(data stored in ACNUC22986 zone)

HOVERGEN: RGN_MOUSE

ID   RGN_MOUSE               Reviewed;         299 AA.
AC   Q64374; A2AFC8; Q3UJG3; Q60944;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-NOV-2009, entry version 71.
DE   RecName: Full=Regucalcin;
DE            Short=RC;
DE   AltName: Full=Senescence marker protein 30;
DE            Short=SMP-30;
GN   Name=Rgn; Synonyms=Smp30;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Liver;
RX   MEDLINE=96328264; PubMed=8765750; DOI=10.1016/0167-4781(96)00064-4;
RA   Fujita T., Shirasawa T., Maruyama N.;
RT   "Isolation and characterization of genomic and cDNA clones encoding
RT   mouse senescence marker protein-30 (SMP30).";
RL   Biochim. Biophys. Acta 1308:49-57(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Liver;
RX   MEDLINE=97422495; PubMed=9278263; DOI=10.1023/A:1006887929369;
RA   Murata T., Yamaguchi M.;
RT   "Molecular cloning of the cDNA coding for regucalcin and its mRNA
RT   expression in mouse liver: the expression is stimulated by calcium
RT   administration.";
RL   Mol. Cell. Biochem. 173:127-133(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic liver;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Calcium-binding protein which regulates Ca(2+) signaling
CC       by regulating Ca(2+)-dependent enzymatic activity in the liver and
CC       kidney. Decrease of RGN leads to the dysregulation of calcium
CC       signaling in the aged liver (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Mainly present in the liver. Weak expression
CC       was found in the brain, lung and kidney.
CC   -!- DEVELOPMENTAL STAGE: Protein amounts in liver decrease
CC       significantly with age.
CC   -!- INDUCTION: By calcium.
CC   -!- SIMILARITY: Belongs to the SMP-30/CGR1 family.
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CC   -!- GENE_FAMILY: HBG004347 [ FAMILY / ALN / TREE ]
DR   EMBL; U28937; AAC52721.1; -; mRNA.
DR   EMBL; U32170; AAD03478.1; -; Genomic_DNA.
DR   EMBL; D86217; BAA13046.1; -; mRNA.
DR   EMBL; AK146465; BAE27192.1; -; mRNA.
DR   EMBL; AL672073; CAM21274.1; -; Genomic_DNA.
DR   EMBL; BC012710; AAH12710.1; -; mRNA.
DR   IPI; IPI00133456; -.
DR   PIR; S72173; S72173.
DR   RefSeq; NP_033086.1; -.
DR   UniGene; Mm.2118; -.
DR   STRING; Q64374; -.
DR   PhosphoSite; Q64374; -.
DR   SWISS-2DPAGE; Q64374; -.
DR   REPRODUCTION-2DPAGE; Q64374; -.
DR   PRIDE; Q64374; -.
DR   Ensembl; ENSMUST00000023832; ENSMUSP00000023832; ENSMUSG00000023070; Mus musculus.
DR   GeneID; 19733; -.
DR   KEGG; mmu:19733; -.
DR   NMPDR; fig|10090.3.peg.21318; -.
DR   UCSC; uc009std.1; mouse.
DR   CTD; 19733; -.
DR   MGI; MGI:108024; Rgn.
DR   HOGENOM; Q64374; -.
DR   HOVERGEN; Q64374; -.
DR   OMA; CDNPSNP; -.
DR   NextBio; 297164; -.
DR   ArrayExpress; Q64374; -.
DR   Bgee; Q64374; -.
DR   CleanEx; MM_RGN; -.
DR   Genevestigator; Q64374; -.
DR   GermOnline; ENSMUSG00000023070; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0032781; P:positive regulation of ATPase activity; ISS:UniProtKB.
DR   GO; GO:0050848; P:regulation of calcium-mediated signaling; ISS:UniProtKB.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR008367; Regucalcin.
DR   InterPro; IPR013658; SGL.
DR   InterPro; IPR005511; SMP-30.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Pfam; PF08450; SGL; 1.
DR   PRINTS; PR01791; REGUCALCIN.
DR   PRINTS; PR01790; SMP30FAMILY.
PE   1: Evidence at protein level;
DR   PRODOM; Q64374.
DR   SWISS-2DPAGE; Q64374.
KW   Calcium; Cytoplasm; Phosphoprotein.
FT   DOMAIN        1    135       PRODOM:2005.1:PD592867  80
FT   DOMAIN      152    174       PRODOM:2005.1:PD792520  22
FT   DOMAIN      175    224       PRODOM:2005.1:PD009905  108
FT   DOMAIN      225    299       PRODOM:2005.1:PD225809  78
FT   CHAIN         1    299       Regucalcin.
FT                                /FTId=PRO_0000173047.
FT   MOD_RES       3      3       Phosphoserine.
FT   CONFLICT    201    201       Q -> R (in Ref. 3; BAE27192).
FT   CONFLICT    236    236       Q -> P (in Ref. 3; BAE27192).
SQ   SEQUENCE   299 AA;  33407 MW;  DAD55EF618311977 CRC64;
     MSSIKVECVL RENYRCGESP VWEEASQSLL FVDIPSKIIC RWDTVSNQVQ RVAVDAPVSS
     VALRQLGGYV ATIGTKFCAL NWENQSVFVL AMVDEDKKNN RFNDGKVDPA GRYFAGTMAE
     ETAPAVLERH QGSLYSLFPD HSVKKYFDQV DISNGLDWSL DHKIFYYIDS LSYTVDAFDY
     DLQTGQISNR RIVYKMEKDE QIPDGMCIDA EGKLWVACYN GGRVIRLDPE TGKRLQTVKL
     PVDKTTSCCF GGKDYSEMYV TCARDGLNAE GLLRQPDAGN IFKITGLGVK GIAPYSYAG
//

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