Q8CC27; MM.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
GO; GO:0051015; F:actin filament binding; IDA:BHF-UCL.
GO; GO:0005246; F:calcium channel regulator activity; ISO:MGI.
GO; GO:0008331; F:high voltage-gated calcium channel activity; TAS:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:MGI.
GO; GO:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; IEA:Ensembl.
GO; GO:0070509; P:calcium ion import; ISO:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISS:BHF-UCL.
GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:BHF-UCL.
GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
GO; GO:1901843; P:positive regulation of high voltage-gated calcium channel activity; ISS:BHF-UCL.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:BHF-UCL.
GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISO:MGI.
GO; GO:0007601; P:visual perception; IMP:MGI.
CDD; cd12040; SH3_CACNB2; 1.
InterPro; IPR035605; CACNB2_SH3.
InterPro; IPR008145; GK/Ca_channel_bsu.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR005444; VDCC_L_b2su.
InterPro; IPR000584; VDCC_L_bsu.
PANTHER; PTHR11824; PTHR11824; 1.
Pfam; PF00625; Guanylate_kin; 1.
Pfam; PF12052; VGCC_beta4Aa_N; 1.
PRINTS; PR01626; LCACHANNELB.
PRINTS; PR01628; LCACHANNELB2.
SMART; SM00072; GuKc; 1.
SUPFAM; SSF50044; SSF50044; 2.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calcium channel; Calcium transport;
Cell membrane; Complete proteome; Ion channel; Ion transport;
Membrane; Phosphoprotein; Reference proteome; SH3 domain; Transport;
Voltage-gated channel.
CHAIN 1 655 Voltage-dependent L-type calcium channel
subunit beta-2.
/FTId=PRO_0000144052.
DOMAIN 110 179 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
SITE 544 544 Required for CaMK2D-binding.
{ECO:0000250}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VGC3}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 549 549 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 67 MVQSDTSKSPPVAAVAQESQMELLESAAPAGALGAQSYGKG
ARRKNRFKGSDGSTSSDTTSNSFVRQ -> MQCCGLVHRRR
VRVSY (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010730.
VAR_SEQ 1 67 MVQSDTSKSPPVAAVAQESQMELLESAAPAGALGAQSYGKG
ARRKNRFKGSDGSTSSDTTSNSFVRQ -> MKATWIRLLKR
AKGGRLKSSDIC (in isoform 3 and isoform
4). {ECO:0000303|PubMed:16141072}.
/FTId=VSP_010731.
VAR_SEQ 221 264 IDIDATGLDAEENDIPANHRSPKPSANSVTSPHSKEKRMPF
FKK -> KQKQKS (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010732.
CONFLICT 124 124 A -> R (in Ref. 1; BAD01474).
{ECO:0000305}.
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


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