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Protein

Regucalcin

Gene

rgn

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 similarity

Catalytic activityi

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

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.
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. no protein annotated in this organism
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

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
Short name:
xSMP-30
Gene namesi
Name:rgnBy similarity
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865001. rgn.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299RegucalcinPRO_0000287686Add
BLAST

Expressioni

Tissue specificityi

Expressed in the liver, and in the pronephros from the late tadpole stage.1 Publication

Inductioni

By activin and retinoic acid.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9I922.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SMP-30/CGR1 family.By similarity

Phylogenomic databases

HOVERGENiHBG004347.
KOiK01053.

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.

Q9I922-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSIKIECVV SETYKIGESP VWEEKEGTLL FVDITGQKVC RWDPSTKKVQ
60 70 80 90 100
SVSVEAPIGS VALRKSGGYV LAMGNTFSAL NWEDQSVTTL ARVDEDKPNN
110 120 130 140 150
RFNDGKVDPE GRFLAGTMSQ EIRPAVVERN QGSLFTLYPD HSVVKHFDMV
160 170 180 190 200
DISNGLDWSL DHKTLYYIDS LSFKVDALDY DMKTGKSSNR RTLYKLQQDE
210 220 230 240 250
GIPDGMCIDA EGKLWVACYN GGRVIRIDPE TGKQIQTVKL PIDKTTSCCF
260 270 280 290
GGPDYSEMYV TSACDGMDED WKKRQPQSGG IYKITGLGVK GIAPTAFAG
Length:299
Mass (Da):33,087
Last modified:October 1, 2000 - v1
Checksum:iBABB9749258BB2C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti285 – 2851T → S in BAA93719 (PubMed:10727865).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037936 mRNA. Translation: BAA90694.1.
AB033368 mRNA. Translation: BAA93719.1.
RefSeqiNP_001079124.1. NM_001085655.1.
UniGeneiXl.983.

Genome annotation databases

GeneIDi373659.
KEGGixla:373659.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037936 mRNA. Translation: BAA90694.1.
AB033368 mRNA. Translation: BAA93719.1.
RefSeqiNP_001079124.1. NM_001085655.1.
UniGeneiXl.983.

3D structure databases

ProteinModelPortaliQ9I922.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi373659.
KEGGixla:373659.

Organism-specific databases

CTDi9104.
XenbaseiXB-GENE-865001. rgn.

Phylogenomic databases

HOVERGENiHBG004347.
KOiK01053.

Enzyme and pathway databases

UniPathwayiUPA00991; UER00938.

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

  1. "The gene of Ca2+-binding protein regucalcin is highly conserved in vertebrate species."
    Misawa H., Yamaguchi M.
    Int. J. Mol. Med. 6:191-196(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: LiverImported.
  2. "Cloning and expression pattern of a Xenopus pronephros-specific gene, XSMP-30."
    Sato A., Asashima M., Yokota T., Nishinakamura R.
    Mech. Dev. 92:273-275(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Tissue: Animal capImported.

Entry informationi

Entry nameiRGN_XENLA
AccessioniPrimary (citable) accession number: Q9I922
Secondary accession number(s): Q9IBA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.