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RCAN3_MOUSE
ID   RCAN3_MOUSE             Reviewed;         239 AA.
AC   Q9JKK0; Q3U2I5; Q9CX87;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Calcipressin-3;
DE   AltName: Full=Down syndrome candidate region 1-like protein 2;
DE   AltName: Full=Myocyte-enriched calcineurin-interacting protein 3;
DE            Short=MCIP3;
DE   AltName: Full=Regulator of calcineurin 3;
GN   Name=Rcan3; Synonyms=Dscr1l2;
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].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic head, and Thymus;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with protein phosphatase PPP3CA/calcineurin A.
CC       {ECO:0000250|UniProtKB:Q9UKA8}.
CC   -!- SIMILARITY: Belongs to the RCAN family. {ECO:0000305}.
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DR   EMBL; AF237888; AAF62539.1; -; mRNA.
DR   EMBL; AK019377; BAB31687.1; -; mRNA.
DR   EMBL; AK042201; BAE20626.1; -; mRNA.
DR   EMBL; AK155270; BAE33155.1; -; mRNA.
DR   EMBL; AL627185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC059001; AAH59001.1; -; mRNA.
DR   CCDS; CCDS18785.1; -.
DR   RefSeq; NP_075356.1; NM_022980.4.
DR   RefSeq; XP_017175806.1; XM_017320317.1.
DR   AlphaFoldDB; Q9JKK0; -.
DR   SMR; Q9JKK0; -.
DR   STRING; 10090.ENSMUSP00000030606; -.
DR   iPTMnet; Q9JKK0; -.
DR   PhosphoSitePlus; Q9JKK0; -.
DR   EPD; Q9JKK0; -.
DR   jPOST; Q9JKK0; -.
DR   MaxQB; Q9JKK0; -.
DR   PaxDb; Q9JKK0; -.
DR   PRIDE; Q9JKK0; -.
DR   ProteomicsDB; 255169; -.
DR   Antibodypedia; 30319; 254 antibodies from 22 providers.
DR   DNASU; 53902; -.
DR   Ensembl; ENSMUST00000030606; ENSMUSP00000030606; ENSMUSG00000059713.
DR   GeneID; 53902; -.
DR   KEGG; mmu:53902; -.
DR   UCSC; uc008vgm.1; mouse.
DR   CTD; 11123; -.
DR   MGI; MGI:1858220; Rcan3.
DR   VEuPathDB; HostDB:ENSMUSG00000059713; -.
DR   eggNOG; KOG4019; Eukaryota.
DR   GeneTree; ENSGT00940000159501; -.
DR   InParanoid; Q9JKK0; -.
DR   OMA; RMRVNYN; -.
DR   OrthoDB; 1585262at2759; -.
DR   PhylomeDB; Q9JKK0; -.
DR   TreeFam; TF313579; -.
DR   BioGRID-ORCS; 53902; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Rcan3; mouse.
DR   PRO; PR:Q9JKK0; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9JKK0; protein.
DR   Bgee; ENSMUSG00000059713; Expressed in animal zygote and 227 other tissues.
DR   ExpressionAtlas; Q9JKK0; baseline and differential.
DR   Genevisible; Q9JKK0; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR   GO; GO:0031013; F:troponin I binding; ISO:MGI.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
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; IPR034923; RCAN3.
DR   PANTHER; PTHR10300; PTHR10300; 1.
DR   PANTHER; PTHR10300:SF6; PTHR10300:SF6; 1.
DR   Pfam; PF04847; Calcipressin; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome.
FT   CHAIN           1..239
FT                   /note="Calcipressin-3"
FT                   /id="PRO_0000211421"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..203
FT                   /note="Calcineurin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA8"
FT   REGION          202..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   239 AA;  27153 MW;  1B2687B47BB4D272 CRC64;
     MLRDSLKSWN DSQSDLCSSD QEEEEEMVFG ENEDGLEEMM DLSDLPTSLF ACSVHEAVFE
     VQEQKERFEA LFTLYDDQVT FQLFKSFRRV RINFSKPEAA ARARIELHES EFHGRKLKLY
     FAQVQVSGEA RDKSYLLPPQ PTKQFLISPP ASPPVGWKQS EDAMPVINYD LLCAVSKLGP
     GEKYELHAGT ESTPSVVVHV CESETEEEED TKNPKQKITQ TRRPEAPTAA LSERLDCAL
 
 
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