RGN_DANRE
ID RGN_DANRE Reviewed; 295 AA.
AC Q6TLF6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, 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:0000250|UniProtKB:Q03336}; ORFNames=zgc:92078;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AAQ94576.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow {ECO:0000312|EMBL:AAQ94576.1};
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2] {ECO:0000312|EMBL:AAH75882.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) 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; AY394949; AAQ94576.1; -; mRNA.
DR EMBL; BC075882; AAH75882.1; -; mRNA.
DR RefSeq; NP_991309.1; NM_205746.1.
DR AlphaFoldDB; Q6TLF6; -.
DR SMR; Q6TLF6; -.
DR STRING; 7955.ENSDARP00000126252; -.
DR PaxDb; Q6TLF6; -.
DR DNASU; 403070; -.
DR Ensembl; ENSDART00000162588; ENSDARP00000130159; ENSDARG00000098645.
DR GeneID; 403070; -.
DR KEGG; dre:403070; -.
DR CTD; 9104; -.
DR ZFIN; ZDB-GENE-040718-68; rgn.
DR eggNOG; KOG4499; Eukaryota.
DR GeneTree; ENSGT00390000014995; -.
DR HOGENOM; CLU_036110_3_2_1; -.
DR InParanoid; Q6TLF6; -.
DR OMA; AGTMRYD; -.
DR OrthoDB; 1343872at2759; -.
DR PhylomeDB; Q6TLF6; -.
DR TreeFam; TF323663; -.
DR UniPathway; UPA00991; UER00938.
DR PRO; PR:Q6TLF6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000098645; Expressed in liver and 19 other 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:cellular 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; -; 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..295
FT /note="Regucalcin"
FT /id="PRO_0000287685"
FT ACT_SITE 200
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 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 295 AA; 32809 MW; 1FF5C6DD40D6B68D CRC64;
MSSIKVECVI KEKNEVGESP VWEEKDSSLL YVDITGQKVS RWSSLTKQIE SMNTEKLVGC
VVPRQAGGYV IAEGTRFAFV DWVKRSITAV AEVNEKPNTR FNDGKVDPAG RFFAGTMSMD
MKPDVVDAAL YNLQPDHSVV RHFDQVHLSN GLDWSLDHRV FYYIDSLAFM VEAFDYDIQT
GGLSNRRTVY KMEKDEGIPD GMCIDTEGKL WVACFNGGRV LRIDPQTGKR LQTVKLPAER
ITSCCFGGKD YSDLYITSAY IGMDAEALAK QPEAGCTFKV TGLGVKGIPP YSYTG
