位置:首页 > 蛋白库 > RCAN1_MOUSE
RCAN1_MOUSE
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   03-AUG-2022, entry version 162.
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; Q9JHG6; -.
DR   PRIDE; Q9JHG6; -.
DR   ProteomicsDB; 255166; -. [Q9JHG6-1]
DR   ProteomicsDB; 255167; -. [Q9JHG6-2]
DR   ProteomicsDB; 255168; -. [Q9JHG6-3]
DR   ProteomicsDB; 329214; -.
DR   Antibodypedia; 22959; 580 antibodies from 35 providers.
DR   DNASU; 54720; -.
DR   Ensembl; ENSMUST00000023672; ENSMUSP00000023672; ENSMUSG00000022951. [Q9JHG6-2]
DR   Ensembl; ENSMUST00000060005; ENSMUSP00000060394; ENSMUSG00000022951. [Q9JHG6-1]
DR   Ensembl; ENSMUST00000231410; ENSMUSP00000156110; ENSMUSG00000022951. [Q9JHG6-3]
DR   Ensembl; ENSMUST00000232197; ENSMUSP00000155863; ENSMUSG00000022951. [Q9JHG6-3]
DR   Ensembl; ENSMUST00000232239; ENSMUSP00000156053; ENSMUSG00000022951. [Q9JHG6-4]
DR   GeneID; 54720; -.
DR   KEGG; mmu:54720; -.
DR   UCSC; uc007zze.2; mouse.
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; DMPPVVC; -.
DR   OrthoDB; 1585262at2759; -.
DR   PhylomeDB; Q9JHG6; -.
DR   TreeFam; TF313579; -.
DR   BioGRID-ORCS; 54720; 2 hits in 73 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 287 other tissues.
DR   ExpressionAtlas; Q9JHG6; baseline and differential.
DR   Genevisible; Q9JHG6; MM.
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:0043666; P:regulation of phosphoprotein phosphatase activity; IDA: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; IPR031271; RCAN1.
DR   InterPro; IPR034906; RCAN1_RRM.
DR   PANTHER; PTHR10300; PTHR10300; 1.
DR   PANTHER; PTHR10300:SF4; PTHR10300:SF4; 1.
DR   Pfam; PF04847; Calcipressin; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024