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Database: UniProt
Entry: M3ZV87_XIPMA
LinkDB: M3ZV87_XIPMA
Original site: M3ZV87_XIPMA 
ID   M3ZV87_XIPMA            Unreviewed;       298 AA.
AC   M3ZV87;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Regucalcin {ECO:0000256|ARBA:ARBA00016808};
DE            EC=3.1.1.17 {ECO:0000256|ARBA:ARBA00013227};
DE   AltName: Full=Gluconolactonase {ECO:0000256|ARBA:ARBA00032464};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000006130.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000006130.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000006130.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00001589};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the SMP-30/CGR1 family.
CC       {ECO:0000256|ARBA:ARBA00008853}.
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DR   AlphaFoldDB; M3ZV87; -.
DR   STRING; 8083.ENSXMAP00000006130; -.
DR   Ensembl; ENSXMAT00000006136.2; ENSXMAP00000006130.2; ENSXMAG00000006115.2.
DR   eggNOG; KOG4499; Eukaryota.
DR   GeneTree; ENSGT00390000014995; -.
DR   HOGENOM; CLU_036110_3_2_1; -.
DR   InParanoid; M3ZV87; -.
DR   OMA; WAGTMRY; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0004341; F:gluconolactonase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT   DOMAIN          16..262
FT                   /note="SMP-30/Gluconolactonase/LRE-like region"
FT                   /evidence="ECO:0000259|Pfam:PF08450"
SQ   SEQUENCE   298 AA;  31945 MW;  AD4660DD9900F5BF CRC64;
     MSSVKVESVV KEHAQIGEGP VWEESEQTLL FIDITGQKIH RWNAATNQIQ SLQTADTVGF
     AVPRRSGGYV AGVGCSIVAV DWSTQKVTSL ASVEDDKPEN RLNDGKADPM GRLLAGTAHL
     RDAQTAQVKP GSLYLMKSDL SVTKLLGQVD ISNGMDWTAD LKTLFYIDSL AMSVDAFDYD
     SASGNLGNRR VVYRLEEGEG VPDGMTLDAN DRLWVACYNG GRVLNIDPAT GKRLQTVSLP
     ATKTTSCCFG GPDYSDLYVT SASLGLDQSE LQKQPAAGNT FRVTGLGVKG RPSNAFSG
//
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