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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)DescriptionActionsGraphical viewLength
Metal bindingi18Divalent metal cation1
Binding sitei101Substrate1
Binding sitei103Substrate1
Binding sitei121Substrate1
Metal bindingi154Divalent metal cation1
Active sitei204Proton donor/acceptor1 Publication1
Metal bindingi204Divalent metal cation1

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
  • extracellular region Source: GO_Central
  • 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)DescriptionActionsGraphical viewLength
ChainiPRO_00001730471 – 299RegucalcinAdd BLAST299

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei144N6-succinyllysineCombined sources1
Modified residuei244N6-succinyllysineCombined sources1
Modified residuei253N6-succinyllysineCombined sources1

Proteomic databases

MaxQBiQ64374.
PaxDbiQ64374.
PeptideAtlasiQ64374.
PRIDEiQ64374.

2D gel databases

REPRODUCTION-2DPAGEQ64374.
SWISS-2DPAGEQ64374.

PTM databases

iPTMnetiQ64374.
PhosphoSitePlusiQ64374.
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

BgeeiENSMUSG00000023070.
CleanExiMM_RGN.
GenevisibleiQ64374. MM.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

1299
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Beta strandi15 – 23Combined sources9
Turni24 – 27Combined sources4
Beta strandi28 – 33Combined sources6
Turni34 – 37Combined sources4
Beta strandi38 – 43Combined sources6
Turni44 – 47Combined sources4
Beta strandi48 – 53Combined sources6
Beta strandi58 – 64Combined sources7
Beta strandi67 – 73Combined sources7
Beta strandi76 – 81Combined sources6
Turni82 – 85Combined sources4
Beta strandi86 – 92Combined sources7
Beta strandi98 – 107Combined sources10
Beta strandi113 – 119Combined sources7
Beta strandi132 – 137Combined sources6
Beta strandi143 – 158Combined sources16
Beta strandi164 – 169Combined sources6
Helixi170 – 172Combined sources3
Beta strandi174 – 181Combined sources8
Turni182 – 185Combined sources4
Beta strandi186 – 195Combined sources10
Helixi198 – 200Combined sources3
Beta strandi202 – 209Combined sources8
Beta strandi214 – 219Combined sources6
Turni220 – 222Combined sources3
Beta strandi223 – 227Combined sources5
Turni229 – 231Combined sources3
Beta strandi234 – 239Combined sources6
Beta strandi245 – 252Combined sources8
Helixi253 – 255Combined sources3
Beta strandi257 – 263Combined sources7
Helixi269 – 274Combined sources6
Turni276 – 279Combined sources4
Beta strandi281 – 285Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
OrthoDBiEOG091G131G.
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)DescriptionActionsGraphical viewLength
Sequence conflicti201Q → R in BAE27192 (PubMed:16141072).Curated1
Sequence conflicti236Q → P in BAE27192 (PubMed:16141072).Curated1

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_006527572.3.
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_006527572.3.
UniGeneiMm.2118.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ64374.
PhosphoSitePlusiQ64374.
SwissPalmiQ64374.

2D gel databases

REPRODUCTION-2DPAGEQ64374.
SWISS-2DPAGEQ64374.

Proteomic databases

MaxQBiQ64374.
PaxDbiQ64374.
PeptideAtlasiQ64374.
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.
OrthoDBiEOG091G131G.
PhylomeDBiQ64374.
TreeFamiTF323663.

Enzyme and pathway databases

UniPathwayiUPA00991; UER00938.

Miscellaneous databases

PROiQ64374.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000023070.
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...

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: November 2, 2016
This is version 121 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.