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

 CACB2_RAT               Reviewed;         655 AA.
Q8VGC3; Q811Q6; Q811Q7; Q91ZJ8; Q9QUU7;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 2.
07-NOV-2018, entry version 130.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=1370480;
Perez-Reyes E., Castellano A., Kim H.S., Bertrand P., Baggstrom E.,
Lacerda A.E., Wei X.Y., Birnbaumer L.;
"Cloning and expression of a cardiac/brain beta subunit of the L-type
calcium channel.";
J. Biol. Chem. 267:1792-1797(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND ALTERNATIVE SPLICING.
STRAIN=Wistar; TISSUE=Heart;
PubMed=11604404; DOI=10.1074/jbc.M108049200;
Yamada Y., Nagashima M., Tsutsuura M., Kobayashi T., Seki S.,
Makita N., Horio Y., Tohse N.;
"Cloning of a functional splice variant of L-type calcium channel
beta2 subunit from rat heart.";
J. Biol. Chem. 276:47163-47170(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), FUNCTION, AND
SUBCELLULAR LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Heart;
PubMed=12042350; DOI=10.1113/jphysiol.2002.018515;
Colecraft H.M., Alseikhan B., Takahashi S.X., Chaudhuri D.,
Mittman S., Yegnasubramanian V., Alvania R.S., Johns D.C., Marban E.,
Yue D.T.;
"Novel functional properties of Ca(2+) channel beta subunits revealed
by their expression in adult rat heart cells.";
J. Physiol. (Lond.) 541:435-452(2002).
[4]
INTERACTION WITH CAMK2D, AND PHOSPHORYLATION AT THR-549 BY CAMK2D.
PubMed=20194790; DOI=10.1073/pnas.0913760107;
Koval O.M., Guan X., Wu Y., Joiner M.L., Gao Z., Chen B.,
Grumbach I.M., Luczak E.D., Colbran R.J., Song L.S., Hund T.J.,
Mohler P.J., Anderson M.E.;
"CaV1.2 beta-subunit coordinates CaMKII-triggered cardiomyocyte death
and afterdepolarizations.";
Proc. Natl. Acad. Sci. U.S.A. 107:4996-5000(2010).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND SER-203, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[6]
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).
[7] {ECO:0000244|PDB:1T0H, ECO:0000244|PDB:1T0J}
X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 68-476 IN COMPLEX WITH
CACNA1C.
PubMed=15141227; DOI=10.1038/nature02588;
Van Petegem F., Clark K.A., Chatelain F.C., Minor D.L. Jr.;
"Structure of a complex between a voltage-gated calcium channel beta-
subunit and an alpha-subunit domain.";
Nature 429:671-675(2004).
[8] {ECO:0000244|PDB:3JBR}
STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF 68-475 IN COMPLEX
WITH CACNA1S; CACNG1 AND CACNA2D1, AND SUBUNIT.
PubMed=26680202; DOI=10.1126/science.aad2395;
Wu J., Yan Z., Li Z., Yan C., Lu S., Dong M., Yan N.;
"Structure of the voltage-gated calcium channel Cav1.1 complex.";
Science 350:2395-2395(2015).
-!- 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:11604404, ECO:0000269|PubMed:12042350,
ECO:0000269|PubMed:1370480}.
-!- 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 (PubMed:26680202). 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
(PubMed:26680202). Interacts with CACNA1C (PubMed:15141227).
Interacts with RRAD. Interaction with RRAD regulates the
trafficking of CACNA1C to the cell membrane (By similarity).
Interacts with TMIGD2 (By similarity). Interacts with CAMK2D
(PubMed:20194790). Interacts with CBARP (PubMed:24751537).
Interacts with CAMK2A (By similarity).
{ECO:0000250|UniProtKB:Q08289, ECO:0000269|PubMed:15141227,
ECO:0000269|PubMed:20194790, ECO:0000269|PubMed:24751537,
ECO:0000269|PubMed:26680202}.
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
{ECO:0000269|PubMed:12042350}; Peripheral membrane protein
{ECO:0000269|PubMed:12042350}; Cytoplasmic side
{ECO:0000269|PubMed:12042350}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8VGC3-1; Sequence=Displayed;
Name=2;
IsoId=Q8VGC3-2; Sequence=VSP_010734;
Name=3; Synonyms=Beta-2c;
IsoId=Q8VGC3-3; Sequence=VSP_010733;
Name=4; Synonyms=Beta-2e;
IsoId=Q8VGC3-4; Sequence=VSP_010735;
Name=5; Synonyms=Beta-2b;
IsoId=Q8VGC3-5; Sequence=VSP_010736;
-!- TISSUE SPECIFICITY: Highly expressed in heart and brain, and at
lower levels in lung. {ECO:0000269|PubMed:11604404,
ECO:0000269|PubMed:1370480}.
-!- PTM: Regulated through phosphorylation at Thr-549 by CaMK2D.
{ECO:0000269|PubMed:20194790}.
-!- SIMILARITY: Belongs to the calcium channel beta subunit family.
{ECO:0000305}.
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EMBL; AF394941; AAL47074.1; -; mRNA.
EMBL; M80545; AAK14821.1; -; mRNA.
EMBL; AF423193; AAL16952.1; -; mRNA.
EMBL; AY190119; AAO38996.1; -; mRNA.
EMBL; AY190120; AAO38997.1; -; mRNA.
PIR; A42044; A42044.
RefSeq; NP_446303.1; NM_053851.1.
RefSeq; XP_006254360.1; XM_006254298.3.
RefSeq; XP_006254365.1; XM_006254303.3. [Q8VGC3-5]
UniGene; Rn.10739; -.
PDB; 1T0H; X-ray; 1.97 A; A=68-196, B=254-476.
PDB; 1T0J; X-ray; 2.00 A; A=68-196, B=254-476.
PDB; 3JBR; EM; 4.20 A; B=68-196, B=254-475.
PDB; 5V2P; X-ray; 2.00 A; A=68-189, A=254-476.
PDB; 5V2Q; X-ray; 1.70 A; A=68-189, A=254-476.
PDBsum; 1T0H; -.
PDBsum; 1T0J; -.
PDBsum; 3JBR; -.
PDBsum; 5V2P; -.
PDBsum; 5V2Q; -.
ProteinModelPortal; Q8VGC3; -.
SMR; Q8VGC3; -.
DIP; DIP-29590N; -.
IntAct; Q8VGC3; 4.
STRING; 10116.ENSRNOP00000037354; -.
CarbonylDB; Q8VGC3; -.
iPTMnet; Q8VGC3; -.
PhosphoSitePlus; Q8VGC3; -.
SwissPalm; Q8VGC3; -.
PaxDb; Q8VGC3; -.
PRIDE; Q8VGC3; -.
GeneID; 116600; -.
KEGG; rno:116600; -.
UCSC; RGD:67385; rat. [Q8VGC3-1]
CTD; 783; -.
RGD; 67385; Cacnb2.
eggNOG; KOG3812; Eukaryota.
eggNOG; ENOG410XRDI; LUCA.
HOGENOM; HOG000230979; -.
HOVERGEN; HBG050765; -.
InParanoid; Q8VGC3; -.
KO; K04863; -.
PhylomeDB; Q8VGC3; -.
BRENDA; 2.7.4.8; 5301.
EvolutionaryTrace; Q8VGC3; -.
PRO; PR:Q8VGC3; -.
Proteomes; UP000002494; Unplaced.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
GO; GO:0051015; F:actin filament binding; IDA:BHF-UCL.
GO; GO:0005246; F:calcium channel regulator activity; IDA:RGD.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051219; F:phosphoprotein binding; IPI:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0019901; F:protein kinase binding; IDA:RGD.
GO; GO:0005245; F:voltage-gated calcium channel activity; TAS:RGD.
GO; GO:0006816; P:calcium ion transport; TAS:RGD.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
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; IDA:BHF-UCL.
GO; GO:1901843; P:positive regulation of high voltage-gated calcium channel activity; IDA:BHF-UCL.
GO; GO:0072659; P:protein localization to plasma membrane; IDA: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; IDA:RGD.
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; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; 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_0000144054.
DOMAIN 110 179 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
SITE 544 544 Required for CaMK2D-binding.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CC27}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CC27}.
MOD_RES 549 549 Phosphothreonine; by CaMK2D.
{ECO:0000269|PubMed:20194790}.
VAR_SEQ 1 67 MVQSDTSKSPPIAAVAQESQMELLESAAPAGALGAQSYGKG
ARRKNRFKGSDDSTSSDTTSNSFVRQ -> MQCCGLVHRRR
VRVSR (in isoform 2).
{ECO:0000303|PubMed:1370480}.
/FTId=VSP_010734.
VAR_SEQ 1 67 MVQSDTSKSPPIAAVAQESQMELLESAAPAGALGAQSYGKG
ARRKNRFKGSDDSTSSDTTSNSFVRQ -> MKATWIRLLKR
AKGERLKDSDIC (in isoform 4).
{ECO:0000303|PubMed:12042350}.
/FTId=VSP_010735.
VAR_SEQ 1 67 MVQSDTSKSPPIAAVAQESQMELLESAAPAGALGAQSYGKG
ARRKNRFKGSDDSTSSDTTSNSFVRQ -> MLDRQLVSSQT
QSSIPG (in isoform 5).
{ECO:0000303|PubMed:12042350}.
/FTId=VSP_010736.
VAR_SEQ 1 36 MVQSDTSKSPPIAAVAQESQMELLESAAPAGALGAQ -> M
DQASGLDRLKI (in isoform 3).
{ECO:0000303|PubMed:12042350}.
/FTId=VSP_010733.
CONFLICT 53 53 D -> G (in Ref. 3; AAO38996).
{ECO:0000305}.
HELIX 91 106 {ECO:0000244|PDB:5V2Q}.
STRAND 113 119 {ECO:0000244|PDB:5V2Q}.
HELIX 125 127 {ECO:0000244|PDB:5V2Q}.
STRAND 143 151 {ECO:0000244|PDB:5V2Q}.
STRAND 154 161 {ECO:0000244|PDB:5V2Q}.
STRAND 167 170 {ECO:0000244|PDB:5V2Q}.
HELIX 172 186 {ECO:0000244|PDB:5V2Q}.
STRAND 270 274 {ECO:0000244|PDB:5V2Q}.
STRAND 280 283 {ECO:0000244|PDB:5V2Q}.
HELIX 291 307 {ECO:0000244|PDB:5V2Q}.
TURN 308 310 {ECO:0000244|PDB:5V2Q}.
STRAND 311 317 {ECO:0000244|PDB:5V2Q}.
HELIX 321 323 {ECO:0000244|PDB:5V2Q}.
HELIX 344 361 {ECO:0000244|PDB:5V2Q}.
STRAND 366 371 {ECO:0000244|PDB:5V2Q}.
HELIX 377 379 {ECO:0000244|PDB:5V2Q}.
TURN 380 382 {ECO:0000244|PDB:5V2Q}.
STRAND 388 392 {ECO:0000244|PDB:5V2Q}.
HELIX 397 406 {ECO:0000244|PDB:5V2Q}.
HELIX 409 412 {ECO:0000244|PDB:5V2Q}.
HELIX 415 427 {ECO:0000244|PDB:5V2Q}.
HELIX 430 433 {ECO:0000244|PDB:5V2Q}.
STRAND 435 438 {ECO:0000244|PDB:5V2Q}.
HELIX 443 461 {ECO:0000244|PDB:5V2Q}.
HELIX 464 466 {ECO:0000244|PDB:5V2Q}.
SEQUENCE 655 AA; 73226 MW; 0BD9B42FD4CDF52A CRC64;
MVQSDTSKSP PIAAVAQESQ MELLESAAPA GALGAQSYGK GARRKNRFKG SDDSTSSDTT
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 THPPSSNLPN PLLSRTLATS
TLPLSPTLAS NSQGSQGDQR TDRSAPRSAS QAEEEPCLEP VKKSQHRSSS ATHQNHRSGT
GRGLSRQETF DSETQESRDS AYVEPKEDYS HEHVDRYVPH REHNHREESH SSNGHRHREP
RHRTRDMGRD QDHNECSKQR SRHKSKDRYC DKEGEVISKR RSEAGEWNRD VYIRQ


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