CACB3_HUMAN
ID CACB3_HUMAN Reviewed; 484 AA.
AC P54284; A8K0Z4; B7Z4Q1; B7Z973; B7ZAK8; F5GZW7; F5H2P6; F8VSG3; Q13913;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 201.
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; Synonyms=CACNLB3 {ECO:0000303|PubMed:7557998};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Murakami M., Klugbauer N., Flockerzi V.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7557998; DOI=10.1006/geno.1995.1048;
RA Yamada Y., Masuda K., Li Q., Ihara Y., Kubota A., Miura T., Nakamura K.,
RA Fujii Y., Seino S., Seino Y.;
RT "The structures of the human calcium channel alpha 1 subunit (CACNL1A2) and
RT beta subunit (CACNLB3) genes.";
RL Genomics 27:312-319(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Furneaux H.M.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8119293; DOI=10.1111/j.1432-1033.1994.tb18621.x;
RA Collin T., Lory P., Taviaux S., Courtieu C., Guilbault P., Berta P.,
RA Nargeot J.;
RT "Cloning, chromosomal location and functional expression of the human
RT voltage-dependent calcium-channel beta 3 subunit.";
RL Eur. J. Biochem. 220:257-262(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain, Small intestine, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH CACNA2D4, AND IDENTIFICATION IN A COMPLEX WITH CACNA1C.
RX PubMed=12181424; DOI=10.1124/mol.62.3.485;
RA Qin N., Yagel S., Momplaisir M.-L., Codd E.E., D'Andrea M.R.;
RT "Molecular cloning and characterization of the human voltage-gated calcium
RT channel alpha(2)delta-4 subunit.";
RL Mol. Pharmacol. 62:485-496(2002).
RN [10]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [11]
RP INTERACTION WITH CACNA1C, AND SUBUNIT.
RX PubMed=29742403; DOI=10.1016/j.bpj.2018.03.029;
RA Bartels P., Yu D., Huang H., Hu Z., Herzig S., Soong T.W.;
RT "Alternative Splicing at N Terminus and Domain I Modulates CaV1.2
RT Inactivation and Surface Expression.";
RL Biophys. J. 114:2095-2106(2018).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 38-361 IN COMPLEX WITH
RP HUMAN CAV2.2/CACNA1B AND ALPHA2DELTA-1 SUBUNIT IN PRESENCE AND ABSENCE OF
RP THE OMEGA-CONOTOXIN MVIIA, DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
RX PubMed=34234349; DOI=10.1038/s41586-021-03699-6;
RA Gao S., Yao X., Yan N.;
RT "Structure of human Cav2.2 channel blocked by the painkiller ziconotide.";
RL Nature 596:143-147(2021).
CC -!- FUNCTION: Regulatory subunit of the voltage-gated calcium channel that
CC gives rise to L-type calcium currents (PubMed:8119293). Increases
CC CACNA1B peak calcium current and shifts the voltage dependencies of
CC channel activation and inactivation (By similarity). Increases CACNA1C
CC peak calcium current and shifts the voltage dependencies of channel
CC activation and inactivation (By similarity).
CC {ECO:0000250|UniProtKB:P54287, ECO:0000250|UniProtKB:Q9MZL3,
CC ECO:0000269|PubMed:8119293}.
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 (PubMed:29742403). The channel complex contains alpha, beta,
CC gamma and delta subunits in a 1:1:1:1 ratio (Probable). Interacts with
CC CACNA2D4 (PubMed:12181424). Interacts with FASLG (PubMed:19807924).
CC Interacts with CBARP; prevents the interaction of CACNB3 with the alpha
CC subunit CACNA1C thereby negatively regulating the activity of the
CC corresponding calcium channel (By similarity).
CC {ECO:0000250|UniProtKB:P54287, ECO:0000269|PubMed:12181424,
CC ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:29742403, ECO:0000305}.
CC -!- INTERACTION:
CC P54284; Q9H1P6: C20orf85; NbExp=3; IntAct=EBI-1184651, EBI-12155483;
CC P54284; Q13936: CACNA1C; NbExp=2; IntAct=EBI-1184651, EBI-1038838;
CC P54284; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-1184651, EBI-742887;
CC P54284; Q6FI81: CIAPIN1; NbExp=5; IntAct=EBI-1184651, EBI-750511;
CC P54284; P56545-3: CTBP2; NbExp=8; IntAct=EBI-1184651, EBI-10171902;
CC P54284; P55040: GEM; NbExp=8; IntAct=EBI-1184651, EBI-744104;
CC P54284; P50221: MEOX1; NbExp=3; IntAct=EBI-1184651, EBI-2864512;
CC P54284; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-1184651, EBI-11522433;
CC P54284; Q15477: SKIV2L; NbExp=3; IntAct=EBI-1184651, EBI-373226;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:34234349}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=3A;
CC IsoId=P54284-1; Sequence=Displayed;
CC Name=2; Synonyms=3B;
CC IsoId=P54284-2; Sequence=VSP_000634;
CC Name=3;
CC IsoId=P54284-3; Sequence=VSP_046708;
CC Name=4;
CC IsoId=P54284-4; Sequence=VSP_046709;
CC Name=5;
CC IsoId=P54284-5; Sequence=VSP_046710;
CC -!- TISSUE SPECIFICITY: Expressed mostly in brain, colon and ovary.
CC {ECO:0000269|PubMed:8119293}.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; X76555; CAA54055.1; -; mRNA.
DR EMBL; X76556; CAA54056.1; -; mRNA.
DR EMBL; D43704; BAA07803.1; -; Genomic_DNA.
DR EMBL; U07139; AAA95958.1; -; mRNA.
DR EMBL; L27584; AAA19799.1; -; mRNA.
DR EMBL; AK289709; BAF82398.1; -; mRNA.
DR EMBL; AK297639; BAH12637.1; -; mRNA.
DR EMBL; AK304537; BAH14209.1; -; mRNA.
DR EMBL; AK316323; BAH14694.1; -; mRNA.
DR EMBL; AC117498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58008.1; -; Genomic_DNA.
DR EMBL; BC041811; AAH41811.1; -; mRNA.
DR CCDS; CCDS55821.1; -. [P54284-3]
DR CCDS; CCDS55822.1; -. [P54284-4]
DR CCDS; CCDS55823.1; -. [P54284-5]
DR CCDS; CCDS8769.1; -. [P54284-1]
DR PIR; S39315; S39315.
DR PIR; S39316; S39316.
DR PIR; S41211; S41211.
DR RefSeq; NP_000716.2; NM_000725.3. [P54284-1]
DR RefSeq; NP_001193844.1; NM_001206915.1. [P54284-5]
DR RefSeq; NP_001193845.1; NM_001206916.1. [P54284-4]
DR RefSeq; NP_001193846.1; NM_001206917.1. [P54284-3]
DR PDB; 7MIX; EM; 3.00 A; C=1-484.
DR PDB; 7MIY; EM; 3.10 A; C=1-484.
DR PDBsum; 7MIX; -.
DR PDBsum; 7MIY; -.
DR AlphaFoldDB; P54284; -.
DR SMR; P54284; -.
DR BioGRID; 107238; 30.
DR DIP; DIP-39138N; -.
DR IntAct; P54284; 19.
DR STRING; 9606.ENSP00000301050; -.
DR BindingDB; P54284; -.
DR ChEMBL; CHEMBL3351206; -.
DR DrugBank; DB01118; Amiodarone.
DR DrugBank; DB09231; Benidipine.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugBank; DB09232; Cilnidipine.
DR DrugBank; DB04855; Dronedarone.
DR DrugBank; DB06751; Drotaverine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB00153; Ergocalciferol.
DR DrugBank; DB13961; Fish oil.
DR DrugBank; DB09236; Lacidipine.
DR DrugBank; DB00825; Levomenthol.
DR DrugBank; DB00653; Magnesium sulfate.
DR DrugBank; DB09238; Manidipine.
DR DrugBank; DB01388; Mibefradil.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB00393; Nimodipine.
DR DrugBank; DB00252; Phenytoin.
DR DrugBank; DB00243; Ranolazine.
DR DrugBank; DB00421; Spironolactone.
DR DrugBank; DB00273; Topiramate.
DR DrugBank; DB09089; Trimebutine.
DR TCDB; 8.A.22.1.3; the ca(2+) channel auxiliary subunit Beta types 1-4 (cca-Beta) family.
DR iPTMnet; P54284; -.
DR PhosphoSitePlus; P54284; -.
DR BioMuta; CACNB3; -.
DR DMDM; 1705683; -.
DR EPD; P54284; -.
DR jPOST; P54284; -.
DR MassIVE; P54284; -.
DR MaxQB; P54284; -.
DR PaxDb; P54284; -.
DR PeptideAtlas; P54284; -.
DR PRIDE; P54284; -.
DR ProteomicsDB; 25153; -.
DR ProteomicsDB; 26032; -.
DR ProteomicsDB; 28606; -.
DR ProteomicsDB; 56673; -. [P54284-1]
DR ProteomicsDB; 56674; -. [P54284-2]
DR Antibodypedia; 13690; 212 antibodies from 30 providers.
DR DNASU; 784; -.
DR Ensembl; ENST00000301050.7; ENSP00000301050.2; ENSG00000167535.8. [P54284-1]
DR Ensembl; ENST00000536187.6; ENSP00000444160.2; ENSG00000167535.8. [P54284-4]
DR Ensembl; ENST00000540990.5; ENSP00000445495.1; ENSG00000167535.8. [P54284-3]
DR Ensembl; ENST00000547230.5; ENSP00000448304.1; ENSG00000167535.8. [P54284-5]
DR GeneID; 784; -.
DR KEGG; hsa:784; -.
DR MANE-Select; ENST00000301050.7; ENSP00000301050.2; NM_000725.4; NP_000716.2.
DR UCSC; uc001rsl.3; human. [P54284-1]
DR CTD; 784; -.
DR DisGeNET; 784; -.
DR GeneCards; CACNB3; -.
DR HGNC; HGNC:1403; CACNB3.
DR HPA; ENSG00000167535; Tissue enhanced (brain).
DR MIM; 601958; gene.
DR neXtProt; NX_P54284; -.
DR OpenTargets; ENSG00000167535; -.
DR PharmGKB; PA89; -.
DR VEuPathDB; HostDB:ENSG00000167535; -.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_0_1_1; -.
DR InParanoid; P54284; -.
DR OMA; PCQGSAD; -.
DR OrthoDB; 926074at2759; -.
DR PhylomeDB; P54284; -.
DR TreeFam; TF316195; -.
DR PathwayCommons; P54284; -.
DR Reactome; R-HSA-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR Reactome; R-HSA-422356; Regulation of insulin secretion.
DR SignaLink; P54284; -.
DR BioGRID-ORCS; 784; 212 hits in 1074 CRISPR screens.
DR ChiTaRS; CACNB3; human.
DR GeneWiki; CACNB3; -.
DR GenomeRNAi; 784; -.
DR Pharos; P54284; Tbio.
DR PRO; PR:P54284; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P54284; protein.
DR Bgee; ENSG00000167535; Expressed in cortical plate and 172 other tissues.
DR ExpressionAtlas; P54284; baseline and differential.
DR Genevisible; P54284; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
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:0005245; F:voltage-gated calcium channel activity; TAS:ProtInc.
DR GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0060402; P:calcium ion transport into cytosol; ISS:BHF-UCL.
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:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0098903; P:regulation of membrane repolarization during action potential; ISS:BHF-UCL.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Cytoplasm; Ion channel; Ion transport; Phosphoprotein;
KW Reference proteome; SH3 domain; Transport; Voltage-gated channel.
FT CHAIN 1..484
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-3"
FT /id="PRO_0000144056"
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 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 VAR_SEQ 1..15
FT /note="MYDDSYVPGFEDSEA -> ME (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046708"
FT VAR_SEQ 1..15
FT /note="MYDDSYVPGFEDSEA -> MSFSDSSATFLLNE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046709"
FT VAR_SEQ 57..97
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_046710"
FT VAR_SEQ 440..484
FT /note="HRQHTSGLPSANGHDPQDRLLAQDSEHNHSDRNWQRNRPWPKDSY -> QCQ
FT LLSLL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_000634"
FT VARIANT 423
FT /note="R -> H (in dbSNP:rs2229954)"
FT /id="VAR_024384"
FT CONFLICT 7
FT /note="V -> L (in Ref. 4; AAA19799)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="Missing (in Ref. 4; AAA19799)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="V -> E (in Ref. 4; AAA19799)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="N -> D (in Ref. 5; BAH14694)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="Q -> R (in Ref. 5; BAH14209)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="M -> T (in Ref. 5; BAH12637)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="S -> P (in Ref. 5; BAH12637)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="Missing (in Ref. 4; AAA19799)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="H -> L (in Ref. 4; AAA19799)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="S -> T (in Ref. 4; AAA19799)"
FT /evidence="ECO:0000305"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:7MIY"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:7MIX"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:7MIY"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:7MIX"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7MIX"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 247..262
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 342..359
FT /evidence="ECO:0007829|PDB:7MIX"
SQ SEQUENCE 484 AA; 54532 MW; 19CD3549F5A8E17A CRC64;
MYDDSYVPGF EDSEAGSADS YTSRPSLDSD VSLEEDRESA RREVESQAQQ QLERAKHKPV
AFAVRTNVSY CGVLDEECPV QGSGVNFEAK DFLHIKEKYS NDWWIGRLVK EGGDIAFIPS
PQRLESIRLK QEQKARRSGN PSSLSDIGNR RSPPPSLAKQ KQKQAEHVPP 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 DAYQDLYQPH RQHTSGLPSA NGHDPQDRLL AQDSEHNHSD RNWQRNRPWP
KDSY
