RGN_RABIT
ID RGN_RABIT Reviewed; 299 AA.
AC Q9TTJ6;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Regucalcin;
DE Short=RC;
DE AltName: Full=Gluconolactonase;
DE Short=GNL;
DE EC=3.1.1.17;
DE AltName: Full=Senescence marker protein 30;
DE Short=SMP-30;
GN Name=RGN; Synonyms=SMP30;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10891565; DOI=10.3892/ijmm.6.2.191;
RA Misawa H., Yamaguchi M.;
RT "The gene of Ca2+-binding protein regucalcin is highly conserved in
RT vertebrate species.";
RL Int. J. Mol. Med. 6:191-196(2000).
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
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DR EMBL; AB035445; BAA88079.1; -; mRNA.
DR RefSeq; NP_001075472.1; NM_001082003.1.
DR RefSeq; XP_008270558.1; XM_008272336.2.
DR AlphaFoldDB; Q9TTJ6; -.
DR SMR; Q9TTJ6; -.
DR STRING; 9986.ENSOCUP00000022189; -.
DR Ensembl; ENSOCUT00000028528; ENSOCUP00000022189; ENSOCUG00000023725.
DR GeneID; 100008619; -.
DR KEGG; ocu:100008619; -.
DR CTD; 9104; -.
DR eggNOG; KOG4499; Eukaryota.
DR GeneTree; ENSGT00390000014995; -.
DR HOGENOM; CLU_036110_3_2_1; -.
DR InParanoid; Q9TTJ6; -.
DR OMA; QKIWAFD; -.
DR OrthoDB; 1343872at2759; -.
DR TreeFam; TF323663; -.
DR UniPathway; UPA00991; UER00938.
DR Proteomes; UP000001811; Chromosome X.
DR Bgee; ENSOCUG00000023725; Expressed in liver and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
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:0019853; P:L-ascorbic acid biosynthetic process; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008367; Regucalcin.
DR InterPro; IPR013658; SGL.
DR InterPro; IPR005511; SMP-30.
DR Pfam; PF08450; SGL; 1.
DR PRINTS; PR01791; REGUCALCIN.
DR PRINTS; PR01790; SMP30FAMILY.
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_0000173048"
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"
FT MOD_RES 144
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64374"
FT MOD_RES 244
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64374"
FT MOD_RES 253
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64374"
SQ SEQUENCE 299 AA; 33109 MW; A8F94AD6596A0C68 CRC64;
MSSIKIECVL PENCHCGESP VWEEASGSLL FVDIPGKKFC RWNPLTKAVQ RMTMDAPVTS
VALRKSGGYV ATVGTKFCAL NLEDQSVVAL ATVDKDKKNN RFNDGKVDPA GRYFAGTMAE
ETAPAVLERH QGSLYALFPD HQVKKYFDQV DISNGLDWSL DHKIFYYIDS LAYSVDAFDY
DLQTGQISNR RSIYKLEKEE QIPDGMCIDT EGKLWVACYN GGRVIRLDPE TGKRLQTVKL
PVDKTTSCCF GGKDYSEMYV TCARDGLDPD SLSRQPEAGG IFKITGLGVK GIPPYSYAG
