CACB1_RAT
ID CACB1_RAT Reviewed; 597 AA.
AC P54283;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 160.
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; Synonyms=Cacnlb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1657644; DOI=10.1016/0014-5793(91)81296-k;
RA Pragnell M., Sakamoto J., Jay S.D., Campbell K.P.;
RT "Cloning and tissue-specific expression of the brain calcium channel beta-
RT subunit.";
RL FEBS Lett. 291:253-258(1991).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21127204; DOI=10.1096/fj.10-172353;
RA Yang L., Katchman A., Morrow J.P., Doshi D., Marx S.O.;
RT "Cardiac L-type calcium channel (Cav1.2) associates with gamma subunits.";
RL FASEB J. 25:928-936(2011).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-47; SER-73; SER-186;
RP SER-193 AND SER-547, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP INTERACTION WITH CBARP.
RX PubMed=24751537; DOI=10.1083/jcb.201304101;
RA Beguin P., Nagashima K., Mahalakshmi R.N., Vigot R., Matsunaga A., Miki T.,
RA Ng M.Y., Ng Y.J., Lim C.H., Tay H.S., Hwang L.A., Firsov D., Tang B.L.,
RA Inagaki N., Mori Y., Seino S., Launey T., Hunziker W.;
RT "BARP suppresses voltage-gated calcium channel activity and Ca2+-evoked
RT exocytosis.";
RL J. Cell Biol. 205:233-249(2014).
CC -!- FUNCTION: Regulatory subunit of L-type calcium channels. Regulates the
CC activity of L-type calcium channels that contain CACNA1A as pore-
CC forming subunit (By similarity). Regulates the activity of L-type
CC calcium channels that contain CACNA1C as pore-forming subunit and
CC increases the presence of the channel complex at the cell membrane
CC (Probable). Required for functional expression L-type calcium channels
CC that contain CACNA1D as pore-forming subunit. Regulates the activity of
CC L-type calcium channels that contain CACNA1B as pore-forming subunit
CC (By similarity). {ECO:0000250|UniProtKB:P19517,
CC ECO:0000250|UniProtKB:Q02641, ECO:0000305|PubMed:21127204}.
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:21127204). Interacts with CACNA1A, CACNA1B, CACNA1C
CC and CACNA1S (By similarity). Component of a calcium channel complex
CC consisting of a pore-forming alpha subunit (CACNA1S) and the ancillary
CC subunits CACNB1 or CACNB2, CACNG1 and CACNA2D1. Identified in a complex
CC with CACNA1C (By similarity). Identified in a complex with the L-type
CC calcium channel subunits CACNA1C, CACNA2D1, CACNB1 and one of the gamma
CC subunits (CACNG4, CACNG6, CACNG7, or CACNG8) (PubMed:21127204). Part of
CC a L-type calcium channel complex that contains CACNA1D, CACNA2D1 and
CC CACNB1. Part of a L-type calcium channel complex that contains CACNA1B,
CC CACNA2D1 and CACNB1 (By similarity). Interacts with JSRP1. Interacts
CC with RYR1 (By similarity). Interacts with CBARP (PubMed:24751537).
CC {ECO:0000250|UniProtKB:P19517, ECO:0000250|UniProtKB:Q02641,
CC ECO:0000250|UniProtKB:Q8R3Z5, ECO:0000269|PubMed:21127204,
CC ECO:0000269|PubMed:24751537}.
CC -!- INTERACTION:
CC P54283; P54283: Cacnb1; NbExp=2; IntAct=EBI-349245, EBI-349245;
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 -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:1657644}.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; X61394; CAA43665.1; -; mRNA.
DR PIR; S18304; S18304.
DR RefSeq; NP_059042.1; NM_017346.1.
DR AlphaFoldDB; P54283; -.
DR SMR; P54283; -.
DR BioGRID; 248426; 4.
DR DIP; DIP-33255N; -.
DR IntAct; P54283; 1.
DR STRING; 10116.ENSRNOP00000006098; -.
DR BindingDB; P54283; -.
DR ChEMBL; CHEMBL3885653; -.
DR ChEMBL; CHEMBL3988639; -.
DR iPTMnet; P54283; -.
DR PhosphoSitePlus; P54283; -.
DR PaxDb; P54283; -.
DR PRIDE; P54283; -.
DR ABCD; P54283; 1 sequenced antibody.
DR GeneID; 50688; -.
DR KEGG; rno:50688; -.
DR UCSC; RGD:68382; rat.
DR CTD; 782; -.
DR RGD; 68382; Cacnb1.
DR eggNOG; KOG3812; Eukaryota.
DR InParanoid; P54283; -.
DR Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-RNO-5576893; Phase 2 - plateau phase.
DR PRO; PR:P54283; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0030315; C:T-tubule; ISO:RGD.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IDA:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
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:0006612; P:protein targeting to membrane; ISO:RGD.
DR GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:RGD.
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 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..597
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-1"
FT /id="PRO_0000144049"
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..597
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:0007744|PubMed:22673903"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3Z5"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 597 AA; 65680 MW; D95BF4982AF1FD5E CRC64;
MVQKSGMSRG PYPPSQEIPM EVFDPSPQGK YSKRKGRFKR SDGSTSSDTT SNSFVRQGSA
ESYTSRPSDS DVSLEEDREA LRKEAERQAL AQLEKAKTKP VAFAVRTNVG YNPSPGDEVP
VQGVAITFEP KDFLHIKEKY NNDWWIGRLV KEGCEVGFIP SPVKLDSLRL LQEQTLRQNR
LSSSKSGDNS SSSLGDVVTG TRRPTPPASA KQKQKSTEHV PPYDVVPSMR PIILVGPSLK
GYEVTDMMQK ALFDFLKHRF DGRISITRVT ADISLAKRSV LNNPSKHIII ERSNTRSSLA
EVQSEIERIF ELARTLQLVA LDADTINHPA QLSKTSLAPI IVYIKITSPK VLQRLIKSRG
KSQSKHLNVQ IAASEKLAQC PPEMFDIILD ENQLEDACEH LAEYLEAYWK ATHPPSRTPP
NPLLNRTMAT AALAVSPAPV SNLQGPYLVS GDQPLDRATG EHASVHEYPG ELGQPPGLYP
SNHPPGRAGT LWALSRQDTF DADTPGSRNS VYTEPGDSCV DMETDPSEGP GPGDPAGGGT
PPARQGSWEE EEDYEEEMTD NRNRGRNKAR YCAEGGGPVL GRNKNELEGW GQGVYIR
