CACB4_RAT
ID CACB4_RAT Reviewed; 519 AA.
AC D4A055;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 103.
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|RGD:68385};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-447 AND SER-507, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 49-407.
RX PubMed=15170217; DOI=10.1038/nature02641;
RA Chen Y.H., Li M.H., Zhang Y., He L.L., Yamada Y., Fitzmaurice A., Shen Y.,
RA Zhang H., Tong L., Yang J.;
RT "Structural basis of the alpha1-beta subunit interaction of voltage-gated
RT Ca2+ channels.";
RL Nature 429:675-680(2004).
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 (By similarity). {ECO:0000250|UniProtKB:O00305,
CC ECO:0000250|UniProtKB:Q8R0S4}.
CC -!- INTERACTION:
CC D4A055; Q91V89: Ppp2r5d; Xeno; NbExp=4; IntAct=EBI-8028403, EBI-8028449;
CC D4A055; P63058: Thra; Xeno; NbExp=2; IntAct=EBI-8028403, EBI-6935292;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=D4A055-2; Sequence=Displayed;
CC Name=2;
CC IsoId=D4A055-1; Sequence=VSP_058665;
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AABR07052125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07052126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473983; EDM00433.1; -; Genomic_DNA.
DR RefSeq; NP_001099203.1; NM_001105733.1. [D4A055-1]
DR RefSeq; XP_017447488.1; XM_017591999.1. [D4A055-2]
DR PDB; 1VYV; X-ray; 3.00 A; A/B=49-407.
DR PDB; 6HW2; X-ray; 1.94 A; A=56-232.
DR PDBsum; 1VYV; -.
DR PDBsum; 6HW2; -.
DR AlphaFoldDB; D4A055; -.
DR SMR; D4A055; -.
DR IntAct; D4A055; 4.
DR MINT; D4A055; -.
DR STRING; 10116.ENSRNOP00000056186; -.
DR iPTMnet; D4A055; -.
DR PhosphoSitePlus; D4A055; -.
DR PaxDb; D4A055; -.
DR PRIDE; D4A055; -.
DR ABCD; D4A055; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000107851; ENSRNOP00000097125; ENSRNOG00000007666. [D4A055-2]
DR GeneID; 58942; -.
DR KEGG; rno:58942; -.
DR CTD; 785; -.
DR RGD; 68385; Cacnb4.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_0_1_1; -.
DR InParanoid; D4A055; -.
DR OMA; DYRADRP; -.
DR OrthoDB; 926074at2759; -.
DR PhylomeDB; D4A055; -.
DR TreeFam; TF316195; -.
DR Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
DR PRO; PR:D4A055; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000007666; Expressed in frontal cortex and 9 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:RGD.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IDA:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:RGD.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; ISO:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; IMP:RGD.
DR GO; GO:0046058; P:cAMP metabolic process; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISO:RGD.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; ISO:RGD.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:RGD.
DR GO; GO:0055001; P:muscle cell development; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:RGD.
DR GO; GO:0050877; P:nervous system process; ISO:RGD.
DR GO; GO:0007528; P:neuromuscular junction development; ISO:RGD.
DR GO; GO:0019227; P:neuronal action potential propagation; ISO:RGD.
DR GO; GO:0048541; P:Peyer's patch development; ISO:RGD.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IDA:RGD.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISO:RGD.
DR GO; GO:0048536; P:spleen development; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
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 3D-structure; Alternative splicing; Methylation; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..519
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-4"
FT /id="PRO_0000438478"
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:0007744|PubMed:22673903"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S4"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S4"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 505
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S4"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 2..48
FT /note="SSSYAKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTSTSFILRQ -> Y
FT DNLYLHGVEDSEA (in isoform 2)"
FT /id="VSP_058665"
FT HELIX 64..87
FT /evidence="ECO:0007829|PDB:6HW2"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:6HW2"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6HW2"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:6HW2"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:6HW2"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6HW2"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:6HW2"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:6HW2"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:6HW2"
FT HELIX 232..248
FT /evidence="ECO:0007829|PDB:1VYV"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1VYV"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:1VYV"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1VYV"
FT HELIX 288..302
FT /evidence="ECO:0007829|PDB:1VYV"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:1VYV"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:1VYV"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:1VYV"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:1VYV"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:1VYV"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:1VYV"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:1VYV"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:1VYV"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:1VYV"
FT HELIX 383..401
FT /evidence="ECO:0007829|PDB:1VYV"
SQ 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
