CACB1_HUMAN
ID CACB1_HUMAN Reviewed; 598 AA.
AC Q02641; A8K114; O15331; Q02639; Q02640; Q8N3X9; Q9C085; Q9UD79;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 209.
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 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; 2 AND 3).
RC TISSUE=Hippocampus, and Skeletal muscle;
RX PubMed=1385409; DOI=10.1016/s0021-9258(18)50042-9;
RA Powers P.A., Liu S., Hogan K., Gregg R.G.;
RT "Skeletal muscle and brain isoforms of a beta-subunit of human voltage-
RT dependent calcium channels are encoded by a single gene.";
RL J. Biol. Chem. 267:22967-22972(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=1309651; DOI=10.1016/0896-6273(92)90109-q;
RA Williams M.E., Feldman D.H., McCue A.F., Brenner R., Velicelebi G.,
RA Ellis S.B., Harpold M.M.;
RT "Structure and functional expression of alpha 1, alpha 2, and beta subunits
RT of a novel human neuronal calcium channel subtype.";
RL Neuron 8:71-84(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Heart;
RX PubMed=7916667; DOI=10.1161/01.res.72.6.1337;
RA Collin T., Wang J., Nargeot J., Schwartz A.;
RT "Molecular cloning of three isoforms of the L-type voltage-dependent
RT calcium channel beta subunit from normal human heart.";
RL Circ. Res. 72:1337-1344(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain cortex;
RX PubMed=8905728; DOI=10.1016/0304-3940(96)13055-x;
RA Fukuda K., Kaneko S., Yada N., Kikuwaka M., Akaike A., Satoh M.;
RT "Cyclic AMP-dependent modulation of N- and Q-type Ca2+ channels expressed
RT in Xenopus oocytes.";
RL Neurosci. Lett. 217:13-16(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=10624822; DOI=10.1016/s0304-3940(99)00851-4;
RA Hogan K., Greg R.G., Powers P.A.;
RT "Structure and alternative splicing of the gene encoding the human beta1
RT subunit of voltage dependent calcium channels.";
RL Neurosci. Lett. 277:111-114(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [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=Hippocampus;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-209.
RX PubMed=8395940; DOI=10.1093/hmg/2.7.863;
RA Iles D.E., Segers B., Sengers R.C.A., Monsieurs K., Heytens L.,
RA Halsall P.J., Hopkins P.M., Ellis F.R., Hall-Curran J.L., Stewart A.D.,
RA Wieringa B.;
RT "Genetic mapping of the beta 1- and gamma-subunits of the human skeletal
RT muscle L-type voltage-dependent calcium channel on chromosome 17q and
RT exclusion as candidate genes for malignant hyperthermia susceptibility.";
RL Hum. Mol. Genet. 2:863-868(1993).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 445-598 (ISOFORMS 1 AND 3), FUNCTION,
RP SUBUNIT, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=8107964; DOI=10.1016/0028-3908(93)90004-m;
RA Brust P.F., Simerson S., McCue A.F., Deal C.R., Schoonmaker S.,
RA Williams M.E., Velicelebi G., Johnson E.C., Harpold M.M., Ellis S.B.;
RT "Human neuronal voltage-dependent calcium channels: studies on subunit
RT structure and role in channel assembly.";
RL Neuropharmacology 32:1089-1102(1993).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15615847; DOI=10.1152/ajpheart.00348.2004;
RA Cohen R.M., Foell J.D., Balijepalli R.C., Shah V., Hell J.W., Kamp T.J.;
RT "Unique modulation of L-type Ca2+ channels by short auxiliary beta1d
RT subunit present in cardiac muscle.";
RL Am. J. Physiol. 288:H2363-H2374(2005).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-339.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Regulatory subunit of L-type calcium channels
CC (PubMed:1309651, PubMed:8107964, PubMed:15615847). 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 (PubMed:15615847). Required for functional expression L-type calcium
CC channels that contain CACNA1D as pore-forming subunit (PubMed:1309651).
CC Regulates the activity of L-type calcium channels that contain CACNA1B
CC as pore-forming subunit (PubMed:8107964).
CC {ECO:0000250|UniProtKB:P19517, ECO:0000269|PubMed:1309651,
CC ECO:0000269|PubMed:15615847, ECO:0000269|PubMed:8107964}.
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 (By similarity). Interacts with CACNA1A, CACNA1B, CACNA1C and
CC 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 (PubMed:15615847). 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) (By similarity). Part of a
CC L-type calcium channel complex that contains CACNA1D, CACNA2D1 and
CC CACNB1 (PubMed:1309651). Part of a L-type calcium channel complex that
CC contains CACNA1B, CACNA2D1 and CACNB1 (PubMed:8107964). Interacts with
CC JSRP1. Interacts with RYR1 (By similarity). Interacts with CBARP (By
CC similarity). {ECO:0000250|UniProtKB:P19517,
CC ECO:0000250|UniProtKB:P54283, ECO:0000250|UniProtKB:Q8R3Z5,
CC ECO:0000269|PubMed:1309651, ECO:0000269|PubMed:15615847,
CC ECO:0000269|PubMed:8107964}.
CC -!- INTERACTION:
CC Q02641; P56545-3: CTBP2; NbExp=3; IntAct=EBI-947514, EBI-10171902;
CC Q02641-1; Q13936: CACNA1C; NbExp=2; IntAct=EBI-15707950, EBI-1038838;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000305|PubMed:15615847}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P19517}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P19517}. Cell membrane
CC {ECO:0000305|PubMed:1309651}; Peripheral membrane protein
CC {ECO:0000305|PubMed:1309651}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Beta-1b2, BetaA, Beta-1B, Beta1-2;
CC IsoId=Q02641-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta-1M, BetaC, Beta-1a;
CC IsoId=Q02641-2; Sequence=VSP_000623, VSP_000624, VSP_000625;
CC Name=3; Synonyms=Beta-1b1, BetaB, Beta-1c, Beta1-3;
CC IsoId=Q02641-3; Sequence=VSP_000624, VSP_000625;
CC -!- TISSUE SPECIFICITY: Detected in heart ventricle (at protein level)
CC (PubMed:15615847). Isoform 1 and isoform 3 are expressed in brain,
CC heart, spleen, central nervous system and neuroblastoma cells. Isoform
CC 2 is expressed in skeletal muscle. {ECO:0000269|PubMed:15615847,
CC ECO:0000269|PubMed:8107964}.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA79825.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M92303; AAA35633.1; -; mRNA.
DR EMBL; M92301; AAA35631.1; -; mRNA.
DR EMBL; M92302; AAA35632.1; -; mRNA.
DR EMBL; M76560; AAA51894.1; -; mRNA.
DR EMBL; L06110; AAA36167.1; -; mRNA.
DR EMBL; L06111; AAA36168.1; -; mRNA.
DR EMBL; L06112; AAA36169.1; -; mRNA.
DR EMBL; AB054985; BAB21444.1; -; mRNA.
DR EMBL; U86960; AAB58779.1; -; Genomic_DNA.
DR EMBL; U86952; AAB58779.1; JOINED; Genomic_DNA.
DR EMBL; U86953; AAB58779.1; JOINED; Genomic_DNA.
DR EMBL; U86954; AAB58779.1; JOINED; Genomic_DNA.
DR EMBL; U86955; AAB58779.1; JOINED; Genomic_DNA.
DR EMBL; U86956; AAB58779.1; JOINED; Genomic_DNA.
DR EMBL; U86957; AAB58779.1; JOINED; Genomic_DNA.
DR EMBL; U86958; AAB58779.1; JOINED; Genomic_DNA.
DR EMBL; U86959; AAB58779.1; JOINED; Genomic_DNA.
DR EMBL; U86960; AAB58780.1; -; Genomic_DNA.
DR EMBL; U86952; AAB58780.1; JOINED; Genomic_DNA.
DR EMBL; U86953; AAB58780.1; JOINED; Genomic_DNA.
DR EMBL; U86954; AAB58780.1; JOINED; Genomic_DNA.
DR EMBL; U86955; AAB58780.1; JOINED; Genomic_DNA.
DR EMBL; U86956; AAB58780.1; JOINED; Genomic_DNA.
DR EMBL; U86957; AAB58780.1; JOINED; Genomic_DNA.
DR EMBL; U86958; AAB58780.1; JOINED; Genomic_DNA.
DR EMBL; U86959; AAB58780.1; JOINED; Genomic_DNA.
DR EMBL; U86961; AAB58781.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U86952; AAB58781.1; JOINED; Genomic_DNA.
DR EMBL; U86953; AAB58781.1; JOINED; Genomic_DNA.
DR EMBL; U86954; AAB58781.1; JOINED; Genomic_DNA.
DR EMBL; U86955; AAB58781.1; JOINED; Genomic_DNA.
DR EMBL; U86956; AAB58781.1; JOINED; Genomic_DNA.
DR EMBL; U86957; AAB58781.1; JOINED; Genomic_DNA.
DR EMBL; U86958; AAB58781.1; JOINED; Genomic_DNA.
DR EMBL; U86959; AAB58781.1; JOINED; Genomic_DNA.
DR EMBL; U86960; AAB58781.1; JOINED; Genomic_DNA.
DR EMBL; AK289729; BAF82418.1; -; mRNA.
DR EMBL; CH471152; EAW60562.1; -; Genomic_DNA.
DR EMBL; BC037311; AAH37311.2; -; mRNA.
DR EMBL; Z21725; CAA79824.1; -; Genomic_DNA.
DR EMBL; Z21726; CAA79825.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS11334.1; -. [Q02641-2]
DR CCDS; CCDS42311.1; -. [Q02641-1]
DR CCDS; CCDS45665.1; -. [Q02641-3]
DR PIR; A44461; A44461.
DR PIR; B44461; B44461.
DR PIR; C44461; C44461.
DR PIR; I38002; I38002.
DR PIR; I52859; I52859.
DR PIR; I65766; I65766.
DR PIR; I65767; I65767.
DR PIR; JH0566; JH0566.
DR RefSeq; NP_000714.3; NM_000723.4. [Q02641-1]
DR RefSeq; NP_954855.1; NM_199247.2. [Q02641-2]
DR RefSeq; NP_954856.1; NM_199248.2. [Q02641-3]
DR PDB; 7VFS; EM; 2.80 A; D=1-598.
DR PDB; 7VFU; EM; 3.00 A; D=1-598.
DR PDB; 7VFV; EM; 3.00 A; D=1-598.
DR PDB; 7VFW; EM; 3.30 A; D=1-598.
DR PDBsum; 7VFS; -.
DR PDBsum; 7VFU; -.
DR PDBsum; 7VFV; -.
DR PDBsum; 7VFW; -.
DR AlphaFoldDB; Q02641; -.
DR SMR; Q02641; -.
DR BioGRID; 107236; 14.
DR ComplexPortal; CPX-3192; Skeletal muscle VGCC complex.
DR CORUM; Q02641; -.
DR IntAct; Q02641; 10.
DR MINT; Q02641; -.
DR STRING; 9606.ENSP00000377840; -.
DR BindingDB; Q02641; -.
DR ChEMBL; CHEMBL3988638; -.
DR ChEMBL; CHEMBL3988640; -.
DR ChEMBL; CHEMBL4106160; -.
DR DrugBank; DB01118; Amiodarone.
DR DrugBank; DB00381; Amlodipine.
DR DrugBank; DB09230; Azelnidipine.
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; DB00898; Ethanol.
DR DrugBank; DB13961; Fish oil.
DR DrugBank; DB00308; Ibutilide.
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 GlyGen; Q02641; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q02641; -.
DR PhosphoSitePlus; Q02641; -.
DR BioMuta; CACNB1; -.
DR DMDM; 20455481; -.
DR jPOST; Q02641; -.
DR MassIVE; Q02641; -.
DR MaxQB; Q02641; -.
DR PaxDb; Q02641; -.
DR PeptideAtlas; Q02641; -.
DR PRIDE; Q02641; -.
DR ProteomicsDB; 58113; -. [Q02641-1]
DR ProteomicsDB; 58114; -. [Q02641-2]
DR ProteomicsDB; 58115; -. [Q02641-3]
DR ABCD; Q02641; 1 sequenced antibody.
DR Antibodypedia; 4063; 403 antibodies from 35 providers.
DR DNASU; 782; -.
DR Ensembl; ENST00000344140.5; ENSP00000345461.5; ENSG00000067191.16. [Q02641-2]
DR Ensembl; ENST00000394303.8; ENSP00000377840.3; ENSG00000067191.16. [Q02641-1]
DR Ensembl; ENST00000394310.7; ENSP00000377847.3; ENSG00000067191.16. [Q02641-3]
DR GeneID; 782; -.
DR KEGG; hsa:782; -.
DR MANE-Select; ENST00000394303.8; ENSP00000377840.3; NM_000723.5; NP_000714.3.
DR UCSC; uc002hrm.2; human. [Q02641-1]
DR CTD; 782; -.
DR DisGeNET; 782; -.
DR GeneCards; CACNB1; -.
DR HGNC; HGNC:1401; CACNB1.
DR HPA; ENSG00000067191; Group enriched (skeletal muscle, tongue).
DR MIM; 114207; gene.
DR neXtProt; NX_Q02641; -.
DR OpenTargets; ENSG00000067191; -.
DR PharmGKB; PA87; -.
DR VEuPathDB; HostDB:ENSG00000067191; -.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_3_0_1; -.
DR InParanoid; Q02641; -.
DR OMA; FFRKAEH; -.
DR OrthoDB; 926074at2759; -.
DR PhylomeDB; Q02641; -.
DR TreeFam; TF316195; -.
DR PathwayCommons; Q02641; -.
DR Reactome; R-HSA-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-HSA-5576893; Phase 2 - plateau phase.
DR SignaLink; Q02641; -.
DR SIGNOR; Q02641; -.
DR BioGRID-ORCS; 782; 17 hits in 1075 CRISPR screens.
DR ChiTaRS; CACNB1; human.
DR GeneWiki; CACNB1; -.
DR GenomeRNAi; 782; -.
DR Pharos; Q02641; Tbio.
DR PRO; PR:Q02641; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q02641; protein.
DR Bgee; ENSG00000067191; Expressed in gastrocnemius and 149 other tissues.
DR ExpressionAtlas; Q02641; baseline and differential.
DR Genevisible; Q02641; HS.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IGI:ARUK-UCL.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IC:ComplexPortal.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-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:0045933; P:positive regulation of muscle contraction; IC:ComplexPortal.
DR GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IGI:ARUK-UCL.
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 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain; Transport;
KW Voltage-gated channel.
FT CHAIN 1..598
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-1"
FT /id="PRO_0000144046"
FT DOMAIN 100..169
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..76
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..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..589
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 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 210..216
FT /note="AKQKQKS -> GNEMTNLAFELDPLELEEEEAELGEQSGSAKTSVSSVTTPP
FT PHGKRIPFFKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1385409,
FT ECO:0000303|PubMed:7916667"
FT /id="VSP_000623"
FT VAR_SEQ 445..478
FT /note="GPYLASGDQPLERATGEHASMHEYPGELGQPPGL -> VQVLTSLRRNLGFW
FT GGLESSQRGSVVPQEQEHAM (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:1309651,
FT ECO:0000303|PubMed:1385409, ECO:0000303|PubMed:7916667,
FT ECO:0000303|PubMed:8107964"
FT /id="VSP_000624"
FT VAR_SEQ 479..598
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:1309651,
FT ECO:0000303|PubMed:1385409, ECO:0000303|PubMed:7916667,
FT ECO:0000303|PubMed:8107964"
FT /id="VSP_000625"
FT VARIANT 339
FT /note="P -> L (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1266205915)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036349"
FT CONFLICT 5..6
FT /note="TS -> SG (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="E -> G (in Ref. 2; AAA51894)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="Missing (in Ref. 3; AAA36168/AAA36169)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="G -> R (in Ref. 3; AAA36167/AAA36168/AAA36169)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="H -> D (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..176
FT /note="KL -> TV (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="G -> S (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="T -> S (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="I -> T (in Ref. 8; AAH37311)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..296
FT /note="SNTR -> LQHT (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="I -> L (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="P -> H (in Ref. 8; AAH37311)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="M -> I (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 434..435
FT /note="AA -> RR (in Ref. 1; AAA35631/AAA35632/AAA35633 and
FT 5; AAB58779/AAB58780/AAB58781)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="E -> D (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="M -> V (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="S -> N (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="R -> W (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="L -> P (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="L -> P (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 539..541
FT /note="GTP -> A (in Ref. 1; AAA35633 and 5; AAB58781)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="Missing (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="L -> M (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 573..574
FT /note="CA -> WP (in Ref. 1; AAA35633 and 5; AAB58781)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="R -> Q (in Ref. 3; AAA36167)"
FT /evidence="ECO:0000305"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 243..259
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 349..358
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 394..411
FT /evidence="ECO:0007829|PDB:7VFS"
SQ SEQUENCE 598 AA; 65714 MW; 44FE4E3BA6F016FD CRC64;
MVQKTSMSRG PYPPSQEIPM EVFDPSPQGK YSKRKGRFKR SDGSTSSDTT SNSFVRQGSA
ESYTSRPSDS DVSLEEDREA LRKEAERQAL AQLEKAKTKP VAFAVRTNVG YNPSPGDEVP
VQGVAITFEP KDFLHIKEKY NNDWWIGRLV KEGCEVGFIP SPVKLDSLRL LQEQKLRQNR
LGSSKSGDNS 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 GDQPLERATG EHASMHEYPG ELGQPPGLYP
SSHPPGRAGT LRALSRQDTF DADTPGSRNS AYTELGDSCV DMETDPSEGP GLGDPAGGGT
PPARQGSWED EEEDYEEELT DNRNRGRNKA RYCAEGGGPV LGRNKNELEG WGRGVYIR
