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Regucalcin (RC) (Gluconolactonase) (GNL) (EC 3.1.1.17) (Senescence marker protein 30) (SMP-30)

 RGN_RAT                 Reviewed;         299 AA.
Q03336; Q63496; Q925W3; Q9QWP2;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 3.
05-JUL-2017, entry version 126.
RecName: Full=Regucalcin;
Short=RC;
AltName: Full=Gluconolactonase;
Short=GNL;
EC=3.1.1.17;
AltName: Full=Senescence marker protein 30;
Short=SMP-30;
Name=Rgn; Synonyms=Smp30;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
SPECIFICITY.
STRAIN=Wistar; TISSUE=Liver;
PubMed=1420310; DOI=10.1016/0167-4781(92)90164-U;
Fujita T., Shirasawa T., Uchida K., Maruyama N.;
"Isolation of cDNA clone encoding rat senescence marker protein-30
(SMP30) and its tissue distribution.";
Biochim. Biophys. Acta 1132:297-305(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Liver;
PubMed=8348951; DOI=10.1016/0014-5793(93)80998-A;
Shimokawa N., Yamaguchi M.;
"Molecular cloning and sequencing of the cDNA coding for a calcium-
binding protein regucalcin from rat liver.";
FEBS Lett. 327:251-255(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Misawa H., Yamaguchi M.;
"The gene family encoding the calcium-binding protein regucalcin.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
STRAIN=Sprague-Dawley;
PubMed=8979263; DOI=10.1007/BF00229476;
Yamaguchi M., Makino R., Shimokawa N.;
"The 5' end sequences and exon organization in rat regucalcin gene.";
Mol. Cell. Biochem. 165:145-150(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-299.
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=8569761; DOI=10.1007/BF01322338;
Shimokawa N., Matsuda Y., Yamaguchi M.;
"Genomic cloning and chromosomal assignment of rat regucalcin gene.";
Mol. Cell. Biochem. 151:157-163(1995).
[7]
PROTEIN SEQUENCE OF 113-124, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=16585534; DOI=10.1073/pnas.0511225103;
Kondo Y., Inai Y., Sato Y., Handa S., Kubo S., Shimokado K., Goto S.,
Nishikimi M., Maruyama N., Ishigami A.;
"Senescence marker protein 30 functions as gluconolactonase in L-
ascorbic acid biosynthesis, and its knockout mice are prone to
scurvy.";
Proc. Natl. Acad. Sci. U.S.A. 103:5723-5728(2006).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=8794449; DOI=10.1016/0047-6374(96)01711-3;
Fujita T., Shirasawa T., Uchida K., Maruyama N.;
"Gene regulation of senescence marker protein-30 (SMP30): coordinated
up-regulation with tissue maturation and gradual down-regulation with
aging.";
Mech. Ageing Dev. 87:219-229(1996).
[9]
FUNCTION, AND COFACTOR.
PubMed=15251439; DOI=10.1016/j.febslet.2004.06.028;
Kondo Y., Ishigami A., Kubo S., Handa S., Gomi K., Hirokawa K.,
Kajiyama N., Chiba T., Shimokado K., Maruyama N.;
"Senescence marker protein-30 is a unique enzyme that hydrolyzes
diisopropyl phosphorofluoridate in the liver.";
FEBS Lett. 570:57-62(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Gluconolactonase with low activity towards other sugar
lactones, including gulonolactone and galactonolactone. Catalyzes
a key step in ascorbic acid (vitamin C) biosynthesis. Can also
hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in
vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and
Ca(2+)-dependent cellular processes and enzyme activities.
{ECO:0000269|PubMed:15251439, ECO:0000269|PubMed:16585534,
ECO:0000269|PubMed:8794449}.
-!- CATALYTIC ACTIVITY: D-glucono-1,5-lactone + H(2)O = D-gluconate.
{ECO:0000269|PubMed:16585534}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:15251439,
ECO:0000269|PubMed:16585534};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:15251439,
ECO:0000269|PubMed:16585534};
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:15251439,
ECO:0000269|PubMed:16585534};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15251439,
ECO:0000269|PubMed:16585534};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:15251439,
ECO:0000269|PubMed:16585534};
Note=Binds 1 divalent metal cation per subunit. Most active with
Zn(2+) and Mn(2+) ions. The physiological cofactor for
gluconolactonase activity is most likely Ca(2+) or Mg(2+). Mg(2+),
Mn(2+) and Co(2+) are equally efficient for the hydrolysis of
diisopropyl phosphorofluoridate. {ECO:0000269|PubMed:15251439,
ECO:0000269|PubMed:16585534};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=9.4 mM for gluconolactone {ECO:0000269|PubMed:16585534};
Vmax=345 umol/min/mg enzyme {ECO:0000269|PubMed:16585534};
pH dependence:
Optimum pH is 6.4. {ECO:0000269|PubMed:16585534};
-!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via UDP-
alpha-D-glucuronate pathway; L-ascorbate from UDP-alpha-D-
glucuronate: step 3/4. {ECO:0000269|PubMed:16585534}.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Detected in liver (at protein level).
Hepatocytes and renal proximal tubular epithelium.
{ECO:0000269|PubMed:1420310, ECO:0000269|PubMed:16585534,
ECO:0000269|PubMed:8794449}.
-!- DEVELOPMENTAL STAGE: In liver, the first peak of expression was
found in 5-day-old neonates. Expression increases from day 7 and
reaches a plateau at day 10. 3-6.5 moth-old adults express about a
third the amount of neonates level. In kidney, expression
increases from day 21 and reaches a maximal level at day 35,
remains high until 3 months of age.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
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EMBL; X69021; CAA48786.1; -; mRNA.
EMBL; D38467; BAA07490.1; -; mRNA.
EMBL; AB037934; BAA90692.1; -; mRNA.
EMBL; BC078794; AAH78794.1; -; mRNA.
EMBL; D67070; BAA11083.1; -; Genomic_DNA.
EMBL; D31662; BAA06507.1; -; Genomic_DNA.
PIR; S34588; S34588.
RefSeq; NP_113734.1; NM_031546.1.
UniGene; Rn.10006; -.
ProteinModelPortal; Q03336; -.
SMR; Q03336; -.
MINT; MINT-4567633; -.
STRING; 10116.ENSRNOP00000010984; -.
iPTMnet; Q03336; -.
PhosphoSitePlus; Q03336; -.
PaxDb; Q03336; -.
PRIDE; Q03336; -.
Ensembl; ENSRNOT00000010984; ENSRNOP00000010984; ENSRNOG00000007949.
GeneID; 25106; -.
KEGG; rno:25106; -.
UCSC; RGD:3560; rat.
CTD; 9104; -.
RGD; 3560; Rgn.
eggNOG; KOG4499; Eukaryota.
eggNOG; COG3386; LUCA.
GeneTree; ENSGT00390000014995; -.
HOGENOM; HOG000220627; -.
HOVERGEN; HBG004347; -.
InParanoid; Q03336; -.
KO; K01053; -.
OMA; CRWDSLT; -.
OrthoDB; EOG091G131G; -.
PhylomeDB; Q03336; -.
TreeFam; TF323663; -.
BioCyc; MetaCyc:MONOMER-13233; -.
BRENDA; 3.1.8.2; 5301.
UniPathway; UPA00991; UER00938.
PRO; PR:Q03336; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000007949; -.
Genevisible; Q03336; RN.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005576; C:extracellular region; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
GO; GO:0004341; F:gluconolactonase activity; IDA:RGD.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
GO; GO:0001822; P:kidney development; IEP:RGD.
GO; GO:0019853; P:L-ascorbic acid biosynthetic process; ISS:UniProtKB.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:1903011; P:negative regulation of bone development; IDA:RGD.
GO; GO:1903611; P:negative regulation of calcium-dependent ATPase activity; IMP:RGD.
GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; IDA:RGD.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:RGD.
GO; GO:1903625; P:negative regulation of DNA catabolic process; IDA:RGD.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:RGD.
GO; GO:1901318; P:negative regulation of flagellated sperm motility; IDA:RGD.
GO; GO:0034260; P:negative regulation of GTPase activity; IMP:RGD.
GO; GO:1903634; P:negative regulation of leucine-tRNA ligase activity; IDA:RGD.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IMP:RGD.
GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IMP:RGD.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:RGD.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
GO; GO:1902679; P:negative regulation of RNA biosynthetic process; IMP:RGD.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:UniProtKB.
GO; GO:1901896; P:positive regulation of calcium-transporting ATPase activity; IDA:RGD.
GO; GO:1903629; P:positive regulation of dUTP diphosphatase activity; IDA:RGD.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:RGD.
GO; GO:0010907; P:positive regulation of glucose metabolic process; IDA:RGD.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:RGD.
GO; GO:0010922; P:positive regulation of phosphatase activity; IMP:RGD.
GO; GO:1903052; P:positive regulation of proteolysis involved in cellular protein catabolic process; IDA:RGD.
GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IDA:RGD.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:RGD.
GO; GO:0050848; P:regulation of calcium-mediated signaling; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IDA:RGD.
Gene3D; 2.120.10.30; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR008367; Regucalcin.
InterPro; IPR013658; SGL.
InterPro; IPR005511; SMP-30.
Pfam; PF08450; SGL; 1.
PRINTS; PR01791; REGUCALCIN.
PRINTS; PR01790; SMP30FAMILY.
1: Evidence at protein level;
Ascorbate biosynthesis; Calcium; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Metal-binding; Phosphoprotein;
Reference proteome.
CHAIN 1 299 Regucalcin.
/FTId=PRO_0000173049.
ACT_SITE 204 204 Proton donor/acceptor. {ECO:0000250}.
METAL 18 18 Divalent metal cation. {ECO:0000250}.
METAL 154 154 Divalent metal cation. {ECO:0000250}.
METAL 204 204 Divalent metal cation. {ECO:0000250}.
BINDING 101 101 Substrate. {ECO:0000250}.
BINDING 103 103 Substrate. {ECO:0000250}.
BINDING 121 121 Substrate. {ECO:0000250}.
MOD_RES 144 144 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q64374}.
MOD_RES 244 244 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q64374}.
MOD_RES 253 253 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q64374}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 148 148 D -> N (in Ref. 2; BAA07490 and 6;
BAA06507). {ECO:0000305}.
SEQUENCE 299 AA; 33390 MW; 5D8F2D95FCA4EE35 CRC64;
MSSIKIECVL RENYRCGESP VWEEASKCLL FVDIPSKTVC RWDSISNRVQ RVGVDAPVSS
VALRQSGGYV ATIGTKFCAL NWEDQSVFIL AMVDEDKKNN RFNDGKVDPA GRYFAGTMAE
ETAPAVLERH QGSLYSLFPD HSVKKYFDQV DISNGLDWSL DHKIFYYIDS LSYTVDAFDY
DLPTGQISNR RTVYKMEKDE QIPDGMCIDV EGKLWVACYN GGRVIRLDPE TGKRLQTVKL
PVDKTTSCCF GGKDYSEMYV TCARDGMSAE GLLRQPDAGN IFKITGLGVK GIAPYSYAG


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