ID   RGN_HUMAN               Reviewed;         299 AA.
AC   Q15493; A4FTW1; A8K271; Q53FC9; Q5JRR5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 178.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=7548213; DOI=10.1016/0167-4781(95)00120-6;
RA   Fujita T., Mandel J.-L., Shirasawa T., Hino O., Shirai T., Maruyama N.;
RT   "Isolation of cDNA clone encoding human homologue of senescence marker
RT   protein-30 (SMP30) and its location on the X chromosome.";
RL   Biochim. Biophys. Acta 1263:249-252(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=10677570;
RA   Misawa H., Yamaguchi M.;
RT   "Transcript heterogeneity of the human gene for Ca2+-binding protein
RT   regucalcin.";
RL   Int. J. Mol. Med. 5:283-287(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Colon, and PNS;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) IN COMPLEXES WITH CALCIUM AND ZINC
RP   IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP   MUTAGENESIS OF GLU-18; ASN-103; ASN-154 AND ASP-204.
RX   PubMed=20329768; DOI=10.1021/bi9022297;
RA   Chakraborti S., Bahnson B.J.;
RT   "Crystal structure of human senescence marker protein 30: insights linking
RT   structural, enzymatic, and physiological functions.";
RL   Biochemistry 49:3436-3444(2010).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH DIVALENT METAL CATION
RP   AND SUBSTRATE ANALOG, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, AND
RP   SUBUNIT.
RX   PubMed=23349732; DOI=10.1371/journal.pone.0053706;
RA   Aizawa S., Senda M., Harada A., Maruyama N., Ishida T., Aigaki T.,
RA   Ishigami A., Senda T.;
RT   "Structural basis of the gamma-lactone-ring formation in ascorbic acid
RT   biosynthesis by the senescence marker protein-30/gluconolactonase.";
RL   PLoS ONE 8:E53706-E53706(2013).
CC   -!- FUNCTION: Gluconolactonase with low activity towards other sugar
CC       lactones, including gulonolactone and galactonolactone. Can also
CC       hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro).
CC       Calcium-binding protein. Modulates Ca(2+) signaling, and Ca(2+)-
CC       dependent 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         Evidence={ECO:0000269|PubMed:20329768, ECO:0000269|PubMed:23349732};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:20329768, ECO:0000269|PubMed:23349732};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:20329768, ECO:0000269|PubMed:23349732};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:20329768, ECO:0000269|PubMed:23349732};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:20329768, ECO:0000269|PubMed:23349732};
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:0000269|PubMed:20329768, ECO:0000269|PubMed:23349732};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.7 mM for gluconolactone (with Zn(2+) as cofactor)
CC         {ECO:0000269|PubMed:20329768};
CC         KM=0.6 mM for gluconolactone (with Mn(2+) as cofactor)
CC         {ECO:0000269|PubMed:20329768};
CC         KM=1.3 mM for gluconolactone (with Mg(2+) as cofactor)
CC         {ECO:0000269|PubMed:20329768};
CC         KM=3.7 mM for gluconolactone (with Ca(2+) as cofactor)
CC         {ECO:0000269|PubMed:20329768};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23349732}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q15493-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15493-2; Sequence=VSP_025456, VSP_025457;
CC   -!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
CC   -!- CAUTION: Gluconolactonase catalyzes a key step in ascorbic acid
CC       (vitamin C) biosynthesis, but primates lack the last enzyme in the
CC       pathway and are unable to synthesize vitamin C. {ECO:0000305}.
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DR   EMBL; D31815; BAA06602.1; -; mRNA.
DR   EMBL; AB028125; BAA78693.1; -; mRNA.
DR   EMBL; AB032064; BAA84082.1; -; mRNA.
DR   EMBL; AK290136; BAF82825.1; -; mRNA.
DR   EMBL; AK223360; BAD97080.1; -; mRNA.
DR   EMBL; AL513366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC050371; AAH50371.1; -; mRNA.
DR   EMBL; BC073173; AAH73173.1; -; mRNA.
DR   CCDS; CCDS14272.1; -. [Q15493-1]
DR   CCDS; CCDS75968.1; -. [Q15493-2]
DR   PIR; S60035; S60035.
DR   RefSeq; NP_001269777.1; NM_001282848.1.
DR   RefSeq; NP_001269778.1; NM_001282849.1. [Q15493-2]
DR   RefSeq; NP_004674.1; NM_004683.5. [Q15493-1]
DR   RefSeq; NP_690608.1; NM_152869.3. [Q15493-1]
DR   RefSeq; XP_006724630.1; XM_006724567.2. [Q15493-2]
DR   PDB; 3G4E; X-ray; 1.42 A; A/B=3-299.
DR   PDB; 3G4H; X-ray; 1.92 A; A/B=3-299.
DR   PDB; 4GNB; X-ray; 1.50 A; A/B=1-299.
DR   PDB; 4GNC; X-ray; 1.75 A; A/B=1-299.
DR   PDBsum; 3G4E; -.
DR   PDBsum; 3G4H; -.
DR   PDBsum; 4GNB; -.
DR   PDBsum; 4GNC; -.
DR   AlphaFoldDB; Q15493; -.
DR   SMR; Q15493; -.
DR   BioGRID; 114557; 9.
DR   IntAct; Q15493; 2.
DR   STRING; 9606.ENSP00000380365; -.
DR   DrugBank; DB11093; Calcium citrate.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   iPTMnet; Q15493; -.
DR   PhosphoSitePlus; Q15493; -.
DR   BioMuta; RGN; -.
DR   DMDM; 3334328; -.
DR   MassIVE; Q15493; -.
DR   MaxQB; Q15493; -.
DR   PaxDb; 9606-ENSP00000380365; -.
DR   PeptideAtlas; Q15493; -.
DR   ProteomicsDB; 60611; -. [Q15493-1]
DR   ProteomicsDB; 60612; -. [Q15493-2]
DR   Antibodypedia; 25260; 200 antibodies from 27 providers.
DR   DNASU; 9104; -.
DR   Ensembl; ENST00000336169.3; ENSP00000338400.3; ENSG00000130988.13. [Q15493-1]
DR   Ensembl; ENST00000352078.8; ENSP00000253303.4; ENSG00000130988.13. [Q15493-1]
DR   Ensembl; ENST00000397180.6; ENSP00000380365.1; ENSG00000130988.13. [Q15493-1]
DR   Ensembl; ENST00000457380.5; ENSP00000406568.1; ENSG00000130988.13. [Q15493-2]
DR   GeneID; 9104; -.
DR   KEGG; hsa:9104; -.
DR   MANE-Select; ENST00000397180.6; ENSP00000380365.1; NM_152869.4; NP_690608.1.
DR   UCSC; uc010nhp.2; human. [Q15493-1]
DR   AGR; HGNC:9989; -.
DR   CTD; 9104; -.
DR   DisGeNET; 9104; -.
DR   GeneCards; RGN; -.
DR   HGNC; HGNC:9989; RGN.
DR   HPA; ENSG00000130988; Group enriched (adrenal gland, liver).
DR   MIM; 300212; gene.
DR   neXtProt; NX_Q15493; -.
DR   OpenTargets; ENSG00000130988; -.
DR   PharmGKB; PA34359; -.
DR   VEuPathDB; HostDB:ENSG00000130988; -.
DR   eggNOG; KOG4499; Eukaryota.
DR   GeneTree; ENSGT00390000014995; -.
DR   HOGENOM; CLU_036110_3_2_1; -.
DR   InParanoid; Q15493; -.
DR   OMA; WAGTMRY; -.
DR   OrthoDB; 3091635at2759; -.
DR   PhylomeDB; Q15493; -.
DR   TreeFam; TF323663; -.
DR   BRENDA; 3.1.1.17; 2681.
DR   PathwayCommons; Q15493; -.
DR   SignaLink; Q15493; -.
DR   BioGRID-ORCS; 9104; 11 hits in 775 CRISPR screens.
DR   ChiTaRS; RGN; human.
DR   EvolutionaryTrace; Q15493; -.
DR   GeneWiki; RGN_(gene); -.
DR   GenomeRNAi; 9104; -.
DR   Pharos; Q15493; Tbio.
DR   PRO; PR:Q15493; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q15493; Protein.
DR   Bgee; ENSG00000130988; Expressed in right adrenal gland cortex and 170 other cell types or tissues.
DR   ExpressionAtlas; Q15493; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0004341; F:gluconolactonase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:1903011; P:negative regulation of bone development; IEA:Ensembl.
DR   GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IEA:Ensembl.
DR   GO; GO:1903625; P:negative regulation of DNA catabolic process; IEA:Ensembl.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:1901318; P:negative regulation of flagellated sperm motility; IEA:Ensembl.
DR   GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:1902679; P:negative regulation of RNA biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR   GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010907; P:positive regulation of glucose metabolic process; IEA:Ensembl.
DR   GO; GO:1903052; P:positive regulation of proteolysis involved in protein catabolic process; IEA:Ensembl.
DR   GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Ensembl.
DR   GO; GO:0050848; P:regulation of calcium-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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:SF54; REGUCALCIN; 1.
DR   Pfam; PF08450; SGL; 1.
DR   PRINTS; PR01791; REGUCALCIN.
DR   PRINTS; PR01790; SMP30FAMILY.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   Genevisible; Q15493; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cytoplasm; Hydrolase;
KW   Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..299
FT                   /note="Regucalcin"
FT                   /id="PRO_0000173046"
FT   ACT_SITE        204
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000305|PubMed:23349732"
FT   BINDING         18
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000269|PubMed:23349732"
FT   BINDING         101
FT                   /ligand="substrate"
FT   BINDING         103
FT                   /ligand="substrate"
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:0000269|PubMed:23349732"
FT   BINDING         204
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000269|PubMed:23349732"
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"
FT   VAR_SEQ         116..187
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025456"
FT   VAR_SEQ         188
FT                   /note="S -> A (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025457"
FT   MUTAGEN         18
FT                   /note="E->A: Reduces enzyme activity by about 90%."
FT                   /evidence="ECO:0000269|PubMed:20329768"
FT   MUTAGEN         103
FT                   /note="N->A: Reduces enzyme activity by about 95%."
FT                   /evidence="ECO:0000269|PubMed:20329768"
FT   MUTAGEN         154
FT                   /note="N->A: Reduces enzyme activity by about 95%."
FT                   /evidence="ECO:0000269|PubMed:20329768"
FT   MUTAGEN         204
FT                   /note="D->A: Reduces enzyme activity by over 98%."
FT                   /evidence="ECO:0000269|PubMed:20329768"
FT   CONFLICT        292..293
FT                   /note="IA -> TS (in Ref. 4; BAD97080)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          15..23
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   TURN            24..27
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          28..33
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   TURN            34..37
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          58..64
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          67..73
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   TURN            82..85
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          86..92
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          98..107
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          113..119
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          143..158
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   HELIX           170..172
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          174..180
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   TURN            182..184
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          187..195
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          202..209
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          214..219
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   TURN            220..222
FT                   /evidence="ECO:0007829|PDB:4GNB"
FT   STRAND          223..227
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   TURN            229..231
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          234..239
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          241..243
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          245..252
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   HELIX           253..255
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          257..263
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   HELIX           269..274
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   TURN            276..279
FT                   /evidence="ECO:0007829|PDB:3G4E"
FT   STRAND          281..285
FT                   /evidence="ECO:0007829|PDB:3G4E"
SQ   SEQUENCE   299 AA;  33253 MW;  95BA1C73B7B77635 CRC64;
     MSSIKIECVL PENCRCGESP VWEEVSNSLL FVDIPAKKVC RWDSFTKQVQ RVTMDAPVSS
     VALRQSGGYV ATIGTKFCAL NWKEQSAVVL ATVDNDKKNN RFNDGKVDPA GRYFAGTMAE
     ETAPAVLERH QGALYSLFPD HHVKKYFDQV DISNGLDWSL DHKIFYYIDS LSYSVDAFDY
     DLQTGQISNR RSVYKLEKEE QIPDGMCIDA EGKLWVACYN GGRVIRLDPV TGKRLQTVKL
     PVDKTTSCCF GGKNYSEMYV TCARDGMDPE GLLRQPEAGG IFKITGLGVK GIAPYSYAG
//