CACB1_BOVIN
ID CACB1_BOVIN Reviewed; 598 AA.
AC Q9MZL7; Q9MZL6;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit beta-1;
DE Short=CAB1;
DE AltName: Full=Calcium channel voltage-dependent subunit beta 1;
GN Name=CACNB1;
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] (ISOFORMS 1 AND 2), FUNCTION, AND SUBUNIT.
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: Regulatory subunit of L-type calcium channels
CC (PubMed:10684870). Regulates the activity of L-type calcium channels
CC that contain CACNA1A as pore-forming subunit (By similarity). Regulates
CC the activity of L-type calcium channels that contain CACNA1C as pore-
CC forming subunit and increases the presence of the channel complex at
CC the cell membrane. Required for functional expression L-type calcium
CC channels that contain CACNA1D as pore-forming subunit (By similarity).
CC Regulates the activity of L-type calcium channels that contain CACNA1B
CC as pore-forming subunit (PubMed:10684870).
CC {ECO:0000250|UniProtKB:P19517, ECO:0000250|UniProtKB:Q02641,
CC ECO:0000269|PubMed:10684870}.
CC -!- SUBUNIT: Regulatory subunit of L-type calcium channels that consist of
CC a pore-forming alpha subunit and auxiliary beta, gamma and delta
CC subunits (PubMed:10684870). Interacts with CACNA1A, CACNA1B, CACNA1C
CC and CACNA1S. Component of a calcium channel complex consisting of a
CC pore-forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1
CC or CACNB2, CACNG1 and CACNA2D1. Identified in a complex with CACNA1C.
CC Identified in a complex with the L-type calcium channel subunits
CC CACNA1C, CACNA2D1, CACNB1 and one of the gamma subunits (CACNG4,
CC CACNG6, CACNG7, or CACNG8) (By similarity). Part of a L-type calcium
CC channel complex that contains CACNA1D, CACNA2D1 and CACNB1 (By
CC similarity). Part of a L-type calcium channel complex that contains
CC CACNA1B, CACNA2D1 and CACNB1 (PubMed:10684870). Interacts with JSRP1.
CC Interacts with RYR1 (By similarity). Interacts with CBARP (By
CC similarity). {ECO:0000250|UniProtKB:P19517,
CC ECO:0000250|UniProtKB:P54283, ECO:0000250|UniProtKB:Q02641,
CC ECO:0000250|UniProtKB:Q8R3Z5, ECO:0000269|PubMed:10684870}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P19517}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P19517}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P19517}. Cell membrane
CC {ECO:0000250|UniProtKB:Q02641}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P19517}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Beta-1B, CACNB1B;
CC IsoId=Q9MZL7-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta-1C, CACNB1C;
CC IsoId=Q9MZL7-2; Sequence=VSP_000621, VSP_000622;
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AF174415; AAF26679.1; -; mRNA.
DR EMBL; AF174416; AAF26680.1; -; mRNA.
DR RefSeq; NP_787013.1; NM_175819.2. [Q9MZL7-1]
DR AlphaFoldDB; Q9MZL7; -.
DR SMR; Q9MZL7; -.
DR STRING; 9913.ENSBTAP00000040778; -.
DR PaxDb; Q9MZL7; -.
DR PRIDE; Q9MZL7; -.
DR Ensembl; ENSBTAT00000084808; ENSBTAP00000067820; ENSBTAG00000002036. [Q9MZL7-1]
DR GeneID; 327703; -.
DR KEGG; bta:327703; -.
DR CTD; 782; -.
DR VEuPathDB; HostDB:ENSBTAG00000002036; -.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_3_1_1; -.
DR InParanoid; Q9MZL7; -.
DR OrthoDB; 926074at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000002036; Expressed in laryngeal cartilage and 102 other tissues.
DR ExpressionAtlas; Q9MZL7; baseline and differential.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
DR GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
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 Gene3D; 3.40.50.300; -; 1.
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; IPR005443; VDCC_L_b1su.
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; PR01627; LCACHANNELB1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Cell membrane; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain; Transport; Voltage-gated channel.
FT CHAIN 1..598
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-1"
FT /id="PRO_0000144045"
FT DOMAIN 100..169
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3Z5"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3Z5"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3Z5"
FT VAR_SEQ 445..478
FT /note="GPYLASGDQSLERATGEHASVHEYPGELGQPPGL -> VQVLTSLRRNLSFW
FT GGLEASQRARAVPQQQEHTV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10684870"
FT /id="VSP_000621"
FT VAR_SEQ 479..598
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10684870"
FT /id="VSP_000622"
SQ SEQUENCE 598 AA; 65749 MW; 9DBD44364C96B823 CRC64;
MVQKTSMSRG PYPSSQEIPM EVFDPSPQGK YSKRKGRFKR SDGSTSSDTT SNSFVRQGSA
ESYTSRPSDS DVSLEEDREA LRKEAERQAL AQLEKAKTKP VAFAVRTNVG YNPSPGDEVP
VQGVAITFEP KDFLHIKEKY NNDWWIGRLV KEGCEVGFIP SPVKLDSLRL LQEQKLRQNR
LSSSKSGDNS SSSLGDVVTG TRRPTPPASA KQKQKSTEHV PPYDVVPSMR PIILVGPSLK
GYEVTDMMQK ALFDFLKHRF DGRISITRVT ADISLAKRSV LNNPSKHIII ERSNTRSSLA
EVQSEIERIF ELARTLQLVA LDADTINHPA QLSKTSLAPI IVYIKITSPK VLQRLIKSRG
KSQSKHLNVQ IAASEKLAQC PPEMFDIILD ENQLEDACEH LAEYLEAYWK ATHPPSSTPP
NPLLNRTMAT AALAASPAPV SNLQGPYLAS GDQSLERATG EHASVHEYPG ELGQPPGLYP
SSHPPGRAGT LRALSRQDTF DADTPGNRNS AYTELGDSCV DMETDPSEGP GLGDPAGGST
PPARQGSWED EEEDYEEELT DNRNRGRNKA RYCAEGGGPV LGRNKNELEG WGRGVYIR
