CACB4_MOUSE
ID CACB4_MOUSE Reviewed; 519 AA.
AC Q8R0S4; Q3UHK2; Q8BRN6; Q8CAJ9;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit beta-4 {ECO:0000305};
DE Short=CAB4 {ECO:0000305};
DE AltName: Full=Calcium channel voltage-dependent subunit beta 4 {ECO:0000305};
GN Name=Cacnb4 {ECO:0000312|MGI:MGI:103301}; Synonyms=Cacnlb4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX PubMed=14500989; DOI=10.1385/jmn:21:1:13;
RA Murakami M., Miyoshi I., Suzuki T., Sasano H., Iijima T.;
RT "Structures of the murine genes for the beta1- and beta4-Subunits of the
RT voltage-dependent calcium channel.";
RL J. Mol. Neurosci. 21:13-22(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Hypothalamus, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-410, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND THR-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
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).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-505, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: The beta subunit of voltage-dependent calcium channels
CC contributes to the function of the calcium channel by increasing peak
CC calcium current, shifting the voltage dependencies of activation and
CC inactivation, modulating G protein inhibition and controlling the
CC alpha-1 subunit membrane targeting. {ECO:0000250|UniProtKB:O00305}.
CC -!- SUBUNIT: The L-type calcium channel is composed of four subunits:
CC alpha-1, alpha-2, beta and gamma. Interacts with FASLG (By similarity).
CC Interacts with CBARP (PubMed:24751537). {ECO:0000250|UniProtKB:O00305,
CC ECO:0000269|PubMed:24751537}.
CC -!- INTERACTION:
CC Q8R0S4; Q91V89: Ppp2r5d; NbExp=2; IntAct=EBI-3647752, EBI-8028449;
CC Q8R0S4; Q8IUD2-2: ERC1; Xeno; NbExp=2; IntAct=EBI-3647752, EBI-6920871;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q8R0S4-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8R0S4-1; Sequence=VSP_022599;
CC Name=2;
CC IsoId=Q8R0S4-2; Sequence=VSP_010737;
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AB100402; BAC80139.1; -; Genomic_DNA.
DR EMBL; AK038633; BAC30073.1; -; mRNA.
DR EMBL; AK043850; BAC31681.1; -; mRNA.
DR EMBL; AK079616; BAC37703.1; -; mRNA.
DR EMBL; AK147338; BAE27855.1; -; mRNA.
DR EMBL; BC026479; AAH26479.1; -; mRNA.
DR CCDS; CCDS16034.1; -. [Q8R0S4-3]
DR CCDS; CCDS16035.1; -. [Q8R0S4-1]
DR CCDS; CCDS71052.1; -. [Q8R0S4-2]
DR RefSeq; NP_001032176.1; NM_001037099.2. [Q8R0S4-3]
DR RefSeq; NP_001272356.1; NM_001285427.1. [Q8R0S4-2]
DR RefSeq; NP_666235.1; NM_146123.3. [Q8R0S4-1]
DR RefSeq; XP_006497704.1; XM_006497641.3. [Q8R0S4-2]
DR RefSeq; XP_011237317.1; XM_011239015.1. [Q8R0S4-2]
DR RefSeq; XP_017170652.1; XM_017315163.1. [Q8R0S4-2]
DR AlphaFoldDB; Q8R0S4; -.
DR SMR; Q8R0S4; -.
DR BioGRID; 198442; 10.
DR IntAct; Q8R0S4; 11.
DR MINT; Q8R0S4; -.
DR STRING; 10090.ENSMUSP00000077438; -.
DR iPTMnet; Q8R0S4; -.
DR PhosphoSitePlus; Q8R0S4; -.
DR MaxQB; Q8R0S4; -.
DR PaxDb; Q8R0S4; -.
DR PeptideAtlas; Q8R0S4; -.
DR PRIDE; Q8R0S4; -.
DR ProteomicsDB; 265489; -. [Q8R0S4-3]
DR ProteomicsDB; 265490; -. [Q8R0S4-1]
DR ProteomicsDB; 265491; -. [Q8R0S4-2]
DR ABCD; Q8R0S4; 1 sequenced antibody.
DR DNASU; 12298; -.
DR Ensembl; ENSMUST00000078324; ENSMUSP00000077438; ENSMUSG00000017412. [Q8R0S4-3]
DR Ensembl; ENSMUST00000102760; ENSMUSP00000099821; ENSMUSG00000017412. [Q8R0S4-1]
DR Ensembl; ENSMUST00000102761; ENSMUSP00000099822; ENSMUSG00000017412. [Q8R0S4-2]
DR GeneID; 12298; -.
DR KEGG; mmu:12298; -.
DR UCSC; uc008jra.2; mouse. [Q8R0S4-1]
DR UCSC; uc008jrb.2; mouse. [Q8R0S4-2]
DR UCSC; uc008jrc.1; mouse. [Q8R0S4-3]
DR CTD; 785; -.
DR MGI; MGI:103301; Cacnb4.
DR VEuPathDB; HostDB:ENSMUSG00000017412; -.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_0_1_1; -.
DR InParanoid; Q8R0S4; -.
DR PhylomeDB; Q8R0S4; -.
DR TreeFam; TF316195; -.
DR Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
DR BioGRID-ORCS; 12298; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cacnb4; mouse.
DR EvolutionaryTrace; Q8R0S4; -.
DR PRO; PR:Q8R0S4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R0S4; protein.
DR Bgee; ENSMUSG00000017412; Expressed in cerebellum lobe and 165 other tissues.
DR ExpressionAtlas; Q8R0S4; baseline and differential.
DR Genevisible; Q8R0S4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; IDA:SynGO.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0046058; P:cAMP metabolic process; IMP:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:MGI.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
DR GO; GO:0055001; P:muscle cell development; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0050877; P:nervous system process; IMP:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR GO; GO:0048541; P:Peyer's patch development; IMP:MGI.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; ISO:MGI.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
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; IPR000584; VDCC_L_bsu.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR PRINTS; PR01626; LCACHANNELB.
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 Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Ion channel; Ion transport; Methylation; Phosphoprotein;
KW Reference proteome; SH3 domain; Transport; Voltage-gated channel.
FT CHAIN 1..519
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-4"
FT /id="PRO_0000144061"
FT DOMAIN 91..160
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A055"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A055"
FT MOD_RES 505
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A055"
FT VAR_SEQ 1..48
FT /note="MSSSYGKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTSTSFILRQ ->
FT MYDNLYLHGVEDSEA (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022599"
FT VAR_SEQ 1..48
FT /note="MSSSYGKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTSTSFILRQ ->
FT MA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010737"
FT CONFLICT 492
FT /note="P -> A (in Ref. 2; BAC31681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 57950 MW; 663A88C7BCF7E90C CRC64;
MSSSYGKNGA ADGPHSPSSQ VARGTTTRRS RLKRSDGSTT STSFILRQGS ADSYTSRPSD
SDVSLEEDRE AIRQEREQQA AIQLERAKSK PVAFAVKTNV SYCGALDEDV PVPSTAISFD
AKDFLHIKEK YNNDWWIGRL VKEGCEIGFI PSPLRLENIR IQQEQKRGRF HGGKSSGNSS
SSLGEMVSGT FRATPTTTAK QKQKVTEHIP PYDVVPSMRP VVLVGPSLKG YEVTDMMQKA
LFDFLKHRFD GRISITRVTA DISLAKRSVL NNPSKRAIIE RSNTRSSLAE VQSEIERIFE
LARSLQLVVL DADTINHPAQ LIKTSLAPII VHVKVSSPKV LQRLIKSRGK SQSKHLNVQL
VAADKLAQCP PEMFDVILDE NQLEDACEHL GEYLEAYWRA THTSSSTPMT PLLGRNVGST
ALSPYPTAIS GLQSQRMRHS NHSTENSPIE RRSLMTSDEN YHNERARKSR NRLSSSSQHS
RDHYPLVEED YPDSYQDTYK PHRNRGSPGG CSHDSRHRL
