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 02-SEP-2026, entry version 220. 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). RN [13] {ECO:0007744|PDB:8FHS, ECO:0007744|PDB:8WE6, ECO:0007744|PDB:8WE7, ECO:0007744|PDB:8WE8, ECO:0007744|PDB:8WE9} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) IN COMPLEX WITH RP CAV1.2/CACNA1C AND ALPHA-2/DELTA-1 SUBUNIT. RX PubMed=37972591; DOI=10.1016/j.cell.2023.10.007; RA Gao S., Yao X., Chen J., Huang G., Fan X., Xue L., Li Z., Wu T., Zheng Y., RA Huang J., Jin X., Wang Y., Wang Z., Yu Y., Liu L., Pan X., Song C., Yan N.; RT "Structural basis for human Cav1.2 inhibition by multiple drugs and the RT neurotoxin calciseptine."; RL Cell 186:5363-5374.e16(2023). 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; Q13936: CACNA1C; NbExp=8; IntAct=EBI-1184651, EBI-1038838; CC P54284; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-1184651, EBI-742887; CC P54284; Q6FI81: CIAPIN1; NbExp=7; IntAct=EBI-1184651, EBI-750511; CC P54284; Q9H1P6: CIMIP1; NbExp=3; IntAct=EBI-1184651, EBI-12155483; 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: SKIC2; 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}. 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; 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_000725.4. [P54284-1] DR RefSeq; NP_001193844.1; NM_001206915.2. [P54284-5] DR RefSeq; NP_001193845.1; NM_001206916.2. [P54284-4] DR RefSeq; NP_001193846.1; NM_001206917.2. [P54284-3] DR RefSeq; XP_047285481.1; XM_047429525.1. [P54284-1] DR RefSeq; XP_054229164.1; XM_054373189.1. [P54284-1] DR PDB; 7MIX; EM; 3.00 A; C=1-484. DR PDB; 7MIY; EM; 3.10 A; C=1-484. DR PDB; 7UHF; EM; 3.10 A; C=1-484. DR PDB; 7UHG; EM; 3.00 A; C=1-484. DR PDB; 8E59; EM; 3.10 A; C=1-484. DR PDB; 8E5A; EM; 3.30 A; C=1-484. DR PDB; 8E5B; EM; 3.30 A; C=1-484. DR PDB; 8EPL; EM; 3.10 A; B=1-484. DR PDB; 8FHS; EM; 3.30 A; C=1-484. DR PDB; 8WE6; EM; 2.90 A; C=1-484. DR PDB; 8WE7; EM; 3.20 A; C=1-484. DR PDB; 8WE8; EM; 2.90 A; C=1-484. DR PDB; 8WE9; EM; 3.00 A; C=1-484. DR PDB; 8X90; EM; 2.95 A; C=1-484. DR PDB; 8X91; EM; 3.11 A; C=1-484. DR PDB; 8X93; EM; 2.92 A; C=1-484. DR AlphaFoldDB; P54284; -. DR EMDB; EMD-23867; -. DR EMDB; EMD-23868; -. DR EMDB; EMD-26513; -. DR EMDB; EMD-26514; -. DR EMDB; EMD-27907; -. DR EMDB; EMD-27908; -. DR EMDB; EMD-27909; -. DR EMDB; EMD-28529; -. DR EMDB; EMD-29102; -. DR EMDB; EMD-37472; -. DR EMDB; EMD-37473; -. DR EMDB; EMD-37474; -. DR EMDB; EMD-37475; -. DR EMDB; EMD-38158; -. DR EMDB; EMD-38159; -. DR EMDB; EMD-38160; -. DR SMR; P54284; -. DR BioGRID; 107238; 30. DR ComplexPortal; CPX-8725; Cav1.1 voltage-gated calcium channel complex, CACNA2D1-CACNB3-CACNG1 variant. DR ComplexPortal; CPX-8742; Cav1.1 voltage-gated calcium channel complex, CACNA2D2-CACNB3-CACNG1 variant. DR ComplexPortal; CPX-8764; Cav1.1 voltage-gated calcium channel complex, CACNA2D3-CACNB3-CACNG1 variant. DR ComplexPortal; CPX-8772; Cav1.1 voltage-gated calcium channel complex, CACNA2D4-CACNB3-CACNG1 variant. DR ComplexPortal; CPX-8861; Cav1.2 voltage-gated calcium channel complex, CACNA2D1-CACNB3 variant. DR ComplexPortal; CPX-8866; Cav1.2 voltage-gated calcium channel complex, CACNA2D2-CACNB3 variant. DR ComplexPortal; CPX-8870; Cav1.2 voltage-gated calcium channel complex, CACNA2D3-CACNB3 variant. DR ComplexPortal; CPX-8875; Cav1.2 voltage-gated calcium channel complex, CACNA2D4-CACNB3 variant. DR CORUM; P54284; -. DR DIP; DIP-39138N; -. DR FunCoup; P54284; 671. DR IntAct; P54284; 30. DR NDEx; IQUERY-CP-CACNB3; 5 NDEx IQuery Curated Pathways. 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; DB09235; Efonidipine. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB00153; Ergocalciferol. DR DrugBank; DB12605; Etripamil. 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; DB00622; Nicardipine. DR DrugBank; DB06712; Nilvadipine. DR DrugBank; DB00393; Nimodipine. DR DrugBank; DB01054; Nitrendipine. DR DrugBank; DB00252; Phenytoin. DR DrugBank; DB00243; Ranolazine. DR DrugBank; DB00421; Spironolactone. DR DrugBank; DB00273; Topiramate. DR DrugBank; DB09089; Trimebutine. DR DrugBank; DB00661; Verapamil. 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 jPOST; P54284; -. DR MassIVE; P54284; -. DR PaxDb; 9606-ENSP00000301050; -. DR PeptideAtlas; P54284; -. DR ProteomicsDB; 25153; -. DR ProteomicsDB; 26032; -. DR ProteomicsDB; 28606; -. DR ProteomicsDB; 56673; -. [P54284-1] DR ProteomicsDB; 56674; -. [P54284-2] DR Pumba; P54284; -. DR Antibodypedia; 13690; 211 antibodies from 30 providers. DR DNASU; 784; -. DR Ensembl; ENST00000301050.7; ENSP00000301050.2; ENSG00000167535.9. [P54284-1] DR Ensembl; ENST00000536187.6; ENSP00000444160.2; ENSG00000167535.9. [P54284-4] DR Ensembl; ENST00000540990.5; ENSP00000445495.1; ENSG00000167535.9. [P54284-3] DR Ensembl; ENST00000547230.5; ENSP00000448304.1; ENSG00000167535.9. [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 AGR; HGNC:1403; -. DR ClinPGx; PA89; -. 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 OpenTargets; ENSG00000167535; -. DR VEuPathDB; HostDB:ENSG00000167535; -. DR eggNOG; KOG3812; Eukaryota. DR GeneTree; ENSGT00950000182837; -. DR HOGENOM; CLU_021995_0_1_1; -. DR InParanoid; P54284; -. DR OMA; MGEHESE; -. DR OrthoDB; 5962384at2759; -. DR PAN-GO; P54284; 4 GO annotations based on evolutionary models. DR PhylomeDB; P54284; -. 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 Reactome; R-HSA-9856532; Mechanical load activates signaling by PIEZO1 and integrins in osteocytes. DR SignaLink; P54284; -. DR Agora; ENSG00000167535; -. DR BioGRID-ORCS; 784; 228 hits in 1158 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. 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 174 other cell types or tissues. DR ExpressionAtlas; P54284; baseline and differential. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IPI:ComplexPortal. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0030315; C:T-tubule; NAS:ComplexPortal. 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:0070588; P:calcium ion transmembrane transport; IDA:ComplexPortal. 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:1901843; P:positive regulation of high voltage-gated calcium channel activity; ISS:UniProtKB. DR GO; GO:0045933; P:positive regulation of muscle contraction; NAS:ComplexPortal. 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 CDD; cd12042; SH3_CACNB3; 1. DR FunFam; 3.40.50.300:FF:000023; Voltage-dependent L-type calcium channel subunit beta-2; 1. DR FunFam; 2.30.30.40:FF:000049; Voltage-dependent L-type calcium channel subunit beta-3; 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; 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 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; PR01696; LCACHANNELB3. 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. DR PDBsum; 7MIX; -. DR PDBsum; 7MIY; -. DR PDBsum; 7UHF; -. DR PDBsum; 7UHG; -. DR PDBsum; 8E59; -. DR PDBsum; 8E5A; -. DR PDBsum; 8E5B; -. DR PDBsum; 8EPL; -. DR PDBsum; 8FHS; -. DR PDBsum; 8WE6; -. DR PDBsum; 8WE7; -. DR PDBsum; 8WE8; -. DR PDBsum; 8WE9; -. DR PDBsum; 8X90; -. DR PDBsum; 8X91; -. DR PDBsum; 8X93; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Calcium channel; KW Calcium transport; Cytoplasm; Ion channel; Ion transport; Phosphoprotein; KW Proteomics identification; 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_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 387..399 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 409..420 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 463..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..45 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 47..51 FT /evidence="ECO:0007829|PDB:8WE6" FT TURN 52..57 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:8WE8" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 79..82 FT /evidence="ECO:0007829|PDB:8WE8" FT HELIX 84..87 FT /evidence="ECO:0007829|PDB:8WE7" FT STRAND 91..97 FT /evidence="ECO:0007829|PDB:8WE8" FT STRAND 101..107 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 121..127 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:8X93" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:8WE8" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:8WE6" FT TURN 156..162 FT /evidence="ECO:0007829|PDB:8WE6" FT TURN 164..166 FT /evidence="ECO:0007829|PDB:8WE8" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:8E59" FT HELIX 192..198 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 200..207 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 212..215 FT /evidence="ECO:0007829|PDB:8X93" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:8X93" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:8WE6" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:8WE8" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:8WE8" FT HELIX 247..250 FT /evidence="ECO:0007829|PDB:8WE6" FT TURN 252..256 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 258..263 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 266..269 FT /evidence="ECO:0007829|PDB:8X93" FT TURN 277..281 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 288..291 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 299..305 FT /evidence="ECO:0007829|PDB:8WE6" FT STRAND 306..309 FT /evidence="ECO:0007829|PDB:8WE7" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 316..320 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 323..326 FT /evidence="ECO:0007829|PDB:8WE6" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:8X93" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:8WE8" FT HELIX 342..358 FT /evidence="ECO:0007829|PDB:8WE6" 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 //