NUDT5_HUMAN
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 03-AUG-2022, entry version 189.
DE RecName: Full=ADP-sugar pyrophosphatase;
DE EC=3.6.1.13 {ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:21389046};
DE AltName: Full=8-oxo-dGDP phosphatase;
DE EC=3.6.1.58 {ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:19699693, ECO:0000269|PubMed:21389046};
DE AltName: Full=Nuclear ATP-synthesis protein NUDIX5 {ECO:0000305|PubMed:27257257};
DE EC=2.7.7.96 {ECO:0000269|PubMed:27257257};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 5 {ECO:0000305};
DE Short=Nudix motif 5 {ECO:0000305};
DE Short=hNUDT5 {ECO:0000303|PubMed:21768126};
DE AltName: Full=YSA1H {ECO:0000303|PubMed:10567213};
GN Name=NUDT5; Synonyms=NUDIX5 {ECO:0000303|PubMed:27257257};
GN ORFNames=HSPC115 {ECO:0000303|PubMed:11042152};
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], AND FUNCTION.
RX PubMed=10567213; DOI=10.1042/bj3440331;
RA Gasmi L., Cartwright J.L., McLennan A.G.;
RT "Cloning, expression and characterization of YSA1H, a human adenosine 5'-
RT diphosphosugar pyrophosphatase possessing a MutT motif.";
RL Biochem. J. 344:331-337(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
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., Conrad A.,
RA Miller J.H.;
RT "Cloning and characterization of a new member of the Nudix hydrolases from
RT 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 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT 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., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-74, AND IDENTIFICATION BY
RP 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 cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19699693; DOI=10.1016/j.dnarep.2009.07.011;
RA Kamiya H., Hori M., Arimori T., Sekiguchi M., Yamagata Y., Harashima H.;
RT "NUDT5 hydrolyzes oxidized deoxyribonucleoside diphosphates with broad
RT substrate specificity.";
RL DNA Repair 8:1250-1254(2009).
RN [11]
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., Walther T.C.,
RA 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-10, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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., Buerckstuemmer T.,
RA 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 [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21389046; DOI=10.1093/jb/mvr028;
RA Ito R., Sekiguchi M., Setoyama D., Nakatsu Y., Yamagata Y., Hayakawa H.;
RT "Cleavage of oxidized guanine nucleotide and ADP sugar by human NUDT5
RT protein.";
RL J. Biochem. 149:731-738(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
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., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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., Meinnel T.,
RA 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, INDUCTION, INTERACTION WITH PARG, PHOSPHORYLATION AT
RP THR-45, AND MUTAGENESIS OF THR-45 AND GLU-112.
RX PubMed=27257257; DOI=10.1126/science.aad9335;
RA Wright R.H., Lioutas A., Le Dily F., Soronellas D., Pohl A., Bonet J.,
RA Nacht A.S., Samino S., Font-Mateu J., Vicent G.P., Wierer M., Trabado M.A.,
RA Schelhorn C., Carolis C., Macias M.J., Yanes O., Oliva B., Beato M.;
RT "ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for
RT chromatin remodeling.";
RL Science 352:1221-1225(2016).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-42, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-210 IN COMPLEX WITH AMP;
RP MAGNESIUM IONS AND ADP-RIBOSE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP 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 [22]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-210 IN COMPLEX WITH AMPCPR AND
RP MAGNESIUM IONS, COFACTOR, MUTAGENESIS OF TRP-28; TRP-46; ARG-51; ARG-84;
RP 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).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 13-208 IN COMPLEX WITH
RP 8-OXO-DGDP; 8-OXO-DGMP; 8-OXO-DADP AND MANGANESE IONS, COFACTOR, AND
RP SUBUNIT.
RX PubMed=21768126; DOI=10.1093/nar/gkr575;
RA Arimori T., Tamaoki H., Nakamura T., Kamiya H., Ikemizu S., Takagi Y.,
RA Ishibashi T., Harashima H., Sekiguchi M., Yamagata Y.;
RT "Diverse substrate recognition and hydrolysis mechanisms of human NUDT5.";
RL Nucleic Acids Res. 39:8972-8983(2011).
CC -!- FUNCTION: Enzyme that can either act as an ADP-sugar pyrophosphatase in
CC absence of diphosphate or catalyze the synthesis of ATP in presence of
CC diphosphate (PubMed:27257257). In absence of diphosphate, hydrolyzes
CC with similar activities various modified nucleoside diphosphates such
CC as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP
CC (PubMed:10567213, PubMed:10722730, PubMed:19699693, PubMed:21389046,
CC PubMed:17052728). Can also hydrolyze other nucleotide sugars with low
CC activity (PubMed:19699693, PubMed:21389046). In presence of
CC diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing
CC the conversion of ADP-ribose to ATP and ribose 5-phosphate. Nuclear ATP
CC synthesis takes place when dephosphorylated at Thr-45
CC (PubMed:27257257). Nuclear ATP generation is required for extensive
CC chromatin remodeling events that are energy-consuming
CC (PubMed:27257257). Does not play a role in U8 snoRNA decapping activity
CC (By similarity). Binds U8 snoRNA (By similarity).
CC {ECO:0000250|UniProtKB:Q9JKX6, ECO:0000269|PubMed:10567213,
CC ECO:0000269|PubMed:10722730, ECO:0000269|PubMed:17052728,
CC ECO:0000269|PubMed:19699693, ECO:0000269|PubMed:21389046,
CC ECO:0000269|PubMed:27257257}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate + H(+) = ADP-D-ribose +
CC diphosphate; Xref=Rhea:RHEA:50248, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:78346; EC=2.7.7.96;
CC Evidence={ECO:0000269|PubMed:27257257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC EC=3.6.1.13; Evidence={ECO:0000269|PubMed:17052728,
CC ECO:0000269|PubMed:21389046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dGDP + H2O = 8-oxo-dGMP + H(+) + phosphate;
CC Xref=Rhea:RHEA:32063, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:63224, ChEBI:CHEBI:63715; EC=3.6.1.58;
CC Evidence={ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:19699693,
CC ECO:0000269|PubMed:21389046};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755,
CC ECO:0000269|PubMed:21768126};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:17052728,
CC ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 uM for 8-oxo-dGDP {ECO:0000269|PubMed:19699693};
CC KM=2.9 uM for 8-oxo-dADP {ECO:0000269|PubMed:19699693};
CC KM=8.8 uM for 2-oxo-dADP {ECO:0000269|PubMed:19699693};
CC KM=4.0 uM for 5-CHO-dUDP {ECO:0000269|PubMed:19699693};
CC KM=7.6 uM for dGDP {ECO:0000269|PubMed:19699693};
CC KM=12.6 uM for dADP {ECO:0000269|PubMed:19699693};
CC KM=3.8 uM for 8-oxo-dGDP (at pH 8.0) {ECO:0000269|PubMed:21389046};
CC KM=3.5 uM for 8-oxo-dGDP (at pH 10.0) {ECO:0000269|PubMed:21389046};
CC KM=1.9 uM for ADP-D-ribose (at pH 8.0) {ECO:0000269|PubMed:21389046};
CC KM=36 uM for 8-oxo-dGTP (at pH 10.0) {ECO:0000269|PubMed:21389046};
CC KM=42.6 uM for ADP-D-ribose (in the presence of diphosphate)
CC {ECO:0000269|PubMed:27257257};
CC Vmax=11 pmol/min/ug enzyme with 8-oxo-dGDP as substrate (at pH 8.0)
CC {ECO:0000269|PubMed:21389046};
CC Vmax=2400 pmol/min/ug enzyme with ADP-D-ribose as substrate (at pH
CC 8.0) {ECO:0000269|PubMed:21389046};
CC Vmax=46 pmol/min/ug enzyme with 8-oxo-dGDP as substrate (at pH 10.0)
CC {ECO:0000269|PubMed:21389046};
CC Vmax=1.7 pmol/min/ug enzyme with 8-oxo-dGTP as substrate (at pH 10.0)
CC {ECO:0000269|PubMed:21389046};
CC Note=kcat is 0.369 min(-1) for 8-OH-dGDP. kcat is 0.538 min(-1) for
CC 8-OH-dADP. kcat is 0.226 min(-1) for 2-OH-dADP. kcat is 0.209 min(-1)
CC for 5-CHO-dUDP. kcat is 0.929 min(-1) for dGDP. kcat is 0.365 min(-1)
CC for dADP. {ECO:0000269|PubMed:19699693};
CC -!- SUBUNIT: Homodimer (PubMed:27257257, PubMed:17052728, PubMed:18462755,
CC PubMed:21768126). Interacts with PARG (PubMed:27257257).
CC {ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755,
CC ECO:0000269|PubMed:21768126, ECO:0000269|PubMed:27257257}.
CC -!- INTERACTION:
CC Q9UKK9; P10606: COX5B; NbExp=3; IntAct=EBI-721623, EBI-1053725;
CC Q9UKK9; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-721623, EBI-739467;
CC Q9UKK9; Q9UKK9: NUDT5; NbExp=3; IntAct=EBI-721623, EBI-721623;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:27257257}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Most abundant in liver.
CC {ECO:0000269|PubMed:10722730}.
CC -!- INDUCTION: Overexpressed in cancer patients with a poor outcome.
CC {ECO:0000269|PubMed:27257257}.
CC -!- PTM: Phosphorylation at Thr-45 is required for homodimer stability;
CC dephosphorylation results in destabilization of the homodimer.
CC Dephosphorylation at Thr-45 promotes the ATP-synthesis activity.
CC {ECO:0000269|PubMed:27257257}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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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_014142.3.
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 PDB; 5NQR; X-ray; 2.20 A; A/B=1-219.
DR PDB; 5NWH; X-ray; 2.60 A; A/B=1-219.
DR PDB; 5QJ4; X-ray; 1.89 A; A/B/C/D=1-208.
DR PDB; 5QJ5; X-ray; 1.72 A; A/B/C/D=1-208.
DR PDB; 5QJ6; X-ray; 1.65 A; A/B/C/D=1-208.
DR PDB; 5QJ7; X-ray; 1.56 A; A/B/C/D=1-208.
DR PDB; 5QJ8; X-ray; 1.76 A; A/B/C/D=1-208.
DR PDB; 5QJ9; X-ray; 1.85 A; A/B/C/D=1-208.
DR PDB; 5QJA; X-ray; 1.64 A; A/B/C/D=1-208.
DR PDB; 5QJB; X-ray; 1.66 A; A/B/C/D=1-208.
DR PDB; 5QJC; X-ray; 1.47 A; A/B/C/D=1-208.
DR PDB; 5QJD; X-ray; 1.61 A; A/B/C/D=1-208.
DR PDB; 5QJE; X-ray; 1.75 A; A/B/C/D=1-208.
DR PDB; 5QJF; X-ray; 1.63 A; A/B/C/D=1-208.
DR PDB; 5QJG; X-ray; 1.57 A; A/B/C/D=1-208.
DR PDB; 5QJH; X-ray; 2.03 A; A/B/C/D=1-208.
DR PDB; 5QJI; X-ray; 1.69 A; A/B/C/D=1-208.
DR PDB; 5QJJ; X-ray; 1.71 A; A/B/C/D=1-208.
DR PDB; 5QJK; X-ray; 1.65 A; A/B/C/D=1-208.
DR PDB; 5QJL; X-ray; 1.66 A; A/B/C/D=1-208.
DR PDB; 5QJM; X-ray; 1.75 A; A/B/C/D=1-208.
DR PDB; 5QJN; X-ray; 1.77 A; A/B/C/D=1-208.
DR PDB; 5QJO; X-ray; 1.98 A; A/B/C/D=1-208.
DR PDB; 5QJP; X-ray; 1.50 A; A/B/C/D=1-208.
DR PDB; 5QJQ; X-ray; 1.55 A; A/B/C/D=1-208.
DR PDB; 5QJR; X-ray; 1.62 A; A/B/C/D=1-208.
DR PDB; 5QJS; X-ray; 1.58 A; A/B/C/D=1-208.
DR PDB; 5QJT; X-ray; 1.62 A; A/B/C/D=1-208.
DR PDB; 5QJU; X-ray; 1.77 A; A/B/C/D=1-208.
DR PDB; 5QJV; X-ray; 1.61 A; A/B/C/D=1-208.
DR PDB; 5QJW; X-ray; 1.57 A; A/B/C/D=1-208.
DR PDB; 5QJX; X-ray; 1.73 A; A/B/C/D=1-208.
DR PDB; 5QJY; X-ray; 1.77 A; A/B/C/D=1-208.
DR PDB; 5QJZ; X-ray; 1.52 A; A/B/C/D=1-208.
DR PDB; 5QK0; X-ray; 1.44 A; A/B/C/D=1-208.
DR PDB; 5QK1; X-ray; 1.49 A; A/B/C/D=1-208.
DR PDB; 5QK2; X-ray; 1.65 A; A/B/C/D=1-208.
DR PDB; 5QK3; X-ray; 1.71 A; A/B/C/D=1-208.
DR PDB; 5QK4; X-ray; 1.62 A; A/B/C/D=1-208.
DR PDB; 5QK5; X-ray; 1.63 A; A/B/C/D=1-208.
DR PDB; 5QK6; X-ray; 1.51 A; A/B/C/D=1-208.
DR PDB; 5QK7; X-ray; 1.66 A; A/B/C/D=1-208.
DR PDB; 5QK8; X-ray; 1.71 A; A/B/C/D=1-208.
DR PDB; 5QK9; X-ray; 1.56 A; A/B/C/D=1-208.
DR PDB; 5QKA; X-ray; 1.55 A; A/B/C/D=1-208.
DR PDB; 5QKB; X-ray; 1.58 A; A/B/C/D=1-208.
DR PDB; 5QTL; X-ray; 1.73 A; A/B/C/D=1-208.
DR PDB; 5QTM; X-ray; 1.79 A; A/B/C/D=1-208.
DR PDB; 5QTN; X-ray; 1.83 A; A/B/C/D=1-208.
DR PDB; 5QTO; X-ray; 1.67 A; A/B/C/D=1-208.
DR PDB; 5QTP; X-ray; 1.73 A; A/B/C/D=1-208.
DR PDB; 5QTQ; X-ray; 1.82 A; A/B/C/D=1-208.
DR PDB; 5QTR; X-ray; 1.55 A; A/B/C/D=1-208.
DR PDB; 5QTS; X-ray; 1.85 A; A/B/C/D=1-208.
DR PDB; 6GRU; X-ray; 1.93 A; A/B/C/D=1-208.
DR PDBsum; 2DSB; -.
DR PDBsum; 2DSC; -.
DR PDBsum; 2DSD; -.
DR PDBsum; 3AC9; -.
DR PDBsum; 3ACA; -.
DR PDBsum; 3BM4; -.
DR PDBsum; 3L85; -.
DR PDBsum; 5NQR; -.
DR PDBsum; 5NWH; -.
DR PDBsum; 5QJ4; -.
DR PDBsum; 5QJ5; -.
DR PDBsum; 5QJ6; -.
DR PDBsum; 5QJ7; -.
DR PDBsum; 5QJ8; -.
DR PDBsum; 5QJ9; -.
DR PDBsum; 5QJA; -.
DR PDBsum; 5QJB; -.
DR PDBsum; 5QJC; -.
DR PDBsum; 5QJD; -.
DR PDBsum; 5QJE; -.
DR PDBsum; 5QJF; -.
DR PDBsum; 5QJG; -.
DR PDBsum; 5QJH; -.
DR PDBsum; 5QJI; -.
DR PDBsum; 5QJJ; -.
DR PDBsum; 5QJK; -.
DR PDBsum; 5QJL; -.
DR PDBsum; 5QJM; -.
DR PDBsum; 5QJN; -.
DR PDBsum; 5QJO; -.
DR PDBsum; 5QJP; -.
DR PDBsum; 5QJQ; -.
DR PDBsum; 5QJR; -.
DR PDBsum; 5QJS; -.
DR PDBsum; 5QJT; -.
DR PDBsum; 5QJU; -.
DR PDBsum; 5QJV; -.
DR PDBsum; 5QJW; -.
DR PDBsum; 5QJX; -.
DR PDBsum; 5QJY; -.
DR PDBsum; 5QJZ; -.
DR PDBsum; 5QK0; -.
DR PDBsum; 5QK1; -.
DR PDBsum; 5QK2; -.
DR PDBsum; 5QK3; -.
DR PDBsum; 5QK4; -.
DR PDBsum; 5QK5; -.
DR PDBsum; 5QK6; -.
DR PDBsum; 5QK7; -.
DR PDBsum; 5QK8; -.
DR PDBsum; 5QK9; -.
DR PDBsum; 5QKA; -.
DR PDBsum; 5QKB; -.
DR PDBsum; 5QTL; -.
DR PDBsum; 5QTM; -.
DR PDBsum; 5QTN; -.
DR PDBsum; 5QTO; -.
DR PDBsum; 5QTP; -.
DR PDBsum; 5QTQ; -.
DR PDBsum; 5QTR; -.
DR PDBsum; 5QTS; -.
DR PDBsum; 6GRU; -.
DR AlphaFoldDB; Q9UKK9; -.
DR SMR; Q9UKK9; -.
DR BioGRID; 116335; 38.
DR IntAct; Q9UKK9; 27.
DR MINT; Q9UKK9; -.
DR STRING; 9606.ENSP00000419628; -.
DR BindingDB; Q9UKK9; -.
DR ChEMBL; CHEMBL4105713; -.
DR GlyGen; Q9UKK9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UKK9; -.
DR MetOSite; Q9UKK9; -.
DR PhosphoSitePlus; Q9UKK9; -.
DR SwissPalm; Q9UKK9; -.
DR BioMuta; NUDT5; -.
DR EPD; Q9UKK9; -.
DR jPOST; Q9UKK9; -.
DR MassIVE; Q9UKK9; -.
DR MaxQB; Q9UKK9; -.
DR PaxDb; Q9UKK9; -.
DR PeptideAtlas; Q9UKK9; -.
DR PRIDE; Q9UKK9; -.
DR ProteomicsDB; 84813; -.
DR Antibodypedia; 11248; 115 antibodies from 25 providers.
DR DNASU; 11164; -.
DR Ensembl; ENST00000491614.6; ENSP00000419628.1; ENSG00000165609.13.
DR Ensembl; ENST00000537776.5; ENSP00000445116.1; ENSG00000165609.13.
DR GeneID; 11164; -.
DR KEGG; hsa:11164; -.
DR MANE-Select; ENST00000491614.6; ENSP00000419628.1; NM_014142.4; NP_054861.2.
DR UCSC; uc001ilj.4; human.
DR CTD; 11164; -.
DR DisGeNET; 11164; -.
DR GeneCards; NUDT5; -.
DR HGNC; HGNC:8052; NUDT5.
DR HPA; ENSG00000165609; Low tissue specificity.
DR MIM; 609230; gene.
DR neXtProt; NX_Q9UKK9; -.
DR OpenTargets; ENSG00000165609; -.
DR PharmGKB; PA31838; -.
DR VEuPathDB; HostDB:ENSG00000165609; -.
DR eggNOG; KOG3041; Eukaryota.
DR GeneTree; ENSGT00940000154045; -.
DR HOGENOM; CLU_062658_0_2_1; -.
DR InParanoid; Q9UKK9; -.
DR OMA; CNTNLHM; -.
DR OrthoDB; 1466354at2759; -.
DR PhylomeDB; Q9UKK9; -.
DR TreeFam; TF106347; -.
DR BioCyc; MetaCyc:HS09255-MON; -.
DR BRENDA; 2.7.7.96; 2681.
DR BRENDA; 3.6.1.13; 2681.
DR BRENDA; 3.6.1.58; 2681.
DR PathwayCommons; Q9UKK9; -.
DR Reactome; R-HSA-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR SABIO-RK; Q9UKK9; -.
DR SignaLink; Q9UKK9; -.
DR BioGRID-ORCS; 11164; 15 hits in 1078 CRISPR screens.
DR ChiTaRS; NUDT5; human.
DR EvolutionaryTrace; Q9UKK9; -.
DR GeneWiki; NUDT5; -.
DR GenomeRNAi; 11164; -.
DR Pharos; Q9UKK9; Tbio.
DR PRO; PR:Q9UKK9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9UKK9; protein.
DR Bgee; ENSG00000165609; Expressed in right lobe of liver and 183 other tissues.
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; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; IDA:UniProtKB.
DR GO; GO:0044716; F:8-oxo-GDP phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0019144; F:ADP-sugar diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0019303; P:D-ribose catabolic process; IDA:UniProtKB.
DR GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; NAS:ProtInc.
DR GO; GO:0009191; P:ribonucleoside diphosphate catabolic process; IDA:UniProtKB.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
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; Hydrolase; Isopeptide bond; Magnesium;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Transferase; Ubl conjugation.
FT CHAIN 1..219
FT /note="ADP-sugar pyrophosphatase"
FT /id="PRO_0000057048"
FT DOMAIN 57..197
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 97..118
FT /note="Nudix box"
FT BINDING 28
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:17052728,
FT ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
FT BINDING 46..47
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:17052728,
FT ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
FT BINDING 51
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:17052728,
FT ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
FT BINDING 84
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:17052728,
FT ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17052728,
FT ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
FT BINDING 98
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:17052728"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17052728,
FT ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17052728,
FT ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17052728,
FT ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17052728,
FT ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
FT BINDING 133
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:17052728"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17052728,
FT ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27257257"
FT MOD_RES 74
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 218
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 123
FT /note="I -> T (in dbSNP:rs34863826)"
FT /id="VAR_034159"
FT MUTAGEN 28
FT /note="W->A: Reduces affinity for substrate about 8-fold.
FT Strongly reduced catalytic activity and strongly reduced
FT affinity for substrate; when associated with A-46."
FT /evidence="ECO:0000269|PubMed:18462755"
FT MUTAGEN 45
FT /note="T->A: Impaired phosphorylation; generates ATP in the
FT presence of diphosphate."
FT /evidence="ECO:0000269|PubMed:27257257"
FT MUTAGEN 45
FT /note="T->D: Phosphomimetic mutant; unable to generate ATP
FT in the presence of diphosphate."
FT /evidence="ECO:0000269|PubMed:27257257"
FT MUTAGEN 46
FT /note="W->A: Reduces affinity for substrate about 6-fold.
FT Strongly reduced catalytic activity and strongly reduced
FT affinity for substrate; when associated with A-28."
FT /evidence="ECO:0000269|PubMed:18462755"
FT MUTAGEN 51
FT /note="R->Q: Reduces affinity for substrate about 15-fold
FT and reduces catalytic rate about 17-fold."
FT /evidence="ECO:0000269|PubMed:18462755"
FT MUTAGEN 84
FT /note="R->Q: Reduces affinity for substrate about 5-fold
FT and reduces catalytic rate 67-fold."
FT /evidence="ECO:0000269|PubMed:18462755"
FT MUTAGEN 98
FT /note="L->A: Reduces affinity for substrate about 6-fold."
FT /evidence="ECO:0000269|PubMed:18462755"
FT MUTAGEN 112
FT /note="E->Q: Catalytic inactive mutant for both ADP-sugar
FT pyrophosphatase and nuclear ATP-synthesis activities.
FT Reduces catalytic rate 6300-fold."
FT /evidence="ECO:0000269|PubMed:18462755,
FT ECO:0000269|PubMed:27257257"
FT MUTAGEN 116
FT /note="E->Q: Reduces catalytic rate 2000-fold."
FT /evidence="ECO:0000269|PubMed:18462755"
FT MUTAGEN 166
FT /note="E->Q: Reduces catalytic rate 120-fold."
FT /evidence="ECO:0000269|PubMed:18462755"
FT CONFLICT 50..52
FT /note="KRT -> NVP (in Ref. 2; AAF25479)"
FT /evidence="ECO:0000305"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:5QK0"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:5QK0"
FT STRAND 43..53
FT /evidence="ECO:0007829|PDB:5QK0"
FT STRAND 55..69
FT /evidence="ECO:0007829|PDB:5QK0"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:5QK0"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:5QK0"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:5QK0"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5QK0"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:5QK0"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:5QK0"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:5QK0"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:5QK0"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:5QK0"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3AC9"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:5QK0"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:5QK0"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:5QK0"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5QK0"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:5QK0"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2DSB"
FT HELIX 214..216
FT /evidence="ECO:0007829|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
