CACB2_BOVIN
ID CACB2_BOVIN Reviewed; 603 AA.
AC Q9MZL5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10684870; DOI=10.1523/jneurosci.20-05-01685.2000;
RA Cahill A.L., Hurley J.H., Fox A.P.;
RT "Coexpression of cloned alpha(1B), beta(2a), and alpha(2)/delta subunits
RT produces non-inactivating calcium currents similar to those found in bovine
RT chromaffin cells.";
RL J. Neurosci. 20:1685-1693(2000).
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. 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. Interacts with CBARP (By similarity). Interacts with
CC CAMK2A (By similarity). {ECO:0000250|UniProtKB:Q08289,
CC ECO:0000250|UniProtKB:Q8VGC3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- PTM: Regulated through phosphorylation at Thr-497 by CaMK2D.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AF174417; AAF26681.1; -; mRNA.
DR RefSeq; NP_786983.1; NM_175789.2.
DR AlphaFoldDB; Q9MZL5; -.
DR SMR; Q9MZL5; -.
DR ComplexPortal; CPX-3193; Cardiac muscle VGCC complex.
DR IntAct; Q9MZL5; 2.
DR STRING; 9913.ENSBTAP00000029344; -.
DR BindingDB; Q9MZL5; -.
DR PaxDb; Q9MZL5; -.
DR PRIDE; Q9MZL5; -.
DR Ensembl; ENSBTAT00000029344; ENSBTAP00000029344; ENSBTAG00000022000.
DR GeneID; 327667; -.
DR KEGG; bta:327667; -.
DR CTD; 783; -.
DR VEuPathDB; HostDB:ENSBTAG00000022000; -.
DR VGNC; VGNC:26684; CACNB2.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_3_0_1; -.
DR InParanoid; Q9MZL5; -.
DR OrthoDB; 926074at2759; -.
DR TreeFam; TF316195; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000022000; Expressed in cardiac ventricle and 103 other tissues.
DR ExpressionAtlas; Q9MZL5; baseline and differential.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; SH3 domain;
KW Transport; Voltage-gated channel.
FT CHAIN 1..603
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-2"
FT /id="PRO_0000144050"
FT DOMAIN 59..128
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 135..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 492
FT /note="Required for CaMK2D-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VGC3"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT MOD_RES 497
FT /note="Phosphothreonine; by CaMK2D"
FT /evidence="ECO:0000250|UniProtKB:Q8VGC3"
SQ SEQUENCE 603 AA; 67842 MW; 217E10D1FA91B314 CRC64;
MQCCGLVHRR RARVSYGSAD SYTSRPSDSD VSLEEDREAV RREAERQAQA QLEKAKTKPV
AFAVRTNVSY SAAHEDDVPV PGMAISFEAK DFLHVKEKFN NDWWIGRLVK EGCEIGFIPS
PVKLENMRLQ HEQRAKQGKF YSSKSGGNSS SSLGDIVPSS RKSTPPSSAI DIDATGLDAE
DNDIPANHRS PKPSANSVTS PHSKEKRMPF FKKTEHTPPY DVVPSMRPVV LVGPSLKGYE
VTDMMQKALF DFLKHRFEGR ISITRVTADI SLAKRSVLNN PSKHAIIERS NTRSSLAEVQ
SEIERIFELA RTLQLVVLDA DTINHPAQLS KTSLAPIIVY VKISSPKVLQ RLIKSRGKSQ
AKHLNVQMVA ADKLAQCPPE LFDVILDENQ LEDACEHLAD YLEAYWKATH PPSSSLPNPL
LSRTLATSTL PVSPTLASNS QGSQGDQRTD RGAPGRSASQ AEEEHCPEPV KKAQHRSSTQ
HHNHRSGTSR GLSRQETLDS ETQESRDSAY AEPKEEYSHE HADHYAPHRD HNHREEPHGG
GEHRHREPRH RSRDPDREQD HNESNKQRSR HKSKDRYCDK DGEGLSRRRN EAADWNRDVY
IRQ