ID RCAN1_MOUSE Reviewed; 251 AA. AC Q9JHG6; Q7TNY3; Q91WQ4; Q9JK50; Q9JK51; Q9JKK2; Q9JKK3; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 23-MAY-2018, sequence version 2. DT 27-MAR-2024, entry version 171. DE RecName: Full=Calcipressin-1; DE AltName: Full=Down syndrome critical region protein 1 homolog; DE AltName: Full=Myocyte-enriched calcineurin-interacting protein 1; DE Short=MCIP1; DE AltName: Full=Regulator of calcineurin 1; GN Name=Rcan1; Synonyms=Dscr1; 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 [MRNA] (ISOFORMS B AND E). RX PubMed=10722714; DOI=10.1074/jbc.275.12.8719; RA Rothermel B., Vega R.B., Yang J., Wu H., Bassel-Duby R., Williams R.S.; RT "A protein encoded within the Down syndrome critical region is enriched in RT striated muscles and inhibits calcineurin signaling."; RL J. Biol. Chem. 275:8719-8725(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=11231093; DOI=10.1016/s0925-4773(00)00583-9; RA Casas C., Martinez S., Pritchard M.A., Fuentes J.J., Nadal M., Guimera J., RA Arbones M., Florez J., Soriano E., Estivill X., Alcantara S.; RT "Dscr1, a novel endogenous inhibitor of calcineurin signaling, is expressed RT in the primitive ventricle of the heart and during neurogenesis."; RL Mech. Dev. 101:289-292(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), INTERACTION WITH PPP3CA, RP PHOSPHORYLATION, AND TISSUE SPECIFICITY. RC STRAIN=NIH Swiss; TISSUE=Heart; RX PubMed=12809556; DOI=10.1042/bj20030267; RA Genesca L., Aubareda A., Fuentes J.J., Estivill X., De La Luna S., RA Perez-Riba M.; RT "Phosphorylation of calcipressin 1 increases its ability to inhibit RT calcineurin and decreases calcipressin half-life."; RL Biochem. J. 374:567-575(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C). RA Fuentes J.J., Pritchard M.A., Pucharcos C., Estivill X.; RT "Down syndrome candidate region 1 (Dscr1), one of three alternatively RT spliced exon 1 transcripts."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C). RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; TISSUE=Heart; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC TISSUE=Kidney; 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-251 (ISOFORM A). RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=11080588; DOI=10.1016/s0378-1119(00)00407-8; RA Strippoli P., Petrini M., Lenzi L., Carinci P., Zannotti M.; RT "The murine DSCR1-like (Down syndrome candidate region 1) gene family: RT conserved synteny with the human orthologous genes."; RL Gene 257:223-232(2000). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY RP 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 [10] RP STRUCTURE BY NMR OF 67-156. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of RRM domain in calcipressin 1."; RL Submitted (MAY-2004) to the PDB data bank. CC -!- FUNCTION: Inhibits calcineurin-dependent transcriptional responses by CC binding to the catalytic domain of calcineurin A. Could play a role CC during central nervous system development (PubMed:11231093). CC {ECO:0000269|PubMed:11231093}. CC -!- SUBUNIT: Interacts with RAF1 and PPP3R1 (By similarity). Interacts with CC PPP3CA (PubMed:12809556). {ECO:0000250|UniProtKB:P53805, CC ECO:0000269|PubMed:12809556}. CC -!- INTERACTION: CC Q9JHG6; Q61214: Dyrk1a; NbExp=2; IntAct=EBI-644061, EBI-80344; CC Q9JHG6; P35922: Fmr1; NbExp=3; IntAct=EBI-644061, EBI-645094; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist.; CC Name=A; Synonyms=1, CALP1-L {ECO:0000303|PubMed:12809556}; CC IsoId=Q9JHG6-1; Sequence=Displayed; CC Name=B; Synonyms=4; CC IsoId=Q9JHG6-2; Sequence=VSP_001317; CC Name=C; CC IsoId=Q9JHG6-3; Sequence=VSP_001318; CC Name=E; Synonyms=CALP1-S {ECO:0000303|PubMed:12809556}; CC IsoId=Q9JHG6-4; Sequence=VSP_059568; CC -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle. Also CC expressed in all other tissues. {ECO:0000269|PubMed:11231093, CC ECO:0000269|PubMed:12809556}. CC -!- PTM: Phosphorylation increases its ability to inhibit calcineurin and CC decreases protein half-life. {ECO:0000250|UniProtKB:P53805}. CC -!- SIMILARITY: Belongs to the RCAN family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF91461.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF237789; AAF63485.1; -; mRNA. DR EMBL; AF237790; AAF63486.1; -; mRNA. DR EMBL; AF260717; AAF70343.1; -; mRNA. DR EMBL; AY325904; AAP96744.1; -; mRNA. DR EMBL; AF263239; AAF72701.1; -; mRNA. DR EMBL; AF263240; AAF72702.1; -; mRNA. DR EMBL; AK010696; BAB27128.1; -; mRNA. DR EMBL; AK146764; BAE27416.1; -; mRNA. DR EMBL; AC162305; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC174448; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013551; AAH13551.1; -; mRNA. DR EMBL; AF282255; AAF91461.1; ALT_INIT; mRNA. DR CCDS; CCDS28337.1; -. [Q9JHG6-2] DR CCDS; CCDS37405.1; -. [Q9JHG6-1] DR RefSeq; NP_001075018.1; NM_001081549.2. [Q9JHG6-1] DR RefSeq; NP_062339.2; NM_019466.4. [Q9JHG6-2] DR PDB; 1WEY; NMR; -; A=67-156. DR PDBsum; 1WEY; -. DR AlphaFoldDB; Q9JHG6; -. DR SMR; Q9JHG6; -. DR BioGRID; 207725; 2. DR IntAct; Q9JHG6; 4. DR MINT; Q9JHG6; -. DR STRING; 10090.ENSMUSP00000060394; -. DR iPTMnet; Q9JHG6; -. DR PhosphoSitePlus; Q9JHG6; -. DR jPOST; Q9JHG6; -. DR MaxQB; Q9JHG6; -. DR PaxDb; 10090-ENSMUSP00000060394; -. DR ProteomicsDB; 255166; -. [Q9JHG6-1] DR ProteomicsDB; 255167; -. [Q9JHG6-2] DR ProteomicsDB; 255168; -. [Q9JHG6-3] DR ProteomicsDB; 329214; -. DR Pumba; Q9JHG6; -. DR Antibodypedia; 22959; 631 antibodies from 35 providers. DR DNASU; 54720; -. DR Ensembl; ENSMUST00000023672.10; ENSMUSP00000023672.8; ENSMUSG00000022951.19. [Q9JHG6-2] DR Ensembl; ENSMUST00000060005.15; ENSMUSP00000060394.9; ENSMUSG00000022951.19. [Q9JHG6-1] DR Ensembl; ENSMUST00000231410.2; ENSMUSP00000156110.2; ENSMUSG00000022951.19. [Q9JHG6-3] DR Ensembl; ENSMUST00000232197.2; ENSMUSP00000155863.2; ENSMUSG00000022951.19. [Q9JHG6-3] DR Ensembl; ENSMUST00000232239.2; ENSMUSP00000156053.2; ENSMUSG00000022951.19. [Q9JHG6-4] DR GeneID; 54720; -. DR KEGG; mmu:54720; -. DR UCSC; uc007zze.2; mouse. DR AGR; MGI:1890564; -. DR CTD; 1827; -. DR MGI; MGI:1890564; Rcan1. DR VEuPathDB; HostDB:ENSMUSG00000022951; -. DR eggNOG; KOG4019; Eukaryota. DR GeneTree; ENSGT00940000159870; -. DR HOGENOM; CLU_076190_2_0_1; -. DR InParanoid; Q9JHG6; -. DR OMA; CINCYFA; -. DR OrthoDB; 2727072at2759; -. DR PhylomeDB; Q9JHG6; -. DR TreeFam; TF313579; -. DR BioGRID-ORCS; 54720; 2 hits in 78 CRISPR screens. DR ChiTaRS; Rcan1; mouse. DR EvolutionaryTrace; Q9JHG6; -. DR PRO; PR:Q9JHG6; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q9JHG6; Protein. DR Bgee; ENSMUSG00000022951; Expressed in epithelium of lens and 291 other cell types or tissues. DR ExpressionAtlas; Q9JHG6; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IMP:MGI. DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central. DR GO; GO:0031987; P:locomotion involved in locomotory behavior; IGI:MGI. DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB. DR GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; ISO:MGI. DR GO; GO:0043627; P:response to estrogen; ISO:MGI. DR GO; GO:0002931; P:response to ischemia; IMP:MGI. DR GO; GO:0006979; P:response to oxidative stress; IGI:MGI. DR GO; GO:0007614; P:short-term memory; IGI:MGI. DR GO; GO:0048741; P:skeletal muscle fiber development; IDA:MGI. DR CDD; cd12708; RRM_RCAN1; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR006931; Calcipressin. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR034906; RCAN1_RRM. DR PANTHER; PTHR10300; CALCIPRESSIN; 1. DR PANTHER; PTHR10300:SF4; CALCIPRESSIN-1; 1. DR Pfam; PF04847; Calcipressin; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR Genevisible; Q9JHG6; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Phosphoprotein; Reference proteome. FT CHAIN 1..251 FT /note="Calcipressin-1" FT /id="PRO_0000211415" FT REGION 216..251 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 225..239 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P53805" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P53805" FT MOD_RES 216 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 1..133 FT /note="Missing (in isoform C)" FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.4" FT /id="VSP_001318" FT VAR_SEQ 1..81 FT /note="MEDGVAGPRLGEVAEAVEARAPRRVTLRPFAPFSAAAEGDGGGGGDWSFIDC FT EMEEVDLQDLPSATIACHLDPRVFVDGLC -> MHFRDFSYNFSSLIACVANDDVFSES FT ET (in isoform B)" FT /evidence="ECO:0000303|PubMed:10722714, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4" FT /id="VSP_001317" FT VAR_SEQ 1..53 FT /note="Missing (in isoform E)" FT /evidence="ECO:0000303|PubMed:10722714, FT ECO:0000303|PubMed:11231093" FT /id="VSP_059568" FT CONFLICT 205 FT /note="T -> P (in Ref. 1; AAF63485/AAF63486)" FT /evidence="ECO:0000305" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:1WEY" FT HELIX 73..76 FT /evidence="ECO:0007829|PDB:1WEY" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:1WEY" FT HELIX 81..90 FT /evidence="ECO:0007829|PDB:1WEY" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:1WEY" FT TURN 102..105 FT /evidence="ECO:0007829|PDB:1WEY" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:1WEY" FT HELIX 116..122 FT /evidence="ECO:0007829|PDB:1WEY" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:1WEY" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:1WEY" FT CONFLICT Q9JHG6-2:2 FT /note="H -> D (in Ref. 1; AAF63486)" FT /evidence="ECO:0000305" FT CONFLICT Q9JHG6-2:6 FT /note="F -> Y (in Ref. 4; AAF72701)" FT /evidence="ECO:0000305" SQ SEQUENCE 251 AA; 28137 MW; 09F47C73D847FB2B CRC64; MEDGVAGPRL GEVAEAVEAR APRRVTLRPF APFSAAAEGD GGGGGDWSFI DCEMEEVDLQ DLPSATIACH LDPRVFVDGL CRAKFESLFR TYDKDTTFQY FKSFKRVRIN FSNPLSAADA RLRLHKTEFL GKEMKLYFAQ TLHIGSSHLA PPNPDKQFLI SPPASPPVGW KQVEDATPVI NYDLLYAISK LGPGEKYELH AATDTTPSVV VHVCESDQEN EEEEEEMERM KRPKPKIIQT RRPEYTPIHL S //