RGN_HUMAN
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 03-AUG-2022, entry version 169.
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; Q15493; -.
DR PeptideAtlas; Q15493; -.
DR PRIDE; Q15493; -.
DR ProteomicsDB; 60611; -. [Q15493-1]
DR ProteomicsDB; 60612; -. [Q15493-2]
DR Antibodypedia; 25260; 189 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 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; AGTMRYD; -.
DR OrthoDB; 1343872at2759; -.
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 701 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 169 other tissues.
DR ExpressionAtlas; Q15493; baseline and differential.
DR Genevisible; Q15493; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006874; P:cellular 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:1903611; P:negative regulation of calcium-dependent ATPase activity; IEA:Ensembl.
DR GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; 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:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:1903634; P:negative regulation of leucine-tRNA ligase activity; IEA:Ensembl.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; 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:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:1903629; P:positive regulation of dUTP diphosphatase activity; IEA:Ensembl.
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:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; IEA:Ensembl.
DR GO; GO:1903052; P:positive regulation of proteolysis involved in protein catabolic process; IEA:Ensembl.
DR GO; GO:1901671; P:positive regulation of superoxide dismutase activity; 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; -; 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 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
