CBARP_MOUSE
ID CBARP_MOUSE Reviewed; 698 AA.
AC Q66L44; E9QP85; Q497H6; Q8CBL1; Q9QZY3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 4.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Voltage-dependent calcium channel beta subunit-associated regulatory protein {ECO:0000305};
DE AltName: Full=Downstream of Stk11 protein {ECO:0000303|PubMed:24751537};
GN Name=Cbarp {ECO:0000312|MGI:MGI:1354170};
GN Synonyms=Barp {ECO:0000303|PubMed:24751537},
GN Dos {ECO:0000303|PubMed:24751537}, R29144/1 {ECO:0000303|PubMed:10400995};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-698.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 250-698.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 683-698.
RC STRAIN=129;
RX PubMed=10400995; DOI=10.1093/hmg/8.8.1479;
RA Smith D.P., Spicer J., Smith A., Swift S., Ashworth A.;
RT "The mouse Peutz-Jeghers syndrome gene Lkb1 encodes a nuclear protein
RT kinase.";
RL Hum. Mol. Genet. 8:1479-1485(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-295; SER-501;
RP SER-520; SER-524 AND SER-610, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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 [7]
RP FUNCTION, INTERACTION WITH CACNB1; CACNB2; CACNB3 AND CACNB4, SUBCELLULAR
RP LOCATION, TOPOLOGY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION
RP AT ASN-25, AND MUTAGENESIS OF ASN-25; 426-LEU-TRP-427 AND 545-LEU--LEU-550.
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).
CC -!- FUNCTION: Negatively regulates voltage-gated calcium channels by
CC preventing the interaction between their alpha and beta subunits.
CC Thereby, negatively regulates calcium channels activity at the plasma
CC membrane and indirectly inhibits calcium-regulated exocytosis.
CC {ECO:0000269|PubMed:24751537}.
CC -!- SUBUNIT: Interacts with voltage-dependent calcium channels CACNB1,
CC CACNB2, CACNB3 and CACNB4 beta subunits; prevents their interaction
CC with the CACNA1C alpha subunit thereby negatively regulating the
CC activity of the corresponding calcium channels.
CC {ECO:0000269|PubMed:24751537}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:24751537}; Single-pass type III
CC membrane protein {ECO:0000305|PubMed:24751537}. Cell membrane
CC {ECO:0000269|PubMed:24751537}; Single-pass type III membrane protein
CC {ECO:0000305|PubMed:24751537}. Cell projection, growth cone
CC {ECO:0000269|PubMed:24751537}.
CC -!- TISSUE SPECIFICITY: Expressed by neurons in the cortex, cerebellum and
CC hippocampus and by pancreatic beta cells (at protein level).
CC {ECO:0000269|PubMed:24751537}.
CC -!- DEVELOPMENTAL STAGE: Detected in brain from 14 dpc until adulthood with
CC higher expression between 18 dpc and P7 (at protein level).
CC {ECO:0000269|PubMed:24751537}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00553.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AC159999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC078442; AAH78442.1; -; mRNA.
DR EMBL; BC100552; AAI00553.1; ALT_SEQ; mRNA.
DR EMBL; AK035824; BAC29200.1; -; mRNA.
DR EMBL; AF145697; AAD55370.1; -; Genomic_DNA.
DR CCDS; CCDS56734.1; -.
DR RefSeq; NP_001182197.1; NM_001195268.1.
DR RefSeq; XP_006513028.2; XM_006512965.3.
DR RefSeq; XP_006513032.1; XM_006512969.2.
DR RefSeq; XP_006513037.1; XM_006512974.2.
DR RefSeq; XP_006513039.1; XM_006512976.2.
DR RefSeq; XP_006513040.1; XM_006512977.2.
DR RefSeq; XP_006513041.1; XM_006512978.2.
DR AlphaFoldDB; Q66L44; -.
DR SMR; Q66L44; -.
DR STRING; 10090.ENSMUSP00000132978; -.
DR GlyGen; Q66L44; 1 site.
DR iPTMnet; Q66L44; -.
DR PhosphoSitePlus; Q66L44; -.
DR jPOST; Q66L44; -.
DR MaxQB; Q66L44; -.
DR PaxDb; Q66L44; -.
DR PRIDE; Q66L44; -.
DR ProteomicsDB; 265559; -.
DR Antibodypedia; 2282; 67 antibodies from 18 providers.
DR Ensembl; ENSMUST00000105369; ENSMUSP00000101008; ENSMUSG00000035640.
DR Ensembl; ENSMUST00000170219; ENSMUSP00000131487; ENSMUSG00000035640.
DR GeneID; 100503659; -.
DR KEGG; mmu:100503659; -.
DR UCSC; uc007gbw.1; mouse.
DR UCSC; uc011xim.1; mouse.
DR CTD; 255057; -.
DR MGI; MGI:1354170; Cbarp.
DR VEuPathDB; HostDB:ENSMUSG00000035640; -.
DR eggNOG; ENOG502QQ2E; Eukaryota.
DR GeneTree; ENSGT00390000009230; -.
DR InParanoid; Q66L44; -.
DR OMA; HNQETER; -.
DR OrthoDB; 830111at2759; -.
DR BioGRID-ORCS; 100503659; 1 hit in 38 CRISPR screens.
DR ChiTaRS; Cbarp; mouse.
DR PRO; PR:Q66L44; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q66L44; protein.
DR Bgee; ENSMUSG00000035640; Expressed in suprachiasmatic nucleus and 225 other tissues.
DR ExpressionAtlas; Q66L44; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044325; F:transmembrane transporter binding; IDA:UniProtKB.
DR GO; GO:1903170; P:negative regulation of calcium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:UniProtKB.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IMP:UniProtKB.
DR InterPro; IPR037658; CBARP.
DR PANTHER; PTHR28597; PTHR28597; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..698
FT /note="Voltage-dependent calcium channel beta subunit-
FT associated regulatory protein"
FT /id="PRO_0000079984"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24751537"
FT TRANSMEM 42..62
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24751537"
FT REGION 90..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 691
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N350"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N350"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N350"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24751537"
FT MUTAGEN 25
FT /note="N->Q: Loss of N-glycosylation."
FT /evidence="ECO:0000269|PubMed:24751537"
FT MUTAGEN 426..427
FT /note="LW->AA: Loss of interaction with CACNB3 and loss of
FT the ability to negatively regulate voltage-dependent L-type
FT calcium channel; when associated with 545-A--A-550."
FT /evidence="ECO:0000269|PubMed:24751537"
FT MUTAGEN 545..550
FT /note="LFHEFL->AAHEAA: Loss of interaction with CACNB3 and
FT loss of the ability to negatively regulate voltage-
FT dependent L-type calcium channel; when associated with 426-
FT A-A-427."
FT /evidence="ECO:0000269|PubMed:24751537"
FT CONFLICT 555
FT /note="H -> Y (in Ref. 3; BAC29200)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="E -> K (in Ref. 3; BAC29200)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="G -> A (in Ref. 3; BAC29200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 74131 MW; 6CD6F7DA660590F0 CRC64;
MQPTATMATA AATTATVALT TSWDNATSRP TAEPDPILDN YVLLVVVMSL FVGGTLVVLS
GVLLLCKRCW EVHQRFNRAM EEAEKTTTTY LDNGTHPIQD PDCRGEDPEG QDTETERFLA
TSSTGRRVSF NEAALFEQSR KAQDKGRRYT LTEGDFHHLK NARLTHLHLP PLKIATIHEC
DSGEASAAAT PHPATTSKDS LAIFQPPGKT LTGHSVGPSS ALPGGPYNSV DFSEISPSTS
SDSGEGISLD AGTRGAKAAG PETVPGEMGT GSSGSGTVLQ FFTRLRRHAS LDGASPYFKV
KKWKLEPSQR ASSLDTRGSP KRHHFQRQRA ASESMEQEGD VPHADFIQYI ASAGDSVAFP
PPRPFLASPT SPPPTLGRLE AAEAAGGASP ETPPEHGISL GPEHAQQQDP QQEQDAEHAQ
CSYRDLWSLR ASLELHAATA SDHSSSGNDR DSVRSGDSSG SGSGGGGAAP AFPPPPESPP
ALRPKDGEAR RLLQMDSGYA SIEGRGAGDE VSELPAPARS PPRSPRAWPR RPRRDYSIDE
KTDALFHEFL RHDPHFDDAP RHRTRAHPHT HARKQWQQRG RQHSDPGGAR AATPPGVARP
TRAPLRRGDS VDCPPEGRAL PITGDDPSIP VIEEEPGGGG GGCPGSGLCV EPAGALLDKL
AASLDERLFS PRLAEPVASS QVLIVAAAAP TSPDHSPA
