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   02-SEP-2026, entry version 173.
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}.
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; X61394; CAA43665.1; -; mRNA.
DR   PIR; S18304; S18304.
DR   RefSeq; NP_059042.2; NM_017346.2.
DR   AlphaFoldDB; P54283; -.
DR   SMR; P54283; -.
DR   BioGRID; 248426; 5.
DR   CORUM; P54283; -.
DR   DIP; DIP-33255N; -.
DR   FunCoup; P54283; 2087.
DR   IntAct; P54283; 1.
DR   STRING; 10116.ENSRNOP00000073177; -.
DR   BindingDB; P54283; -.
DR   ChEMBL; CHEMBL3885653; -.
DR   ChEMBL; CHEMBL3988639; -.
DR   GlyGen; P54283; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P54283; -.
DR   PhosphoSitePlus; P54283; -.
DR   PaxDb; 10116-ENSRNOP00000073177; -.
DR   ABCD; P54283; 1 sequenced antibody.
DR   GeneID; 50688; -.
DR   KEGG; rno:50688; -.
DR   UCSC; RGD:68382; rat.
DR   AGR; RGD:68382; -.
DR   CTD; 782; -.
DR   RGD; 68382; Cacnb1.
DR   eggNOG; KOG3812; Eukaryota.
DR   InParanoid; P54283; -.
DR   OrthoDB; 5962384at2759; -.
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:0005886; C:plasma membrane; ISS:UniProtKB.
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:0005246; F:calcium channel regulator activity; ISO: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: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   FunFam; 2.30.30.40:FF:000068; Voltage-dependent L-type calcium channel subunit beta-1 isoform 1; 1.
DR   FunFam; 3.40.50.300:FF:000432; Voltage-dependent L-type calcium channel subunit beta-1 isoform 1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR046937; CAB1-4_N_A-dom.
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   PANTHER; PTHR11824; VOLTAGE-DEPENDENT CALCIUM CHANNEL BETA SUBUNIT; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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..53
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..193
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..540
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..558
FT                   /note="Acidic 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
//