CACB2_RABIT
ID CACB2_RABIT Reviewed; 632 AA.
AC P54288;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2A; 2B AND 2C).
RC TISSUE=Heart;
RX PubMed=1312465; DOI=10.1002/j.1460-2075.1992.tb05126.x;
RA Hullin R., Singer-Lahat D., Freichel M., Biel M., Dascal N., Hofmann F.,
RA Flockerzi V.;
RT "Calcium channel beta subunit heterogeneity: functional expression of
RT cloned cDNA from heart, aorta and brain.";
RL EMBO J. 11:885-890(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 34-415 IN COMPLEX WITH CACNA1S,
RP AND SUBUNIT.
RX PubMed=15134636; DOI=10.1016/s0896-6273(04)00250-8;
RA Opatowsky Y., Chen C.-C., Campbell K.P., Hirsch J.A.;
RT "Structural analysis of the voltage-dependent calcium channel beta subunit
RT functional core and its complex with the alpha1 interaction domain.";
RL Neuron 42:387-399(2004).
RN [3] {ECO:0007744|PDB:4DEX, ECO:0007744|PDB:4DEY}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 51-163 AND 229-448 IN COMPLEX
RP WITH CACNA1C, AND SUBUNIT.
RX PubMed=22649239; DOI=10.1523/jneurosci.5727-11.2012;
RA Almagor L., Chomsky-Hecht O., Ben-Mocha A., Hendin-Barak D., Dascal N.,
RA Hirsch J.A.;
RT "The role of a voltage-dependent Ca2+ channel intracellular linker: a
RT structure-function analysis.";
RL J. Neurosci. 32:7602-7613(2012).
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.
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 (PubMed:15134636). The channel complex
CC contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e.
CC it contains either CACNB1 or CACNB2 (By similarity). Interacts with
CC CACNA1C (PubMed:22649239). Interacts with RRAD. Interaction with RRAD
CC regulates the trafficking of CACNA1C to the cell membrane. Interacts
CC with TMIGD2 (By similarity). Interacts with CAMK2D. Interacts with
CC CBARP (By similarity). Interacts with CAMK2A (By similarity).
CC {ECO:0000250|UniProtKB:Q08289, ECO:0000250|UniProtKB:Q8VGC3,
CC ECO:0000269|PubMed:22649239, ECO:0000305|PubMed:15134636}.
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=3;
CC Name=2B;
CC IsoId=P54288-1; Sequence=Displayed;
CC Name=2A;
CC IsoId=P54288-2; Sequence=VSP_000632;
CC Name=2C;
CC IsoId=P54288-3; Sequence=VSP_000633;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart, aorta and brain.
CC -!- PTM: Regulated through phosphorylation at Thr-526 by CaMK2D.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; X64298; CAA45576.1; -; mRNA.
DR EMBL; X64297; CAA45575.1; -; mRNA.
DR EMBL; X64299; CAA45577.1; -; mRNA.
DR PIR; S21046; S21046.
DR PIR; S21048; S21048.
DR RefSeq; NP_001075865.1; NM_001082396.1. [P54288-1]
DR RefSeq; XP_017203069.1; XM_017347580.1. [P54288-3]
DR PDB; 1T3L; X-ray; 2.20 A; A=51-163, A=229-448.
DR PDB; 1T3S; X-ray; 2.30 A; A=51-163, A=229-422.
DR PDB; 4DEX; X-ray; 2.00 A; A=51-163, A=229-448.
DR PDB; 4DEY; X-ray; 1.95 A; A=51-163, A=229-448.
DR PDBsum; 1T3L; -.
DR PDBsum; 1T3S; -.
DR PDBsum; 4DEX; -.
DR PDBsum; 4DEY; -.
DR AlphaFoldDB; P54288; -.
DR SMR; P54288; -.
DR BioGRID; 1172298; 2.
DR STRING; 9986.ENSOCUP00000021223; -.
DR ChEMBL; CHEMBL3638171; -.
DR iPTMnet; P54288; -.
DR Ensembl; ENSOCUT00000043808; ENSOCUP00000027460; ENSOCUG00000014849. [P54288-3]
DR Ensembl; ENSOCUT00000051118; ENSOCUP00000040459; ENSOCUG00000014849. [P54288-1]
DR Ensembl; ENSOCUT00000062808; ENSOCUP00000034129; ENSOCUG00000014849. [P54288-2]
DR GeneID; 100009277; -.
DR KEGG; ocu:100009277; -.
DR CTD; 783; -.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR InParanoid; P54288; -.
DR OrthoDB; 926074at2759; -.
DR EvolutionaryTrace; P54288; -.
DR Proteomes; UP000001811; Chromosome 16.
DR Bgee; ENSOCUG00000014849; Expressed in heart and 16 other tissues.
DR ExpressionAtlas; P54288; baseline.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:Ensembl.
DR GO; GO:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; IEA:Ensembl.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; IEA:Ensembl.
DR GO; GO:0070509; P:calcium ion import; IEA:Ensembl.
DR GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; IEA:Ensembl.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
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 SMART; SM00326; SH3; 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; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain; Transport;
KW Voltage-gated channel.
FT CHAIN 1..632
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-2"
FT /id="PRO_0000144053"
FT DOMAIN 86..155
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 20..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 521
FT /note="Required for CaMK2D-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VGC3"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT MOD_RES 526
FT /note="Phosphothreonine; by CaMK2D"
FT /evidence="ECO:0000250|UniProtKB:Q8VGC3"
FT VAR_SEQ 1..43
FT /note="MNQASGLDLLKISYGKGARRKNRFKGSDGSTSSDTTSNSFVRQ -> MLDRH
FT LAAPHTQGLVLE (in isoform 2A)"
FT /evidence="ECO:0000303|PubMed:1312465"
FT /id="VSP_000632"
FT VAR_SEQ 197..240
FT /note="IDIDATGLDAEENDIPANHRSPKPSANSVTSPHSKEKRMPFFKK -> KQKQ
FT KS (in isoform 2C)"
FT /evidence="ECO:0000303|PubMed:1312465"
FT /id="VSP_000633"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 267..283
FT /evidence="ECO:0007829|PDB:4DEY"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:4DEX"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:1T3L"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:4DEY"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4DEY"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 391..403
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:4DEY"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:4DEY"
FT HELIX 418..436
FT /evidence="ECO:0007829|PDB:4DEY"
SQ SEQUENCE 632 AA; 70944 MW; EB6873D1F8DEB5D4 CRC64;
MNQASGLDLL KISYGKGARR KNRFKGSDGS TSSDTTSNSF VRQGSADSYT SRPSDSDVSL
EEDREAVRRE AERQAQAQLE KAKTKPVAFA VRTNVSYSAA HEDDVPVPGM AISFEAKDFL
HVKEKFNNDW WIGRLVKEGC EIGFIPSPVK LENMRLQHEQ RAKQGKFYSS KSGGNSSSSL
GDIVPSSRKS TPPSSAIDID ATGLDAEEND IPANHRSPKP SANSVTSPHS KEKRMPFFKK
TEHTPPYDVV PSMRPVVLVG PSLKGYEVTD MMQKALFDFL KHRFEGRISI TRVTADISLA
KRSVLNNPSK HAIIERSNTR SSLAEVQSEI ERIFELARTL QLVVLDADTI NHPAQLSKTS
LAPIVVYVKI SSPKVLQRLI KSRGKSQAKH LNVQMVAADK LAQCPPELFD VILDENQLED
ACEHLADYLE AYWKATHPPS SNLPNPLLSR TLATSALPVS PTLASNSQGS QGDQRTDRSA
PARSASQAEE EPCLEPAKKS QHRSSSSAPH HNHRSGTSRG LSRQETFDSE TQESRDSAYV
EPKEDYSHEH VDHYAPHRDH NHRDETHRSS DHRHRETRHR SRDMDREQDH NECNKQRSRH
KSKDRYCDKD GEVISKKRNE AGEWNRDVYI RQ
