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

 CACB4_RAT               Reviewed;         519 AA.
D4A055;
30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
30-NOV-2016, sequence version 2.
05-DEC-2018, entry version 84.
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|RGD:68385};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-447 AND SER-507,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[4]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 49-407.
PubMed=15170217; DOI=10.1038/nature02641;
Chen Y.H., Li M.H., Zhang Y., He L.L., Yamada Y., Fitzmaurice A.,
Shen Y., Zhang H., Tong L., Yang J.;
"Structural basis of the alpha1-beta subunit interaction of voltage-
gated Ca2+ channels.";
Nature 429:675-680(2004).
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:O00305, ECO:0000250|UniProtKB:Q8R0S4}.
-!- INTERACTION:
Q91V89:Ppp2r5d (xeno); NbExp=4; IntAct=EBI-8028403, EBI-8028449;
P63058:Thra (xeno); NbExp=2; IntAct=EBI-8028403, EBI-6935292;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=D4A055-2; Sequence=Displayed;
Name=2;
IsoId=D4A055-1; Sequence=VSP_058665;
-!- SIMILARITY: Belongs to the calcium channel beta subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AABR07052125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07052126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473983; EDM00433.1; -; Genomic_DNA.
RefSeq; NP_001099203.1; NM_001105733.1. [D4A055-1]
RefSeq; XP_017447488.1; XM_017591999.1. [D4A055-2]
UniGene; Rn.9863; -.
PDB; 1VYV; X-ray; 3.00 A; A/B=49-407.
PDBsum; 1VYV; -.
ProteinModelPortal; D4A055; -.
SMR; D4A055; -.
IntAct; D4A055; 4.
MINT; D4A055; -.
STRING; 10116.ENSRNOP00000056186; -.
iPTMnet; D4A055; -.
PhosphoSitePlus; D4A055; -.
PaxDb; D4A055; -.
PRIDE; D4A055; -.
Ensembl; ENSRNOT00000059430; ENSRNOP00000056186; ENSRNOG00000007666. [D4A055-1]
GeneID; 58942; -.
KEGG; rno:58942; -.
CTD; 785; -.
RGD; 68385; Cacnb4.
eggNOG; KOG3812; Eukaryota.
eggNOG; ENOG410XRDI; LUCA.
GeneTree; ENSGT00940000153663; -.
InParanoid; D4A055; -.
KO; K04865; -.
OMA; SYQDSYK; -.
OrthoDB; EOG091G09C1; -.
PhylomeDB; D4A055; -.
TreeFam; TF316195; -.
Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
Reactome; R-RNO-5576893; Phase 2 - plateau phase.
PRO; PR:D4A055; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000007666; Expressed in 9 organ(s), highest expression level in brain.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IDA:RGD.
GO; GO:0005730; C:nucleolus; IDA:RGD.
GO; GO:0098793; C:presynapse; IDA:SynGO.
GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IDA:RGD.
GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:RGD.
GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; IEA:Ensembl.
GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
GO; GO:0006816; P:calcium ion transport; IMP:RGD.
GO; GO:0046058; P:cAMP metabolic process; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
GO; GO:0014051; P:gamma-aminobutyric acid secretion; IEA:Ensembl.
GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
GO; GO:0048747; P:muscle fiber development; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:RGD.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:RGD.
GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
GO; GO:0019227; P:neuronal action potential propagation; IEA:Ensembl.
GO; GO:0048541; P:Peyer's patch development; IEA:Ensembl.
GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IDA:RGD.
GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IDA:RGD.
GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
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;
3D-structure; Alternative splicing; Complete proteome; Methylation;
Phosphoprotein; Reference proteome; SH3 domain.
CHAIN 1 519 Voltage-dependent L-type calcium channel
subunit beta-4.
/FTId=PRO_0000438478.
DOMAIN 91 160 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R0S4}.
MOD_RES 410 410 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8R0S4}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 505 505 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8R0S4}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 2 48 SSSYAKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTST
SFILRQ -> YDNLYLHGVEDSEA (in isoform 2).
/FTId=VSP_058665.
HELIX 72 88 {ECO:0000244|PDB:1VYV}.
STRAND 94 100 {ECO:0000244|PDB:1VYV}.
STRAND 124 132 {ECO:0000244|PDB:1VYV}.
STRAND 135 142 {ECO:0000244|PDB:1VYV}.
STRAND 148 151 {ECO:0000244|PDB:1VYV}.
HELIX 153 161 {ECO:0000244|PDB:1VYV}.
TURN 162 164 {ECO:0000244|PDB:1VYV}.
STRAND 211 215 {ECO:0000244|PDB:1VYV}.
STRAND 221 224 {ECO:0000244|PDB:1VYV}.
HELIX 232 248 {ECO:0000244|PDB:1VYV}.
TURN 249 251 {ECO:0000244|PDB:1VYV}.
STRAND 252 258 {ECO:0000244|PDB:1VYV}.
HELIX 262 264 {ECO:0000244|PDB:1VYV}.
HELIX 288 302 {ECO:0000244|PDB:1VYV}.
STRAND 307 312 {ECO:0000244|PDB:1VYV}.
HELIX 318 321 {ECO:0000244|PDB:1VYV}.
STRAND 329 333 {ECO:0000244|PDB:1VYV}.
HELIX 338 346 {ECO:0000244|PDB:1VYV}.
HELIX 350 353 {ECO:0000244|PDB:1VYV}.
HELIX 356 367 {ECO:0000244|PDB:1VYV}.
HELIX 371 373 {ECO:0000244|PDB:1VYV}.
STRAND 375 378 {ECO:0000244|PDB:1VYV}.
STRAND 380 382 {ECO:0000244|PDB:1VYV}.
HELIX 383 401 {ECO:0000244|PDB:1VYV}.
SEQUENCE 519 AA; 57964 MW; 663B2CFE1CF7E90C CRC64;
MSSSYAKNGA 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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