ID A0A2T7NRR8_POMCA Unreviewed; 297 AA.
AC A0A2T7NRR8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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};
GN ORFNames=C0Q70_17145 {ECO:0000313|EMBL:PVD23871.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD23871.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD23871.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD23871.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD23871.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD23871.1}.
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DR EMBL; PZQS01000010; PVD23871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7NRR8; -.
DR STRING; 400727.A0A2T7NRR8; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg10.
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:UP000245119}.
FT DOMAIN 17..260
FT /note="SMP-30/Gluconolactonase/LRE-like region"
FT /evidence="ECO:0000259|Pfam:PF08450"
SQ SEQUENCE 297 AA; 32981 MW; F307B29A9994D2A6 CRC64;
MLSLRVEVAI RNGAKHLAEG PHWDDVTQTL LYVDLTGHEM SLLCPKLDDN VTFVIPRKQG
GLMVGLGRTI SQLNWSSHAV TKIVEVDQGT NNRFNDGKCD AKGRLWAGER LINPLVPAGG
NIFWWSLYSL DLHRTVRKQA TNFHLSNGLA WTDDNRTMFF VDSPVRKVYA FDFDLEGGNI
SKKRVAIDMA TAAPDIGGVP DGMNIDMEGK LWVAFYDGGV IGRFDPVTGK HLQTLKFPVT
QVTSMCWGGR NHDELYVTSG RQGHPEEYFV QKEPLAGSVF RVTGSGYKGR AAHVYEG
//