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Regucalcin (RC) (Gluconolactonase) (GNL) (EC 3.1.1.17) (Senescence marker protein 30) (SMP-30)

 RGN_HUMAN               Reviewed;         299 AA.
Q15493; A4FTW1; A8K271; Q53FC9; Q5JRR5;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 142.
RecName: Full=Regucalcin;
Short=RC;
AltName: Full=Gluconolactonase;
Short=GNL;
EC=3.1.1.17;
AltName: Full=Senescence marker protein 30;
Short=SMP-30;
Name=RGN; Synonyms=SMP30;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=7548213; DOI=10.1016/0167-4781(95)00120-6;
Fujita T., Mandel J.-L., Shirasawa T., Hino O., Shirai T.,
Maruyama N.;
"Isolation of cDNA clone encoding human homologue of senescence marker
protein-30 (SMP30) and its location on the X chromosome.";
Biochim. Biophys. Acta 1263:249-252(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=10677570;
Misawa H., Yamaguchi M.;
"Transcript heterogeneity of the human gene for Ca2+-binding protein
regucalcin.";
Int. J. Mol. Med. 5:283-287(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon, and PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[8]
X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) IN COMPLEXES WITH CALCIUM AND
ZINC IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
COFACTOR, AND MUTAGENESIS OF GLU-18; ASN-103; ASN-154 AND ASP-204.
PubMed=20329768; DOI=10.1021/bi9022297;
Chakraborti S., Bahnson B.J.;
"Crystal structure of human senescence marker protein 30: insights
linking structural, enzymatic, and physiological functions.";
Biochemistry 49:3436-3444(2010).
[9]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH DIVALENT METAL
CATION AND SUBSTRATE ANALOG, CATALYTIC ACTIVITY, COFACTOR, ACTIVE
SITE, AND SUBUNIT.
PubMed=23349732; DOI=10.1371/journal.pone.0053706;
Aizawa S., Senda M., Harada A., Maruyama N., Ishida T., Aigaki T.,
Ishigami A., Senda T.;
"Structural basis of the gamma-lactone-ring formation in ascorbic acid
biosynthesis by the senescence marker protein-30/gluconolactonase.";
PLoS ONE 8:E53706-E53706(2013).
-!- FUNCTION: Gluconolactonase with low activity towards other sugar
lactones, including gulonolactone and galactonolactone. Can also
hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in
vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and
Ca(2+)-dependent cellular processes and enzyme activities (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: D-glucono-1,5-lactone + H(2)O = D-gluconate.
{ECO:0000269|PubMed:20329768, ECO:0000269|PubMed:23349732}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:20329768,
ECO:0000269|PubMed:23349732};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:20329768,
ECO:0000269|PubMed:23349732};
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:20329768,
ECO:0000269|PubMed:23349732};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:20329768,
ECO:0000269|PubMed:23349732};
Note=Binds 1 divalent metal cation per subunit. Most active with
Zn(2+) and Mn(2+) ions. The physiological cofactor is most likely
Ca(2+) or Mg(2+). {ECO:0000269|PubMed:20329768,
ECO:0000269|PubMed:23349732};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.7 mM for gluconolactone (with Zn(2+) as cofactor)
{ECO:0000269|PubMed:20329768};
KM=0.6 mM for gluconolactone (with Mn(2+) as cofactor)
{ECO:0000269|PubMed:20329768};
KM=1.3 mM for gluconolactone (with Mg(2+) as cofactor)
{ECO:0000269|PubMed:20329768};
KM=3.7 mM for gluconolactone (with Ca(2+) as cofactor)
{ECO:0000269|PubMed:20329768};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23349732}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15493-1; Sequence=Displayed;
Name=2;
IsoId=Q15493-2; Sequence=VSP_025456, VSP_025457;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
-!- CAUTION: Gluconolactonase catalyzes a key step in ascorbic acid
(vitamin C) biosynthesis, but primates lack the last enzyme in the
pathway and are unable to synthesize vitamin C. {ECO:0000305}.
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EMBL; D31815; BAA06602.1; -; mRNA.
EMBL; AB028125; BAA78693.1; -; mRNA.
EMBL; AB032064; BAA84082.1; -; mRNA.
EMBL; AK290136; BAF82825.1; -; mRNA.
EMBL; AK223360; BAD97080.1; -; mRNA.
EMBL; AL513366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC050371; AAH50371.1; -; mRNA.
EMBL; BC073173; AAH73173.1; -; mRNA.
CCDS; CCDS14272.1; -. [Q15493-1]
CCDS; CCDS75968.1; -. [Q15493-2]
PIR; S60035; S60035.
RefSeq; NP_001269777.1; NM_001282848.1.
RefSeq; NP_001269778.1; NM_001282849.1. [Q15493-2]
RefSeq; NP_004674.1; NM_004683.5. [Q15493-1]
RefSeq; NP_690608.1; NM_152869.3. [Q15493-1]
RefSeq; XP_006724630.1; XM_006724567.2. [Q15493-2]
UniGene; Hs.77854; -.
PDB; 3G4E; X-ray; 1.42 A; A/B=3-299.
PDB; 3G4H; X-ray; 1.92 A; A/B=3-299.
PDB; 4GNB; X-ray; 1.50 A; A/B=1-299.
PDB; 4GNC; X-ray; 1.75 A; A/B=1-299.
PDBsum; 3G4E; -.
PDBsum; 3G4H; -.
PDBsum; 4GNB; -.
PDBsum; 4GNC; -.
ProteinModelPortal; Q15493; -.
SMR; Q15493; -.
BioGrid; 114557; 7.
STRING; 9606.ENSP00000253303; -.
iPTMnet; Q15493; -.
PhosphoSitePlus; Q15493; -.
BioMuta; RGN; -.
DMDM; 3334328; -.
PaxDb; Q15493; -.
PeptideAtlas; Q15493; -.
PRIDE; Q15493; -.
DNASU; 9104; -.
Ensembl; ENST00000336169; ENSP00000338400; ENSG00000130988. [Q15493-1]
Ensembl; ENST00000352078; ENSP00000253303; ENSG00000130988. [Q15493-1]
Ensembl; ENST00000397180; ENSP00000380365; ENSG00000130988. [Q15493-1]
Ensembl; ENST00000457380; ENSP00000406568; ENSG00000130988. [Q15493-2]
GeneID; 9104; -.
KEGG; hsa:9104; -.
UCSC; uc010nhp.2; human. [Q15493-1]
CTD; 9104; -.
DisGeNET; 9104; -.
EuPathDB; HostDB:ENSG00000130988.12; -.
GeneCards; RGN; -.
HGNC; HGNC:9989; RGN.
HPA; HPA029102; -.
HPA; HPA029103; -.
MIM; 300212; gene.
neXtProt; NX_Q15493; -.
OpenTargets; ENSG00000130988; -.
PharmGKB; PA34359; -.
eggNOG; KOG4499; Eukaryota.
eggNOG; COG3386; LUCA.
GeneTree; ENSGT00390000014995; -.
HOGENOM; HOG000220627; -.
HOVERGEN; HBG004347; -.
InParanoid; Q15493; -.
KO; K01053; -.
OMA; CRWDSLT; -.
OrthoDB; EOG091G131G; -.
PhylomeDB; Q15493; -.
TreeFam; TF323663; -.
ChiTaRS; RGN; human.
EvolutionaryTrace; Q15493; -.
GeneWiki; RGN_(gene); -.
GenomeRNAi; 9104; -.
PRO; PR:Q15493; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000130988; -.
CleanEx; HS_RGN; -.
ExpressionAtlas; Q15493; baseline and differential.
Genevisible; Q15493; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; IBA:GO_Central.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
GO; GO:0004341; F:gluconolactonase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IBA:GO_Central.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:1903011; P:negative regulation of bone development; IEA:Ensembl.
GO; GO:1903611; P:negative regulation of calcium-dependent ATPase activity; IEA:Ensembl.
GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:1903625; P:negative regulation of DNA catabolic process; IEA:Ensembl.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:1901318; P:negative regulation of flagellated sperm motility; IEA:Ensembl.
GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
GO; GO:1903634; P:negative regulation of leucine-tRNA ligase activity; IEA:Ensembl.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
GO; GO:1902679; P:negative regulation of RNA biosynthetic process; IEA:Ensembl.
GO; GO:0032781; P:positive regulation of ATPase activity; ISS:UniProtKB.
GO; GO:1901896; P:positive regulation of calcium-transporting ATPase activity; IEA:Ensembl.
GO; GO:1903629; P:positive regulation of dUTP diphosphatase activity; IEA:Ensembl.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
GO; GO:0010907; P:positive regulation of glucose metabolic process; IEA:Ensembl.
GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
GO; GO:0010922; P:positive regulation of phosphatase activity; IEA:Ensembl.
GO; GO:1903052; P:positive regulation of proteolysis involved in cellular protein catabolic process; IEA:Ensembl.
GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IEA:Ensembl.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Ensembl.
GO; GO:0050848; P:regulation of calcium-mediated signaling; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
Gene3D; 2.120.10.30; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR008367; Regucalcin.
InterPro; IPR013658; SGL.
InterPro; IPR005511; SMP-30.
Pfam; PF08450; SGL; 1.
PRINTS; PR01791; REGUCALCIN.
PRINTS; PR01790; SMP30FAMILY.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
CHAIN 1 299 Regucalcin.
/FTId=PRO_0000173046.
ACT_SITE 204 204 Proton donor/acceptor.
{ECO:0000305|PubMed:23349732}.
METAL 18 18 Divalent metal cation.
{ECO:0000269|PubMed:23349732}.
METAL 154 154 Divalent metal cation.
{ECO:0000269|PubMed:23349732}.
METAL 204 204 Divalent metal cation.
{ECO:0000269|PubMed:23349732}.
BINDING 101 101 Substrate.
BINDING 103 103 Substrate.
BINDING 121 121 Substrate. {ECO:0000250}.
MOD_RES 144 144 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q64374}.
MOD_RES 244 244 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q64374}.
MOD_RES 253 253 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q64374}.
VAR_SEQ 116 187 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_025456.
VAR_SEQ 188 188 S -> A (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_025457.
MUTAGEN 18 18 E->A: Reduces enzyme activity by about
90%. {ECO:0000269|PubMed:20329768}.
MUTAGEN 103 103 N->A: Reduces enzyme activity by about
95%. {ECO:0000269|PubMed:20329768}.
MUTAGEN 154 154 N->A: Reduces enzyme activity by about
95%. {ECO:0000269|PubMed:20329768}.
MUTAGEN 204 204 D->A: Reduces enzyme activity by over
98%. {ECO:0000269|PubMed:20329768}.
CONFLICT 292 293 IA -> TS (in Ref. 4; BAD97080).
{ECO:0000305}.
STRAND 5 10 {ECO:0000244|PDB:3G4E}.
STRAND 15 23 {ECO:0000244|PDB:3G4E}.
TURN 24 27 {ECO:0000244|PDB:3G4E}.
STRAND 28 33 {ECO:0000244|PDB:3G4E}.
TURN 34 37 {ECO:0000244|PDB:3G4E}.
STRAND 38 43 {ECO:0000244|PDB:3G4E}.
TURN 44 46 {ECO:0000244|PDB:3G4E}.
STRAND 49 53 {ECO:0000244|PDB:3G4E}.
STRAND 58 64 {ECO:0000244|PDB:3G4E}.
STRAND 67 73 {ECO:0000244|PDB:3G4E}.
STRAND 76 81 {ECO:0000244|PDB:3G4E}.
TURN 82 85 {ECO:0000244|PDB:3G4E}.
STRAND 86 92 {ECO:0000244|PDB:3G4E}.
STRAND 98 107 {ECO:0000244|PDB:3G4E}.
STRAND 113 119 {ECO:0000244|PDB:3G4E}.
STRAND 132 137 {ECO:0000244|PDB:3G4E}.
STRAND 143 158 {ECO:0000244|PDB:3G4E}.
STRAND 164 169 {ECO:0000244|PDB:3G4E}.
HELIX 170 172 {ECO:0000244|PDB:3G4E}.
STRAND 174 180 {ECO:0000244|PDB:3G4E}.
TURN 182 184 {ECO:0000244|PDB:3G4E}.
STRAND 187 195 {ECO:0000244|PDB:3G4E}.
HELIX 198 200 {ECO:0000244|PDB:3G4E}.
STRAND 202 209 {ECO:0000244|PDB:3G4E}.
STRAND 214 219 {ECO:0000244|PDB:3G4E}.
TURN 220 222 {ECO:0000244|PDB:4GNB}.
STRAND 223 227 {ECO:0000244|PDB:3G4E}.
TURN 229 231 {ECO:0000244|PDB:3G4E}.
STRAND 234 239 {ECO:0000244|PDB:3G4E}.
STRAND 241 243 {ECO:0000244|PDB:3G4E}.
STRAND 245 252 {ECO:0000244|PDB:3G4E}.
HELIX 253 255 {ECO:0000244|PDB:3G4E}.
STRAND 257 263 {ECO:0000244|PDB:3G4E}.
HELIX 269 274 {ECO:0000244|PDB:3G4E}.
TURN 276 279 {ECO:0000244|PDB:3G4E}.
STRAND 281 285 {ECO:0000244|PDB:3G4E}.
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


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