ID RGN_XENTR Reviewed; 299 AA.
AC Q6DF62;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Regucalcin;
DE Short=RC;
DE AltName: Full=Gluconolactonase;
DE Short=GNL;
DE EC=3.1.1.17;
GN Name=rgn {ECO:0000312|EMBL:AAH76881.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH76881.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Gluconolactonase with low activity towards other sugar
CC lactones, including gulonolactone and galactonolactone. Catalyzes a key
CC step in ascorbic acid (vitamin C) biosynthesis. Can also hydrolyze
CC diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-
CC binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent
CC cellular processes and enzyme activities (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucono-1,5-lactone + H2O = D-gluconate + H(+);
CC Xref=Rhea:RHEA:10440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:18391; EC=3.1.1.17;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 divalent metal cation per subunit. Most active with Zn(2+)
CC and Mn(2+) ions. The physiological cofactor is most likely Ca(2+) or
CC Mg(2+). {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via UDP-alpha-
CC D-glucuronate pathway; L-ascorbate from UDP-alpha-D-glucuronate: step
CC 3/4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q03336}.
CC -!- SIMILARITY: Belongs to the SMP-30/CGR1 family.
CC {ECO:0000250|UniProtKB:Q03336}.
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DR EMBL; BC076881; AAH76881.1; -; mRNA.
DR RefSeq; NP_001006822.1; NM_001006821.1.
DR RefSeq; XP_012812212.1; XM_012956758.2.
DR AlphaFoldDB; Q6DF62; -.
DR SMR; Q6DF62; -.
DR PaxDb; 8364-ENSXETP00000008925; -.
DR DNASU; 448549; -.
DR Ensembl; ENSXETT00000097085; ENSXETP00000064976; ENSXETG00000004129.
DR GeneID; 448549; -.
DR KEGG; xtr:448549; -.
DR AGR; Xenbase:XB-GENE-483637; -.
DR CTD; 9104; -.
DR Xenbase; XB-GENE-483637; rgn.
DR eggNOG; KOG4499; Eukaryota.
DR HOGENOM; CLU_036110_3_2_1; -.
DR InParanoid; Q6DF62; -.
DR OMA; WAGTMRY; -.
DR OrthoDB; 3091635at2759; -.
DR PhylomeDB; Q6DF62; -.
DR TreeFam; TF323663; -.
DR UniPathway; UPA00991; UER00938.
DR Proteomes; UP000008143; Chromosome 2.
DR Bgee; ENSXETG00000004129; Expressed in mesonephros and 15 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0004341; F:gluconolactonase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008367; Regucalcin.
DR InterPro; IPR013658; SGL.
DR InterPro; IPR005511; SMP-30.
DR PANTHER; PTHR10907; REGUCALCIN; 1.
DR PANTHER; PTHR10907:SF47; REGUCALCIN; 1.
DR Pfam; PF08450; SGL; 1.
DR PRINTS; PR01791; REGUCALCIN.
DR PRINTS; PR01790; SMP30FAMILY.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE 2: Evidence at transcript level;
KW Ascorbate biosynthesis; Calcium; Cytoplasm; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..299
FT /note="Regucalcin"
FT /id="PRO_0000287687"
FT ACT_SITE 204
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 299 AA; 33079 MW; 342707A744622104 CRC64;
MSSIKIECVV SETYKIGESP VWEEKDGTLL FVDITGQKVC RWDPGTKKVQ SVSLEAPVGS
VVLRKSGGYV MAMGNTFSAL NWQDQSVTTL TCVDEDKPNN RFNDGKVDPE GRFLAGTMSQ
EIRPAVVERN QGSLFTLYPD HSVVKHFDMV DISNGLDWSL DHKTLYYIDS LSFKVDALDY
DMKTGKSSNR RTLYKLQQDE GIPDGMCIDA EGKLWVACYN GGRVIRIDPE TGKQIQTVKL
PVDKTTSCCF GGPDYSEMYV TSACEGMDEE WKKRQPQSGG IYKITGLGVK GIAPTAFAG
//
