ID NUDT5_HUMAN Reviewed; 219 AA. AC Q9UKK9; A8K516; Q6IAG0; Q9UH49; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 11-NOV-2015, entry version 141. DE RecName: Full=ADP-sugar pyrophosphatase; DE EC=3.6.1.13; DE AltName: Full=8-oxo-dGDP phosphatase; DE EC=3.6.1.58; DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 5; DE Short=Nudix motif 5; DE AltName: Full=YSA1H; GN Name=NUDT5; ORFNames=HSPC115; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RX PubMed=10567213; DOI=10.1042/0264-6021:3440331; RA Gasmi L., Cartwright J.L., McLennan A.G.; RT "Cloning, expression and characterization of YSA1H, a human adenosine RT 5'-diphosphosugar pyrophosphatase possessing a MutT motif."; RL Biochem. J. 344:331-337(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RX PubMed=10722730; DOI=10.1074/jbc.275.12.8844; RA Yang H., Slupska M.M., Wei Y.-F., Tai J.H., Luther W.M., Xia Y.-R., RA Shih D.M., Chiang J.-H., Baikalov C., Fitz-Gibbon S., Phan I.T., RA Conrad A., Miller J.H.; RT "Cloning and characterization of a new member of the Nudix hydrolases RT from human and mouse."; RL J. Biol. Chem. 275:8844-8853(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-74, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-210 AND LYS-218, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., RA Fischer-Posovszky P., Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion RT profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-210 IN COMPLEX WITH AMP; RP MAGNESIUM IONS AND ADP-RIBOSE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, RP AND COFACTOR. RX PubMed=17052728; DOI=10.1016/j.jmb.2006.09.078; RA Zha M., Zhong C., Peng Y., Hu H., Ding J.; RT "Crystal structures of human NUDT5 reveal insights into the structural RT basis of the substrate specificity."; RL J. Mol. Biol. 364:1021-1033(2006). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-210 IN COMPLEX WITH AMPCPR RP AND MAGNESIUM IONS, COFACTOR, MUTAGENESIS OF TRP-28; TRP-46; ARG-51; RP ARG-84; LEU-98; GLU-112; GLU-116 AND GLU-166, AND SUBUNIT. RX PubMed=18462755; DOI=10.1016/j.jmb.2008.04.006; RA Zha M., Guo Q., Zhang Y., Yu B., Ou Y., Zhong C., Ding J.; RT "Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from RT structural and kinetic studies."; RL J. Mol. Biol. 379:568-578(2008). CC -!- FUNCTION: Hydrolyzes with similar activities ADP-ribose ADP- CC mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze CC other nucleotide sugars with low activity. Does not play a role in CC U8 snoRNA decapping activity. Binds U8 snoRNA. CC {ECO:0000269|PubMed:17052728}. CC -!- CATALYTIC ACTIVITY: ADP-D-ribose + H(2)O = AMP + D-ribose 5- CC phosphate. {ECO:0000269|PubMed:17052728}. CC -!- CATALYTIC ACTIVITY: ADP-sugar + H(2)O = AMP + alpha-D-aldose 5- CC phosphate. {ECO:0000269|PubMed:17052728}. CC -!- CATALYTIC ACTIVITY: 8-oxo-dGDP + H(2)O = 8-oxo-dGMP + phosphate. CC {ECO:0000269|PubMed:17052728}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:17052728, CC ECO:0000269|PubMed:18462755}; CC Note=Binds 3 Mg(2+) ions per subunit. CC {ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17052728, CC ECO:0000269|PubMed:18462755}. CC -!- TISSUE SPECIFICITY: Widely expressed. Most abundant in liver. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00794}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF155832; AAF06734.1; -; mRNA. DR EMBL; AF218818; AAF25479.1; -; mRNA. DR EMBL; AF161464; AAF29079.1; -; mRNA. DR EMBL; CR457195; CAG33476.1; -; mRNA. DR EMBL; AK291131; BAF83820.1; -; mRNA. DR EMBL; CH471072; EAW86322.1; -; Genomic_DNA. DR EMBL; BC000025; AAH00025.1; -; mRNA. DR CCDS; CCDS7089.1; -. DR RefSeq; NP_054861.2; NM_014142.2. DR UniGene; Hs.555956; -. DR UniGene; Hs.656304; -. DR PDB; 2DSB; X-ray; 2.50 A; A/B/C/D=1-219. DR PDB; 2DSC; X-ray; 2.00 A; A/B=1-210. DR PDB; 2DSD; X-ray; 2.60 A; A/B=1-210. DR PDB; 3AC9; X-ray; 2.10 A; A/B=14-208. DR PDB; 3ACA; X-ray; 2.05 A; A/B=13-208. DR PDB; 3BM4; X-ray; 2.00 A; A/B=1-210. DR PDB; 3L85; X-ray; 2.30 A; A/B=14-208. DR PDBsum; 2DSB; -. DR PDBsum; 2DSC; -. DR PDBsum; 2DSD; -. DR PDBsum; 3AC9; -. DR PDBsum; 3ACA; -. DR PDBsum; 3BM4; -. DR PDBsum; 3L85; -. DR ProteinModelPortal; Q9UKK9; -. DR SMR; Q9UKK9; 13-209. DR BioGrid; 116335; 13. DR IntAct; Q9UKK9; 7. DR MINT; MINT-1370495; -. DR STRING; 9606.ENSP00000419628; -. DR PhosphoSite; Q9UKK9; -. DR BioMuta; NUDT5; -. DR MaxQB; Q9UKK9; -. DR PaxDb; Q9UKK9; -. DR PRIDE; Q9UKK9; -. DR DNASU; 11164; -. DR Ensembl; ENST00000491614; ENSP00000419628; ENSG00000165609. DR Ensembl; ENST00000537776; ENSP00000445116; ENSG00000165609. DR GeneID; 11164; -. DR KEGG; hsa:11164; -. DR UCSC; uc001ilj.3; human. DR CTD; 11164; -. DR GeneCards; NUDT5; -. DR HGNC; HGNC:8052; NUDT5. DR HPA; HPA019827; -. DR MIM; 609230; gene. DR neXtProt; NX_Q9UKK9; -. DR PharmGKB; PA31838; -. DR eggNOG; KOG3041; Eukaryota. DR eggNOG; COG0494; LUCA. DR GeneTree; ENSGT00390000006280; -. DR HOGENOM; HOG000174302; -. DR HOVERGEN; HBG052691; -. DR InParanoid; Q9UKK9; -. DR KO; K13987; -. DR OrthoDB; EOG7CVPZW; -. DR PhylomeDB; Q9UKK9; -. DR TreeFam; TF106347; -. DR BRENDA; 3.6.1.13; 2681. DR BRENDA; 3.6.1.58; 2681. DR Reactome; R-HSA-2393930; Phosphate bond hydrolysis by NUDT proteins. DR SABIO-RK; Q9UKK9; -. DR ChiTaRS; NUDT5; human. DR EvolutionaryTrace; Q9UKK9; -. DR GeneWiki; NUDT5; -. DR GenomeRNAi; 11164; -. DR NextBio; 42475; -. DR PRO; PR:Q9UKK9; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; Q9UKK9; -. DR CleanEx; HS_NUDT5; -. DR ExpressionAtlas; Q9UKK9; baseline and differential. DR Genevisible; Q9UKK9; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005622; C:intracellular; NAS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; EXP:Reactome. DR GO; GO:0019144; F:ADP-sugar diphosphatase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IEA:Ensembl. DR GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB. DR GO; GO:0019303; P:D-ribose catabolic process; NAS:UniProtKB. DR GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; TAS:Reactome. DR GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome. DR GO; GO:0009117; P:nucleotide metabolic process; NAS:ProtInc. DR GO; GO:0009191; P:ribonucleoside diphosphate catabolic process; IDA:UniProtKB. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Hydrolase; Magnesium; KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; KW RNA-binding. FT CHAIN 1 219 ADP-sugar pyrophosphatase. FT /FTId=PRO_0000057048. FT DOMAIN 57 197 Nudix hydrolase. {ECO:0000255|PROSITE- FT ProRule:PRU00794}. FT REGION 46 47 Substrate binding; shared with dimeric FT partner. FT MOTIF 97 118 Nudix box. FT METAL 96 96 Magnesium 1; via carbonyl oxygen. FT METAL 112 112 Magnesium 2. FT METAL 112 112 Magnesium 3. FT METAL 116 116 Magnesium 1. FT METAL 116 116 Magnesium 3. FT METAL 166 166 Magnesium 3. FT BINDING 28 28 Substrate. FT BINDING 51 51 Substrate; shared with dimeric partner. FT BINDING 84 84 Substrate. FT BINDING 98 98 Substrate; via amide nitrogen. FT BINDING 133 133 Substrate. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:22223895}. FT MOD_RES 3 3 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 10 10 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 74 74 Phosphotyrosine. FT {ECO:0000244|PubMed:15592455}. FT MOD_RES 210 210 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 218 218 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT VARIANT 123 123 I -> T (in dbSNP:rs34863826). FT /FTId=VAR_034159. FT MUTAGEN 28 28 W->A: Reduces affinity for substrate FT about 8-fold. Strongly reduced catalytic FT activity and strongly reduced affinity FT for substrate; when associated with A-46. FT {ECO:0000269|PubMed:18462755}. FT MUTAGEN 46 46 W->A: Reduces affinity for substrate FT about 6-fold. Strongly reduced catalytic FT activity and strongly reduced affinity FT for substrate; when associated with A-28. FT {ECO:0000269|PubMed:18462755}. FT MUTAGEN 51 51 R->Q: Reduces affinity for substrate FT about 15-fold and reduces catalytic rate FT about 17-fold. FT {ECO:0000269|PubMed:18462755}. FT MUTAGEN 84 84 R->Q: Reduces affinity for substrate FT about 5-fold and reduces catalytic rate FT 67-fold. {ECO:0000269|PubMed:18462755}. FT MUTAGEN 98 98 L->A: Reduces affinity for substrate FT about 6-fold. FT {ECO:0000269|PubMed:18462755}. FT MUTAGEN 112 112 E->Q: Reduces catalytic rate 6300-fold. FT {ECO:0000269|PubMed:18462755}. FT MUTAGEN 116 116 E->Q: Reduces catalytic rate 2000-fold. FT {ECO:0000269|PubMed:18462755}. FT MUTAGEN 166 166 E->Q: Reduces catalytic rate 120-fold. FT {ECO:0000269|PubMed:18462755}. FT CONFLICT 50 52 KRT -> NVP (in Ref. 2; AAF25479). FT {ECO:0000305}. FT STRAND 16 25 {ECO:0000244|PDB:2DSC}. FT STRAND 27 37 {ECO:0000244|PDB:2DSC}. FT STRAND 43 51 {ECO:0000244|PDB:2DSC}. FT STRAND 60 69 {ECO:0000244|PDB:2DSC}. FT STRAND 76 84 {ECO:0000244|PDB:2DSC}. FT HELIX 85 87 {ECO:0000244|PDB:2DSC}. FT STRAND 89 93 {ECO:0000244|PDB:2DSC}. FT STRAND 96 98 {ECO:0000244|PDB:2DSC}. FT HELIX 105 117 {ECO:0000244|PDB:2DSC}. FT STRAND 122 126 {ECO:0000244|PDB:2DSC}. FT STRAND 130 132 {ECO:0000244|PDB:2DSC}. FT TURN 134 136 {ECO:0000244|PDB:2DSC}. FT STRAND 140 149 {ECO:0000244|PDB:2DSC}. FT HELIX 153 155 {ECO:0000244|PDB:2DSC}. FT STRAND 164 166 {ECO:0000244|PDB:3AC9}. FT STRAND 169 174 {ECO:0000244|PDB:2DSC}. FT HELIX 175 177 {ECO:0000244|PDB:2DSC}. FT HELIX 178 189 {ECO:0000244|PDB:2DSC}. FT STRAND 192 194 {ECO:0000244|PDB:2DSC}. FT HELIX 195 207 {ECO:0000244|PDB:2DSC}. FT TURN 211 213 {ECO:0000244|PDB:2DSB}. FT HELIX 214 216 {ECO:0000244|PDB:2DSB}. SQ SEQUENCE 219 AA; 24328 MW; 6574E0BF1EA2BB26 CRC64; MESQEPTESS QNGKQYIISE ELISEGKWVK LEKTTYMDPT GKTRTWESVK RTTRKEQTAD GVAVIPVLQR TLHYECIVLV KQFRPPMGGY CIEFPAGLID DGETPEAAAL RELEEETGYK GDIAECSPAV CMDPGLSNCT IHIVTVTING DDAENARPKP KPGDGEFVEV ISLPKNDLLQ RLDALVAEEH LTVDARVYSY ALALKHANAK PFEVPFLKF //