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Voltage-dependent L-type calcium channel subunit beta-4 (CAB4) (Calcium channel voltage-dependent subunit beta 4)

 CACB4_MOUSE             Reviewed;         519 AA.
Q8R0S4; Q3UHK2; Q8BRN6; Q8CAJ9;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 146.
RecName: Full=Voltage-dependent L-type calcium channel subunit beta-4 {ECO:0000305};
Short=CAB4 {ECO:0000305};
AltName: Full=Calcium channel voltage-dependent subunit beta 4 {ECO:0000305};
Name=Cacnb4 {ECO:0000312|MGI:MGI:103301}; Synonyms=Cacnlb4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
PubMed=14500989; DOI=10.1385/JMN:21:1:13;
Murakami M., Miyoshi I., Suzuki T., Sasano H., Iijima T.;
"Structures of the murine genes for the beta1- and beta4-Subunits of
the voltage-dependent calcium channel.";
J. Mol. Neurosci. 21:13-22(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Brain cortex, Hypothalamus, and Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-410, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND THR-410, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
INTERACTION WITH CBARP.
PubMed=24751537; DOI=10.1083/jcb.201304101;
Beguin P., Nagashima K., Mahalakshmi R.N., Vigot R., Matsunaga A.,
Miki T., Ng M.Y., Ng Y.J., Lim C.H., Tay H.S., Hwang L.A., Firsov D.,
Tang B.L., Inagaki N., Mori Y., Seino S., Launey T., Hunziker W.;
"BARP suppresses voltage-gated calcium channel activity and Ca2+-
evoked exocytosis.";
J. Cell Biol. 205:233-249(2014).
[7]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-505, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: The beta subunit of voltage-dependent calcium channels
contributes to the function of the calcium channel by increasing
peak calcium current, shifting the voltage dependencies of
activation and inactivation, modulating G protein inhibition and
controlling the alpha-1 subunit membrane targeting.
{ECO:0000250|UniProtKB:O00305}.
-!- SUBUNIT: The L-type calcium channel is composed of four subunits:
alpha-1, alpha-2, beta and gamma. Interacts with FASLG (By
similarity). Interacts with CBARP (PubMed:24751537).
{ECO:0000250|UniProtKB:O00305, ECO:0000269|PubMed:24751537}.
-!- INTERACTION:
Q8IUD2-2:ERC1 (xeno); NbExp=2; IntAct=EBI-3647752, EBI-6920871;
Q91V89:Ppp2r5d; NbExp=2; IntAct=EBI-3647752, EBI-8028449;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=3;
IsoId=Q8R0S4-3; Sequence=Displayed;
Name=1;
IsoId=Q8R0S4-1; Sequence=VSP_022599;
Name=2;
IsoId=Q8R0S4-2; Sequence=VSP_010737;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the calcium channel beta subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB100402; BAC80139.1; -; Genomic_DNA.
EMBL; AK038633; BAC30073.1; -; mRNA.
EMBL; AK043850; BAC31681.1; -; mRNA.
EMBL; AK079616; BAC37703.1; -; mRNA.
EMBL; AK147338; BAE27855.1; -; mRNA.
EMBL; BC026479; AAH26479.1; -; mRNA.
CCDS; CCDS16034.1; -. [Q8R0S4-3]
CCDS; CCDS16035.1; -. [Q8R0S4-1]
CCDS; CCDS71052.1; -. [Q8R0S4-2]
RefSeq; NP_001032176.1; NM_001037099.2. [Q8R0S4-3]
RefSeq; NP_001272356.1; NM_001285427.1. [Q8R0S4-2]
RefSeq; NP_666235.1; NM_146123.3. [Q8R0S4-1]
RefSeq; XP_006497704.1; XM_006497641.3. [Q8R0S4-2]
RefSeq; XP_011237317.1; XM_011239015.1. [Q8R0S4-2]
RefSeq; XP_017170652.1; XM_017315163.1. [Q8R0S4-2]
UniGene; Mm.330223; -.
ProteinModelPortal; Q8R0S4; -.
SMR; Q8R0S4; -.
BioGrid; 198442; 5.
IntAct; Q8R0S4; 11.
MINT; Q8R0S4; -.
STRING; 10090.ENSMUSP00000077438; -.
iPTMnet; Q8R0S4; -.
PhosphoSitePlus; Q8R0S4; -.
MaxQB; Q8R0S4; -.
PaxDb; Q8R0S4; -.
PeptideAtlas; Q8R0S4; -.
PRIDE; Q8R0S4; -.
Ensembl; ENSMUST00000078324; ENSMUSP00000077438; ENSMUSG00000017412. [Q8R0S4-3]
Ensembl; ENSMUST00000102760; ENSMUSP00000099821; ENSMUSG00000017412. [Q8R0S4-1]
Ensembl; ENSMUST00000102761; ENSMUSP00000099822; ENSMUSG00000017412. [Q8R0S4-2]
GeneID; 12298; -.
KEGG; mmu:12298; -.
UCSC; uc008jra.2; mouse. [Q8R0S4-1]
UCSC; uc008jrb.2; mouse. [Q8R0S4-2]
UCSC; uc008jrc.1; mouse. [Q8R0S4-3]
CTD; 785; -.
MGI; MGI:103301; Cacnb4.
eggNOG; KOG3812; Eukaryota.
eggNOG; ENOG410XRDI; LUCA.
GeneTree; ENSGT00390000002740; -.
HOGENOM; HOG000230979; -.
HOVERGEN; HBG050765; -.
InParanoid; Q8R0S4; -.
KO; K04865; -.
PhylomeDB; Q8R0S4; -.
TreeFam; TF316195; -.
Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
Reactome; R-MMU-5576893; Phase 2 - plateau phase.
ChiTaRS; Cacnb4; mouse.
EvolutionaryTrace; Q8R0S4; -.
PRO; PR:Q8R0S4; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000017412; Expressed in 179 organ(s), highest expression level in cerebellum lobe.
ExpressionAtlas; Q8R0S4; baseline and differential.
Genevisible; Q8R0S4; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
GO; GO:0008331; F:high voltage-gated calcium channel activity; TAS:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0046058; P:cAMP metabolic process; IMP:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:MGI.
GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
GO; GO:0048747; P:muscle fiber development; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0050877; P:nervous system process; IMP:MGI.
GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
GO; GO:0048541; P:Peyer's patch development; IMP:MGI.
GO; GO:1904751; P:positive regulation of protein localization to nucleolus; ISO:MGI.
GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; ISO:MGI.
GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISO:MGI.
GO; GO:0048536; P:spleen development; IMP:MGI.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
InterPro; IPR008145; GK/Ca_channel_bsu.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR000584; VDCC_L_bsu.
PANTHER; PTHR11824; PTHR11824; 1.
Pfam; PF00625; Guanylate_kin; 1.
Pfam; PF12052; VGCC_beta4Aa_N; 1.
PRINTS; PR01626; LCACHANNELB.
SMART; SM00072; GuKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calcium channel; Calcium transport;
Complete proteome; Ion channel; Ion transport; Methylation;
Phosphoprotein; Reference proteome; SH3 domain; Transport;
Voltage-gated channel.
CHAIN 1 519 Voltage-dependent L-type calcium channel
subunit beta-4.
/FTId=PRO_0000144061.
DOMAIN 91 160 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000250|UniProtKB:D4A055}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 410 410 Phosphothreonine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000250|UniProtKB:D4A055}.
MOD_RES 505 505 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000250|UniProtKB:D4A055}.
VAR_SEQ 1 48 MSSSYGKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTS
TSFILRQ -> MYDNLYLHGVEDSEA (in isoform
1). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_022599.
VAR_SEQ 1 48 MSSSYGKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTS
TSFILRQ -> MA (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010737.
CONFLICT 492 492 P -> A (in Ref. 2; BAC31681).
{ECO:0000305}.
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


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