CACB3_BOVIN
ID CACB3_BOVIN Reviewed; 484 AA.
AC Q9MZL3; Q08DF1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit beta-3;
DE Short=CAB3;
DE AltName: Full=Calcium channel voltage-dependent subunit beta 3;
GN Name=CACNB3;
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], AND FUNCTION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory subunit of the voltage-gated calcium channel that
CC gives rise to L-type calcium currents (PubMed:10684870). Increases
CC CACNA1B peak calcium current and shifts the voltage dependencies of
CC channel activation and inactivation (PubMed:10684870). Increases
CC CACNA1C peak calcium current and shifts the voltage dependencies of
CC channel activation and inactivation (By similarity).
CC {ECO:0000250|UniProtKB:P54287, ECO:0000269|PubMed:10684870}.
CC -!- SUBUNIT: Component of a calcium channel complex consisting of a pore-
CC forming alpha subunit (CACNA1C) and the ancillary subunits CACNB3 and
CC CACNA2D1. The channel complex contains alpha, beta, gamma and delta
CC subunits in a 1:1:1:1 ratio. Interacts with CACNA2D4. Interacts with
CC FASLG (By similarity). Interacts with CBARP; prevents the interaction
CC of CACNB3 with the alpha subunit CACNA1C thereby negatively regulating
CC the activity of the corresponding calcium channel (By similarity).
CC {ECO:0000250|UniProtKB:P54284, ECO:0000250|UniProtKB:P54287}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54285}.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF174419; AAF26683.1; -; mRNA.
DR EMBL; BC123784; AAI23785.1; -; mRNA.
DR RefSeq; NP_776934.1; NM_174509.3.
DR AlphaFoldDB; Q9MZL3; -.
DR SMR; Q9MZL3; -.
DR STRING; 9913.ENSBTAP00000029069; -.
DR PaxDb; Q9MZL3; -.
DR PRIDE; Q9MZL3; -.
DR GeneID; 282160; -.
DR KEGG; bta:282160; -.
DR CTD; 784; -.
DR eggNOG; KOG3812; Eukaryota.
DR HOGENOM; CLU_021995_0_1_1; -.
DR InParanoid; Q9MZL3; -.
DR OrthoDB; 926074at2759; -.
DR TreeFam; TF316195; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0005246; F:calcium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:UniProtKB.
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:1901843; P:positive regulation of high voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR CDD; cd12042; SH3_CACNB3; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR035760; CACNB3_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; IPR008079; VDCC_L_b3su.
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; PR01696; LCACHANNELB3.
DR SMART; SM00072; GuKc; 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; Cytoplasm; Ion channel;
KW Ion transport; Phosphoprotein; Reference proteome; SH3 domain; Transport;
KW Voltage-gated channel.
FT CHAIN 1..484
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-3"
FT /id="PRO_0000144055"
FT DOMAIN 59..128
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..345
FT /note="Mediates interaction with the alpha subunit"
FT /evidence="ECO:0000250|UniProtKB:P54287"
FT REGION 387..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54287"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54287"
FT CONFLICT 366..367
FT /note="GP -> AL (in Ref. 1; AAF26683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 54569 MW; CCD1FE1675CFB726 CRC64;
MYDDSYVPGF EDSEAGSADS YTSRPSLDSD VSLEEDRESA RREVESQAQQ QLERAKHKPV
AFAVRTNVSY CGVLDEECPV QGSGVNFEAK DFLHIKEKYS NDWWIGRLVK EGGDIAFIPS
PQRLESIRLK QEQKARRSGN PSSLSDIGSR RSPPPSLAKQ KQKQAEHIPP YDVVPSMRPV
VLVGPSLKGY EVTDMMQKAL FDFLKHRFDG RISITRVTAD LSLAKRSVLN NPGKRTIIER
SSARSSIAEV QSEIERIFEL AKSLQLVVLD ADTINHPAQL AKTSLAPIIV FVKVSSPKVL
QRLIRSRGKS QMKHLTVQMM AYDKLVQCPP ESFDVILDEN QLEDACEHLA EYLEVYWRAT
HHPAPGPGLL GPPSAIPGLQ NQQLLGERGE EHSPLERDSL MPSDEASESS RQAWTGSSQR
SSRHLEEDYA DAYHDLYQPH RQHTSGLPSA NGHDPQDRLL AQDSEHNHNE RNWQRNRPWP
KDSY
