RGN_MOUSE
ID RGN_MOUSE Reviewed; 299 AA.
AC Q64374; A2AFC8; Q3UJG3; Q60944;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=8765750; DOI=10.1016/0167-4781(96)00064-4;
RA Fujita T., Shirasawa T., Maruyama N.;
RT "Isolation and characterization of genomic and cDNA clones encoding mouse
RT senescence marker protein-30 (SMP30).";
RL Biochim. Biophys. Acta 1308:49-57(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Liver;
RX PubMed=9278263; DOI=10.1023/a:1006887929369;
RA Murata T., Yamaguchi M.;
RT "Molecular cloning of the cDNA coding for regucalcin and its mRNA
RT expression in mouse liver: the expression is stimulated by calcium
RT administration.";
RL Mol. Cell. Biochem. 173:127-133(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=14975739; DOI=10.1016/j.bbrc.2004.01.091;
RA Ishigami A., Kondo Y., Nanba R., Ohsawa T., Handa S., Kubo S., Akita M.,
RA Maruyama N.;
RT "SMP30 deficiency in mice causes an accumulation of neutral lipids and
RT phospholipids in the liver and shortens the life span.";
RL Biochem. Biophys. Res. Commun. 315:575-580(2004).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
RX PubMed=16585534; DOI=10.1073/pnas.0511225103;
RA Kondo Y., Inai Y., Sato Y., Handa S., Kubo S., Shimokado K., Goto S.,
RA Nishikimi M., Maruyama N., Ishigami A.;
RT "Senescence marker protein 30 functions as gluconolactonase in L-ascorbic
RT acid biosynthesis, and its knockout mice are prone to scurvy.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5723-5728(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-144; LYS-244 AND LYS-253, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS,
RP CATALYTIC ACTIVITY, FUNCTION, PATHWAY, COFACTOR, ACTIVE SITE, AND 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. Catalyzes a key
CC step in ascorbic acid (vitamin C) biosynthesis. Can also hydrolyze
CC diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-
CC binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent
CC cellular processes and enzyme activities (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16585534, ECO:0000269|PubMed:23349732}.
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:23349732};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via UDP-alpha-
CC D-glucuronate pathway; L-ascorbate from UDP-alpha-D-glucuronate: step
CC 3/4. {ECO:0000269|PubMed:16585534, ECO:0000269|PubMed:23349732}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23349732}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Mainly present in the liver. Weak expression was
CC found in the brain, lung and kidney. {ECO:0000269|PubMed:8765750,
CC ECO:0000269|PubMed:9278263}.
CC -!- DEVELOPMENTAL STAGE: Protein amounts in liver decrease significantly
CC with age.
CC -!- INDUCTION: By calcium. {ECO:0000269|PubMed:9278263}.
CC -!- DISRUPTION PHENOTYPE: Mice do not thrive after weaning when kept on a
CC vitamin C-less diet. They develop scurvy, have reduced bone mineral
CC density and brittle bones. Hepatocytes exhibit accumulation of lipid
CC droplets. Mice display increased mortality after about 3 months, and
CC their life span is shorter than normal. {ECO:0000269|PubMed:14975739,
CC ECO:0000269|PubMed:16585534}.
CC -!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
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DR EMBL; U28937; AAC52721.1; -; mRNA.
DR EMBL; U32170; AAD03478.1; -; Genomic_DNA.
DR EMBL; D86217; BAA13046.1; -; mRNA.
DR EMBL; AK146465; BAE27192.1; -; mRNA.
DR EMBL; AL672073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012710; AAH12710.1; -; mRNA.
DR CCDS; CCDS30043.1; -.
DR PIR; S72173; S72173.
DR RefSeq; NP_033086.1; NM_009060.2.
DR RefSeq; XP_006527635.1; XM_006527572.3.
DR PDB; 4GN7; X-ray; 1.95 A; A/B=1-299.
DR PDB; 4GN8; X-ray; 1.70 A; A/B=1-299.
DR PDB; 4GN9; X-ray; 2.00 A; A/B=1-299.
DR PDB; 4GNA; X-ray; 1.85 A; A/B=1-299.
DR PDBsum; 4GN7; -.
DR PDBsum; 4GN8; -.
DR PDBsum; 4GN9; -.
DR PDBsum; 4GNA; -.
DR AlphaFoldDB; Q64374; -.
DR SMR; Q64374; -.
DR STRING; 10090.ENSMUSP00000023832; -.
DR iPTMnet; Q64374; -.
DR PhosphoSitePlus; Q64374; -.
DR SwissPalm; Q64374; -.
DR REPRODUCTION-2DPAGE; Q64374; -.
DR SWISS-2DPAGE; Q64374; -.
DR CPTAC; non-CPTAC-3998; -.
DR EPD; Q64374; -.
DR jPOST; Q64374; -.
DR MaxQB; Q64374; -.
DR PaxDb; Q64374; -.
DR PeptideAtlas; Q64374; -.
DR PRIDE; Q64374; -.
DR ProteomicsDB; 254932; -.
DR Antibodypedia; 25260; 189 antibodies from 27 providers.
DR DNASU; 19733; -.
DR Ensembl; ENSMUST00000023832; ENSMUSP00000023832; ENSMUSG00000023070.
DR GeneID; 19733; -.
DR KEGG; mmu:19733; -.
DR UCSC; uc009std.1; mouse.
DR CTD; 9104; -.
DR MGI; MGI:108024; Rgn.
DR VEuPathDB; HostDB:ENSMUSG00000023070; -.
DR eggNOG; KOG4499; Eukaryota.
DR GeneTree; ENSGT00390000014995; -.
DR HOGENOM; CLU_036110_3_2_1; -.
DR InParanoid; Q64374; -.
DR OMA; AGTMRYD; -.
DR OrthoDB; 1343872at2759; -.
DR PhylomeDB; Q64374; -.
DR TreeFam; TF323663; -.
DR BRENDA; 3.1.1.17; 3474.
DR UniPathway; UPA00991; UER00938.
DR BioGRID-ORCS; 19733; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Rgn; mouse.
DR PRO; PR:Q64374; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q64374; protein.
DR Bgee; ENSMUSG00000023070; Expressed in left lobe of liver and 89 other tissues.
DR Genevisible; Q64374; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS: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; ISS: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; IDA:UniProtKB.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:1903011; P:negative regulation of bone development; ISO:MGI.
DR GO; GO:1903611; P:negative regulation of calcium-dependent ATPase activity; ISO:MGI.
DR GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; ISO:MGI.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:1903625; P:negative regulation of DNA catabolic process; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:1901318; P:negative regulation of flagellated sperm motility; ISO:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
DR GO; GO:1903634; P:negative regulation of leucine-tRNA ligase activity; ISO:MGI.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:1902679; P:negative regulation of RNA biosynthetic process; ISO:MGI.
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; ISO:MGI.
DR GO; GO:1903629; P:positive regulation of dUTP diphosphatase activity; ISO:MGI.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0010907; P:positive regulation of glucose metabolic process; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; ISO:MGI.
DR GO; GO:1903052; P:positive regulation of proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:1901671; P:positive regulation of superoxide dismutase activity; ISO:MGI.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISO:MGI.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISO:MGI.
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; Ascorbate biosynthesis; Calcium; Cytoplasm; Hydrolase;
KW Metal-binding; Reference proteome.
FT CHAIN 1..299
FT /note="Regucalcin"
FT /id="PRO_0000173047"
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 BINDING 101
FT /ligand="substrate"
FT BINDING 103
FT /ligand="substrate"
FT BINDING 121
FT /ligand="substrate"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 204
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT MOD_RES 144
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 244
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 253
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 201
FT /note="Q -> R (in Ref. 3; BAE27192)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="Q -> P (in Ref. 3; BAE27192)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 15..23
FT /evidence="ECO:0007829|PDB:4GN8"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4GN8"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4GN8"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:4GN8"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 143..158
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4GN8"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:4GN8"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:4GN8"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:4GN8"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4GN8"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:4GN8"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:4GN8"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:4GN8"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:4GN8"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:4GN8"
SQ SEQUENCE 299 AA; 33407 MW; DAD55EF618311977 CRC64;
MSSIKVECVL RENYRCGESP VWEEASQSLL FVDIPSKIIC RWDTVSNQVQ RVAVDAPVSS
VALRQLGGYV ATIGTKFCAL NWENQSVFVL AMVDEDKKNN RFNDGKVDPA GRYFAGTMAE
ETAPAVLERH QGSLYSLFPD HSVKKYFDQV DISNGLDWSL DHKIFYYIDS LSYTVDAFDY
DLQTGQISNR RIVYKMEKDE QIPDGMCIDA EGKLWVACYN GGRVIRLDPE TGKRLQTVKL
PVDKTTSCCF GGKDYSEMYV TCARDGLNAE GLLRQPDAGN IFKITGLGVK GIAPYSYAG
