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Protein

Regucalcin

Gene

Rgn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Ca2+ signaling, and Ca2+-dependent cellular processes and enzyme activities.3 Publications

Catalytic activityi

D-glucono-1,5-lactone + H2O = D-gluconate.1 Publication

Cofactori

Zn2+2 Publications, Mn2+2 Publications, Ca2+2 Publications, Mg2+2 Publications, Co2+2 PublicationsNote: Binds 1 divalent metal cation per subunit. Most active with Zn2+ and Mn2+ ions. The physiological cofactor for gluconolactonase activity is most likely Ca2+ or Mg2+. Mg2+, Mn2+ and Co2+ are equally efficient for the hydrolysis of diisopropyl phosphorofluoridate.2 Publications

Kineticsi

  1. KM=9.4 mM for gluconolactone1 Publication
  1. Vmax=345 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6.4.1 Publication

Pathwayi: L-ascorbate biosynthesis via UDP-alpha-D-glucuronate pathway

This protein is involved in step 3 of the subpathway that synthesizes L-ascorbate from UDP-alpha-D-glucuronate.1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Regucalcin (Rgn)
  4. L-gulonolactone oxidase (Gulo)
This subpathway is part of the pathway L-ascorbate biosynthesis via UDP-alpha-D-glucuronate pathway, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ascorbate from UDP-alpha-D-glucuronate, the pathway L-ascorbate biosynthesis via UDP-alpha-D-glucuronate pathway and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Divalent metal cationBy similarity
Binding sitei101 – 1011SubstrateBy similarity
Binding sitei103 – 1031SubstrateBy similarity
Binding sitei121 – 1211SubstrateBy similarity
Metal bindingi154 – 1541Divalent metal cationBy similarity
Active sitei204 – 2041Proton donor/acceptorBy similarity
Metal bindingi204 – 2041Divalent metal cationBy similarity

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • cellular calcium ion homeostasis Source: UniProtKB
  • kidney development Source: RGD
  • L-ascorbic acid biosynthetic process Source: UniProtKB
  • liver development Source: RGD
  • liver regeneration Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of bone development Source: RGD
  • negative regulation of calcium-dependent ATPase activity Source: RGD
  • negative regulation of cyclic-nucleotide phosphodiesterase activity Source: RGD
  • negative regulation of DNA biosynthetic process Source: RGD
  • negative regulation of DNA catabolic process Source: RGD
  • negative regulation of epithelial cell proliferation Source: RGD
  • negative regulation of GTPase activity Source: RGD
  • negative regulation of leucine-tRNA ligase activity Source: RGD
  • negative regulation of nitric oxide biosynthetic process Source: RGD
  • negative regulation of phosphoprotein phosphatase activity Source: RGD
  • negative regulation of protein kinase activity Source: RGD
  • negative regulation of protein phosphorylation Source: RGD
  • negative regulation of RNA biosynthetic process Source: RGD
  • negative regulation of sperm motility Source: RGD
  • positive regulation of ATPase activity Source: UniProtKB
  • positive regulation of calcium-transporting ATPase activity Source: RGD
  • positive regulation of dUTP diphosphatase activity Source: RGD
  • positive regulation of fatty acid biosynthetic process Source: RGD
  • positive regulation of glucose metabolic process Source: RGD
  • positive regulation of GTPase activity Source: RGD
  • positive regulation of phosphatase activity Source: RGD
  • positive regulation of proteolysis involved in cellular protein catabolic process Source: RGD
  • positive regulation of superoxide dismutase activity Source: RGD
  • positive regulation of triglyceride biosynthetic process Source: RGD
  • regulation of calcium-mediated signaling Source: UniProtKB
  • spermatogenesis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Ascorbate biosynthesis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13233.
BRENDAi3.1.8.2. 5301.
UniPathwayiUPA00991; UER00938.

Names & Taxonomyi

Protein namesi
Recommended name:
Regucalcin
Short name:
RC
Alternative name(s):
Gluconolactonase (EC:3.1.1.17)
Short name:
GNL
Senescence marker protein 30
Short name:
SMP-30
Gene namesi
Name:Rgn
Synonyms:Smp30
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi3560. Rgn.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: RGD
  • nucleoplasm Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299RegucalcinPRO_0000173049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei144 – 1441N6-succinyllysineBy similarity
Modified residuei244 – 2441N6-succinyllysineBy similarity
Modified residuei253 – 2531N6-succinyllysineBy similarity
Modified residuei268 – 2681PhosphoserineCombined sources

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ03336.
PRIDEiQ03336.

PTM databases

iPTMnetiQ03336.
PhosphoSiteiQ03336.

Expressioni

Tissue specificityi

Detected in liver (at protein level). Hepatocytes and renal proximal tubular epithelium.3 Publications

Developmental stagei

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.

Gene expression databases

GenevisibleiQ03336. RN.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

MINTiMINT-4567633.
STRINGi10116.ENSRNOP00000010984.

Structurei

3D structure databases

ProteinModelPortaliQ03336.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SMP-30/CGR1 family.Curated

Phylogenomic databases

eggNOGiKOG4499. Eukaryota.
COG3386. LUCA.
GeneTreeiENSGT00390000014995.
HOGENOMiHOG000220627.
HOVERGENiHBG004347.
InParanoidiQ03336.
KOiK01053.
OMAiCARDGMD.
OrthoDBiEOG77127C.
PhylomeDBiQ03336.
TreeFamiTF323663.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR008367. Regucalcin.
IPR013658. SGL.
IPR005511. SMP-30.
[Graphical view]
PfamiPF08450. SGL. 1 hit.
[Graphical view]
PRINTSiPR01791. REGUCALCIN.
PR01790. SMP30FAMILY.

Sequencei

Sequence statusi: Complete.

Q03336-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSIKIECVL RENYRCGESP VWEEASKCLL FVDIPSKTVC RWDSISNRVQ
60 70 80 90 100
RVGVDAPVSS VALRQSGGYV ATIGTKFCAL NWEDQSVFIL AMVDEDKKNN
110 120 130 140 150
RFNDGKVDPA GRYFAGTMAE ETAPAVLERH QGSLYSLFPD HSVKKYFDQV
160 170 180 190 200
DISNGLDWSL DHKIFYYIDS LSYTVDAFDY DLPTGQISNR RTVYKMEKDE
210 220 230 240 250
QIPDGMCIDV EGKLWVACYN GGRVIRLDPE TGKRLQTVKL PVDKTTSCCF
260 270 280 290
GGKDYSEMYV TCARDGMSAE GLLRQPDAGN IFKITGLGVK GIAPYSYAG
Length:299
Mass (Da):33,390
Last modified:June 21, 2005 - v3
Checksum:i5D8F2D95FCA4EE35
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481D → N in BAA07490 (PubMed:8348951).Curated
Sequence conflicti148 – 1481D → N in BAA06507 (PubMed:8569761).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69021 mRNA. Translation: CAA48786.1.
D38467 mRNA. Translation: BAA07490.1.
AB037934 mRNA. Translation: BAA90692.1.
BC078794 mRNA. Translation: AAH78794.1.
D67070 Genomic DNA. Translation: BAA11083.1.
D31662 Genomic DNA. Translation: BAA06507.1.
PIRiS34588.
RefSeqiNP_113734.1. NM_031546.1.
UniGeneiRn.10006.

Genome annotation databases

EnsembliENSRNOT00000010984; ENSRNOP00000010984; ENSRNOG00000007949.
GeneIDi25106.
KEGGirno:25106.
UCSCiRGD:3560. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69021 mRNA. Translation: CAA48786.1.
D38467 mRNA. Translation: BAA07490.1.
AB037934 mRNA. Translation: BAA90692.1.
BC078794 mRNA. Translation: AAH78794.1.
D67070 Genomic DNA. Translation: BAA11083.1.
D31662 Genomic DNA. Translation: BAA06507.1.
PIRiS34588.
RefSeqiNP_113734.1. NM_031546.1.
UniGeneiRn.10006.

3D structure databases

ProteinModelPortaliQ03336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4567633.
STRINGi10116.ENSRNOP00000010984.

PTM databases

iPTMnetiQ03336.
PhosphoSiteiQ03336.

Proteomic databases

PaxDbiQ03336.
PRIDEiQ03336.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010984; ENSRNOP00000010984; ENSRNOG00000007949.
GeneIDi25106.
KEGGirno:25106.
UCSCiRGD:3560. rat.

Organism-specific databases

CTDi9104.
RGDi3560. Rgn.

Phylogenomic databases

eggNOGiKOG4499. Eukaryota.
COG3386. LUCA.
GeneTreeiENSGT00390000014995.
HOGENOMiHOG000220627.
HOVERGENiHBG004347.
InParanoidiQ03336.
KOiK01053.
OMAiCARDGMD.
OrthoDBiEOG77127C.
PhylomeDBiQ03336.
TreeFamiTF323663.

Enzyme and pathway databases

UniPathwayiUPA00991; UER00938.
BioCyciMetaCyc:MONOMER-13233.
BRENDAi3.1.8.2. 5301.

Miscellaneous databases

PROiQ03336.

Gene expression databases

GenevisibleiQ03336. RN.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR008367. Regucalcin.
IPR013658. SGL.
IPR005511. SMP-30.
[Graphical view]
PfamiPF08450. SGL. 1 hit.
[Graphical view]
PRINTSiPR01791. REGUCALCIN.
PR01790. SMP30FAMILY.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of cDNA clone encoding rat senescence marker protein-30 (SMP30) and its tissue distribution."
    Fujita T., Shirasawa T., Uchida K., Maruyama N.
    Biochim. Biophys. Acta 1132:297-305(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
    Strain: Wistar.
    Tissue: Liver.
  2. "Molecular cloning and sequencing of the cDNA coding for a calcium-binding protein regucalcin from rat liver."
    Shimokawa N., Yamaguchi M.
    FEBS Lett. 327:251-255(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  3. "The gene family encoding the calcium-binding protein regucalcin."
    Misawa H., Yamaguchi M.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  5. "The 5' end sequences and exon organization in rat regucalcin gene."
    Yamaguchi M., Makino R., Shimokawa N.
    Mol. Cell. Biochem. 165:145-150(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
    Strain: Sprague-Dawley.
  6. "Genomic cloning and chromosomal assignment of rat regucalcin gene."
    Shimokawa N., Matsuda Y., Yamaguchi M.
    Mol. Cell. Biochem. 151:157-163(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-299.
    Strain: Sprague-Dawley.
    Tissue: Kidney.
  7. "Senescence marker protein 30 functions as gluconolactonase in L-ascorbic acid biosynthesis, and its knockout mice are prone to scurvy."
    Kondo Y., Inai Y., Sato Y., Handa S., Kubo S., Shimokado K., Goto S., Nishikimi M., Maruyama N., Ishigami A.
    Proc. Natl. Acad. Sci. U.S.A. 103:5723-5728(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 113-124, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
  8. "Gene regulation of senescence marker protein-30 (SMP30): coordinated up-regulation with tissue maturation and gradual down-regulation with aging."
    Fujita T., Shirasawa T., Uchida K., Maruyama N.
    Mech. Ageing Dev. 87:219-229(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "Senescence marker protein-30 is a unique enzyme that hydrolyzes diisopropyl phosphorofluoridate in the liver."
    Kondo Y., Ishigami A., Kubo S., Handa S., Gomi K., Hirokawa K., Kajiyama N., Chiba T., Shimokado K., Maruyama N.
    FEBS Lett. 570:57-62(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR.
  10. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRGN_RAT
AccessioniPrimary (citable) accession number: Q03336
Secondary accession number(s): Q63496, Q925W3, Q9QWP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: June 21, 2005
Last modified: June 8, 2016
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.