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Protein

Regucalcin

Gene

Rgn

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity2 Publications

Catalytic activityi

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

Cofactori

Zn2+By similarity, Mn2+By similarity, Ca2+By similarity, Mg2+By similarityNote: Binds 1 divalent metal cation per subunit. Most active with Zn2+ and Mn2+ ions. The physiological cofactor is most likely Ca2+ or Mg2+.By similarity

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.2 Publications
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 cation
Binding sitei101 – 1011Substrate
Binding sitei103 – 1031Substrate
Binding sitei121 – 1211Substrate
Metal bindingi154 – 1541Divalent metal cation
Active sitei204 – 2041Proton donor/acceptor1 Publication
Metal bindingi204 – 2041Divalent metal cation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Ascorbate biosynthesis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:108024. Rgn.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice do not thrive after weaning when kept on a vitamin C-less diet. They develop scurvy, have reduced bone mineral density and brittle bones. Hepatocytes exhibit accumulation of lipid droplets. Mice display increased mortality after about 3 months, and their life span is shorter than normal.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299RegucalcinPRO_0000173047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei144 – 1441N6-succinyllysineCombined sources
Modified residuei244 – 2441N6-succinyllysineCombined sources
Modified residuei253 – 2531N6-succinyllysineCombined sources

Proteomic databases

EPDiQ64374.
MaxQBiQ64374.
PaxDbiQ64374.
PRIDEiQ64374.

2D gel databases

REPRODUCTION-2DPAGEQ64374.
SWISS-2DPAGEQ64374.

PTM databases

iPTMnetiQ64374.
PhosphoSiteiQ64374.
SwissPalmiQ64374.

Expressioni

Tissue specificityi

Mainly present in the liver. Weak expression was found in the brain, lung and kidney.2 Publications

Developmental stagei

Protein amounts in liver decrease significantly with age.

Inductioni

By calcium.1 Publication

Gene expression databases

BgeeiQ64374.
CleanExiMM_RGN.
GenevisibleiQ64374. MM.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiQ64374. 3 interactions.
MINTiMINT-1854408.
STRINGi10090.ENSMUSP00000023832.

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Beta strandi15 – 239Combined sources
Turni24 – 274Combined sources
Beta strandi28 – 336Combined sources
Turni34 – 374Combined sources
Beta strandi38 – 436Combined sources
Turni44 – 474Combined sources
Beta strandi48 – 536Combined sources
Beta strandi58 – 647Combined sources
Beta strandi67 – 737Combined sources
Beta strandi76 – 816Combined sources
Turni82 – 854Combined sources
Beta strandi86 – 927Combined sources
Beta strandi98 – 10710Combined sources
Beta strandi113 – 1197Combined sources
Beta strandi132 – 1376Combined sources
Beta strandi143 – 15816Combined sources
Beta strandi164 – 1696Combined sources
Helixi170 – 1723Combined sources
Beta strandi174 – 1818Combined sources
Turni182 – 1854Combined sources
Beta strandi186 – 19510Combined sources
Helixi198 – 2003Combined sources
Beta strandi202 – 2098Combined sources
Beta strandi214 – 2196Combined sources
Turni220 – 2223Combined sources
Beta strandi223 – 2275Combined sources
Turni229 – 2313Combined sources
Beta strandi234 – 2396Combined sources
Beta strandi245 – 2528Combined sources
Helixi253 – 2553Combined sources
Beta strandi257 – 2637Combined sources
Helixi269 – 2746Combined sources
Turni276 – 2794Combined sources
Beta strandi281 – 2855Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GN7X-ray1.95A/B1-299[»]
4GN8X-ray1.70A/B1-299[»]
4GN9X-ray2.00A/B1-299[»]
4GNAX-ray1.85A/B1-299[»]
ProteinModelPortaliQ64374.
SMRiQ64374. Positions 3-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SMP-30/CGR1 family.Curated

Phylogenomic databases

eggNOGiKOG4499. Eukaryota.
COG3386. LUCA.
GeneTreeiENSGT00390000014995.
HOGENOMiHOG000220627.
HOVERGENiHBG004347.
InParanoidiQ64374.
KOiK01053.
OMAiCARDGMD.
OrthoDBiEOG77127C.
PhylomeDBiQ64374.
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.

Q64374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSIKVECVL RENYRCGESP VWEEASQSLL FVDIPSKIIC RWDTVSNQVQ
60 70 80 90 100
RVAVDAPVSS VALRQLGGYV ATIGTKFCAL NWENQSVFVL AMVDEDKKNN
110 120 130 140 150
RFNDGKVDPA GRYFAGTMAE ETAPAVLERH QGSLYSLFPD HSVKKYFDQV
160 170 180 190 200
DISNGLDWSL DHKIFYYIDS LSYTVDAFDY DLQTGQISNR RIVYKMEKDE
210 220 230 240 250
QIPDGMCIDA EGKLWVACYN GGRVIRLDPE TGKRLQTVKL PVDKTTSCCF
260 270 280 290
GGKDYSEMYV TCARDGLNAE GLLRQPDAGN IFKITGLGVK GIAPYSYAG
Length:299
Mass (Da):33,407
Last modified:November 1, 1996 - v1
Checksum:iDAD55EF618311977
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011Q → R in BAE27192 (PubMed:16141072).Curated
Sequence conflicti236 – 2361Q → P in BAE27192 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28937 mRNA. Translation: AAC52721.1.
U32170 Genomic DNA. Translation: AAD03478.1.
D86217 mRNA. Translation: BAA13046.1.
AK146465 mRNA. Translation: BAE27192.1.
AL672073 Genomic DNA. Translation: CAM21274.1.
BC012710 mRNA. Translation: AAH12710.1.
CCDSiCCDS30043.1.
PIRiS72173.
RefSeqiNP_033086.1. NM_009060.2.
XP_006527635.1. XM_006527572.2.
UniGeneiMm.2118.

Genome annotation databases

EnsembliENSMUST00000023832; ENSMUSP00000023832; ENSMUSG00000023070.
GeneIDi19733.
KEGGimmu:19733.
UCSCiuc009std.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28937 mRNA. Translation: AAC52721.1.
U32170 Genomic DNA. Translation: AAD03478.1.
D86217 mRNA. Translation: BAA13046.1.
AK146465 mRNA. Translation: BAE27192.1.
AL672073 Genomic DNA. Translation: CAM21274.1.
BC012710 mRNA. Translation: AAH12710.1.
CCDSiCCDS30043.1.
PIRiS72173.
RefSeqiNP_033086.1. NM_009060.2.
XP_006527635.1. XM_006527572.2.
UniGeneiMm.2118.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GN7X-ray1.95A/B1-299[»]
4GN8X-ray1.70A/B1-299[»]
4GN9X-ray2.00A/B1-299[»]
4GNAX-ray1.85A/B1-299[»]
ProteinModelPortaliQ64374.
SMRiQ64374. Positions 3-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ64374. 3 interactions.
MINTiMINT-1854408.
STRINGi10090.ENSMUSP00000023832.

PTM databases

iPTMnetiQ64374.
PhosphoSiteiQ64374.
SwissPalmiQ64374.

2D gel databases

REPRODUCTION-2DPAGEQ64374.
SWISS-2DPAGEQ64374.

Proteomic databases

EPDiQ64374.
MaxQBiQ64374.
PaxDbiQ64374.
PRIDEiQ64374.

Protocols and materials databases

DNASUi19733.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023832; ENSMUSP00000023832; ENSMUSG00000023070.
GeneIDi19733.
KEGGimmu:19733.
UCSCiuc009std.1. mouse.

Organism-specific databases

CTDi9104.
MGIiMGI:108024. Rgn.

Phylogenomic databases

eggNOGiKOG4499. Eukaryota.
COG3386. LUCA.
GeneTreeiENSGT00390000014995.
HOGENOMiHOG000220627.
HOVERGENiHBG004347.
InParanoidiQ64374.
KOiK01053.
OMAiCARDGMD.
OrthoDBiEOG77127C.
PhylomeDBiQ64374.
TreeFamiTF323663.

Enzyme and pathway databases

UniPathwayiUPA00991; UER00938.

Miscellaneous databases

PROiQ64374.
SOURCEiSearch...

Gene expression databases

BgeeiQ64374.
CleanExiMM_RGN.
GenevisibleiQ64374. MM.

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 and characterization of genomic and cDNA clones encoding mouse senescence marker protein-30 (SMP30)."
    Fujita T., Shirasawa T., Maruyama N.
    Biochim. Biophys. Acta 1308:49-57(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "Molecular cloning of the cDNA coding for regucalcin and its mRNA expression in mouse liver: the expression is stimulated by calcium administration."
    Murata T., Yamaguchi M.
    Mol. Cell. Biochem. 173:127-133(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Tissue: Liver.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic liver.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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].
    Strain: FVB/N.
    Tissue: Liver.
  6. "SMP30 deficiency in mice causes an accumulation of neutral lipids and phospholipids in the liver and shortens the life span."
    Ishigami A., Kondo Y., Nanba R., Ohsawa T., Handa S., Kubo S., Akita M., Maruyama N.
    Biochem. Biophys. Res. Commun. 315:575-580(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  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: DISRUPTION PHENOTYPE, FUNCTION, PATHWAY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver and Pancreas.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-144; LYS-244 AND LYS-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Structural basis of the gamma-lactone-ring formation in ascorbic acid biosynthesis by the senescence marker protein-30/gluconolactonase."
    Aizawa S., Senda M., Harada A., Maruyama N., Ishida T., Aigaki T., Ishigami A., Senda T.
    PLoS ONE 8:E53706-E53706(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, FUNCTION, PATHWAY, COFACTOR, ACTIVE SITE, SUBUNIT.

Entry informationi

Entry nameiRGN_MOUSE
AccessioniPrimary (citable) accession number: Q64374
Secondary accession number(s): A2AFC8, Q3UJG3, Q60944
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.