NUDT4_HUMAN
ID NUDT4_HUMAN Reviewed; 180 AA.
AC Q9NZJ9; B7Z916; Q4AEJ6; Q53EZ2; Q68DD7; Q9NPC5; Q9NS30; Q9NZK0; Q9NZK1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 2 {ECO:0000305};
DE Short=DIPP-2;
DE EC=3.6.1.52 {ECO:0000269|PubMed:10777568, ECO:0000269|PubMed:12370170};
DE AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 4;
DE Short=Nudix motif 4;
GN Name=NUDT4 {ECO:0000312|HGNC:HGNC:8051}; Synonyms=DIPP2, KIAA0487;
GN ORFNames=HDCMB47P;
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] (ISOFORMS 1 AND 2), FUNCTION, ENZYME ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Cerebellum;
RX PubMed=10777568; DOI=10.1074/jbc.275.17.12730;
RA Caffrey J.J., Safrany S.T., Yang X., Shears S.B.;
RT "Discovery of molecular and catalytic diversity among human
RT diphosphoinositol-polyphosphate phosphohydrolases. The expanding NUDT
RT family.";
RL J. Biol. Chem. 275:12730-12736(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT "Novel gene identified from dendritic cells.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Trachea;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, and 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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12121577; DOI=10.1186/1471-2091-3-20;
RA Leslie N.R., McLennan A.G., Safrany S.T.;
RT "Cloning and characterisation of hAps1 and hAps2, human diadenosine
RT polyphosphate-metabolising Nudix hydrolases.";
RL BMC Biochem. 3:20-20(2002).
RN [10]
RP FUNCTION, AND ENZYME ACTIVITY.
RX PubMed=12370170; DOI=10.1074/jbc.m209795200;
RA Fisher D.I., Safrany S.T., Strike P., McLennan A.G., Cartwright J.L.;
RT "Nudix hydrolases that degrade dinucleoside and diphosphoinositol
RT polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP)
RT pyrophosphatase activity that generates the glycolytic activator ribose
RT 1,5-bisphosphate.";
RL J. Biol. Chem. 277:47313-47317(2002).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13] {ECO:0007744|PDB:5LTU}
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS).
RA Srikannathasan V., Huber K.;
RT "Crystal Structure of Human NUDT4A- Diphosphoinositol polyphosphate
RT phosphohydrolase 2.";
RL Submitted (SEP-2016) to the PDB data bank.
CC -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-
CC InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4
CC (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a
CC role in signal transduction (PubMed:10777568, PubMed:12370170). Can
CC also catalyze the hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate
CC (Ap6A) but not diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A) and the
CC major reaction products are ADP and p4a from Ap6A (PubMed:12370170).
CC Also able to hydrolyze 5-phosphoribose 1-diphosphate (PubMed:12370170).
CC Does not play a role in U8 snoRNA decapping activity (By similarity).
CC Binds U8 snoRNA (By similarity). {ECO:0000250|UniProtKB:Q8R2U6,
CC ECO:0000269|PubMed:10777568, ECO:0000269|PubMed:12370170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol
CC polyphosphate + phosphate.; EC=3.6.1.52;
CC Evidence={ECO:0000269|PubMed:10777568, ECO:0000269|PubMed:12370170};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + H2O
CC = 1D-myo-inositol hexakisphosphate + H(+) + phosphate;
CC Xref=Rhea:RHEA:22384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628; EC=3.6.1.52;
CC Evidence={ECO:0000269|PubMed:10777568, ECO:0000269|PubMed:12370170};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,5-bis(diphospho)-1D-myo-inositol 1,2,4,6-tetrakisphosphate +
CC H2O = 3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 2
CC H(+) + phosphate; Xref=Rhea:RHEA:56312, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:140372,
CC ChEBI:CHEBI:140374; EC=3.6.1.52;
CC Evidence={ECO:0000269|PubMed:10777568, ECO:0000269|PubMed:12370170};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96G61};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96G61};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q96G61};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.2 nM for PP-InsP5 {ECO:0000269|PubMed:10777568};
CC -!- INTERACTION:
CC Q9NZJ9; P04792: HSPB1; NbExp=3; IntAct=EBI-4280066, EBI-352682;
CC Q9NZJ9; P42858: HTT; NbExp=6; IntAct=EBI-4280066, EBI-466029;
CC Q9NZJ9; Q14145: KEAP1; NbExp=3; IntAct=EBI-4280066, EBI-751001;
CC Q9NZJ9; O76024: WFS1; NbExp=3; IntAct=EBI-4280066, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12121577}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Alpha, DIPP2alpha;
CC IsoId=Q9NZJ9-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta, DIPP2beta;
CC IsoId=Q9NZJ9-2; Sequence=VSP_014270;
CC Name=3;
CC IsoId=Q9NZJ9-3; Sequence=VSP_014269, VSP_014270;
CC -!- TISSUE SPECIFICITY: Expressed in heart and, at lower level in skeletal
CC muscle, pancreas and kidney. {ECO:0000269|PubMed:10777568}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF75563.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE16985.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF191649; AAF68855.1; -; mRNA.
DR EMBL; AF191650; AAF68856.1; -; mRNA.
DR EMBL; AF191651; AAF68857.1; -; mRNA.
DR EMBL; AF191652; AAF68858.2; -; mRNA.
DR EMBL; AF191653; AAF68859.1; -; mRNA.
DR EMBL; AB007956; BAE16985.1; ALT_INIT; mRNA.
DR EMBL; AF067803; AAF75563.1; ALT_SEQ; mRNA.
DR EMBL; CR749445; CAH18283.1; -; mRNA.
DR EMBL; BT020109; AAV38912.1; -; mRNA.
DR EMBL; BT020110; AAV38913.1; -; mRNA.
DR EMBL; AK304296; BAH14152.1; -; mRNA.
DR EMBL; AK223497; BAD97217.1; -; mRNA.
DR EMBL; BC012069; AAH12069.1; -; mRNA.
DR EMBL; BC051310; AAH51310.1; -; mRNA.
DR CCDS; CCDS44952.1; -. [Q9NZJ9-1]
DR CCDS; CCDS73504.1; -. [Q9NZJ9-3]
DR CCDS; CCDS9044.1; -. [Q9NZJ9-2]
DR RefSeq; NP_001287951.1; NM_001301022.1. [Q9NZJ9-3]
DR RefSeq; NP_001287952.1; NM_001301023.1.
DR RefSeq; NP_001287953.1; NM_001301024.1.
DR RefSeq; NP_061967.3; NM_019094.5. [Q9NZJ9-1]
DR RefSeq; NP_950241.1; NM_199040.3. [Q9NZJ9-2]
DR RefSeq; XP_011536096.1; XM_011537794.2. [Q9NZJ9-3]
DR RefSeq; XP_011536097.1; XM_011537795.2.
DR RefSeq; XP_011536098.1; XM_011537796.2.
DR PDB; 5LTU; X-ray; 2.23 A; A/B=1-180.
DR PDB; 7NNJ; X-ray; 1.75 A; A/B=9-146.
DR PDBsum; 5LTU; -.
DR PDBsum; 7NNJ; -.
DR AlphaFoldDB; Q9NZJ9; -.
DR SMR; Q9NZJ9; -.
DR BioGRID; 116334; 8.
DR IntAct; Q9NZJ9; 6.
DR MINT; Q9NZJ9; -.
DR ChEMBL; CHEMBL4295967; -.
DR iPTMnet; Q9NZJ9; -.
DR MetOSite; Q9NZJ9; -.
DR PhosphoSitePlus; Q9NZJ9; -.
DR BioMuta; NUDT4; -.
DR DMDM; 68565946; -.
DR EPD; Q9NZJ9; -.
DR jPOST; Q9NZJ9; -.
DR MassIVE; Q9NZJ9; -.
DR MaxQB; Q9NZJ9; -.
DR PaxDb; Q9NZJ9; -.
DR PeptideAtlas; Q9NZJ9; -.
DR PRIDE; Q9NZJ9; -.
DR ProteomicsDB; 83421; -. [Q9NZJ9-1]
DR ProteomicsDB; 83422; -. [Q9NZJ9-2]
DR ProteomicsDB; 83423; -. [Q9NZJ9-3]
DR TopDownProteomics; Q9NZJ9-2; -. [Q9NZJ9-2]
DR Antibodypedia; 17488; 90 antibodies from 20 providers.
DR DNASU; 11163; -.
DR Ensembl; ENST00000337179.9; ENSP00000338352.5; ENSG00000173598.14. [Q9NZJ9-2]
DR Ensembl; ENST00000415493.7; ENSP00000406612.2; ENSG00000173598.14. [Q9NZJ9-1]
DR Ensembl; ENST00000547014.5; ENSP00000448032.1; ENSG00000173598.14. [Q9NZJ9-3]
DR GeneID; 11163; -.
DR KEGG; hsa:11163; -.
DR MANE-Select; ENST00000322209.5; ENSP00000492425.1; NM_001355407.2; NP_001342336.1. [Q9NZJ9-2]
DR MANE-Select; ENST00000415493.7; ENSP00000406612.2; NM_019094.6; NP_061967.3.
DR UCSC; uc001tcm.4; human. [Q9NZJ9-1]
DR CTD; 11163; -.
DR GeneCards; NUDT4; -.
DR HGNC; HGNC:8051; NUDT4.
DR HPA; ENSG00000173598; Low tissue specificity.
DR MIM; 609229; gene.
DR neXtProt; NX_Q9NZJ9; -.
DR OpenTargets; ENSG00000173598; -.
DR PharmGKB; PA31835; -.
DR VEuPathDB; HostDB:ENSG00000173598; -.
DR eggNOG; KOG2839; Eukaryota.
DR GeneTree; ENSGT00940000155210; -.
DR HOGENOM; CLU_037162_1_0_1; -.
DR InParanoid; Q9NZJ9; -.
DR OMA; NTNPRHN; -.
DR PhylomeDB; Q9NZJ9; -.
DR TreeFam; TF106349; -.
DR BioCyc; MetaCyc:HS10696-MON; -.
DR PathwayCommons; Q9NZJ9; -.
DR Reactome; R-HSA-1855167; Synthesis of pyrophosphates in the cytosol.
DR SABIO-RK; Q9NZJ9; -.
DR SignaLink; Q9NZJ9; -.
DR BioGRID-ORCS; 11163; 549 hits in 1072 CRISPR screens.
DR ChiTaRS; NUDT4; human.
DR GeneWiki; NUDT4; -.
DR GenomeRNAi; 11163; -.
DR Pharos; Q9NZJ9; Tbio.
DR PRO; PR:Q9NZJ9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NZJ9; protein.
DR Bgee; ENSG00000173598; Expressed in heart right ventricle and 210 other tissues.
DR ExpressionAtlas; Q9NZJ9; baseline and differential.
DR Genevisible; Q9NZJ9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034431; F:bis(5'-adenosyl)-hexaphosphatase activity; IBA:GO_Central.
DR GO; GO:0034432; F:bis(5'-adenosyl)-pentaphosphatase activity; IBA:GO_Central.
DR GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0000298; F:endopolyphosphatase activity; IBA:GO_Central.
DR GO; GO:0052842; F:inositol diphosphate pentakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR GO; GO:1901911; P:adenosine 5'-(hexahydrogen pentaphosphate) catabolic process; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; TAS:UniProtKB.
DR GO; GO:0019935; P:cyclic-nucleotide-mediated signaling; TAS:UniProtKB.
DR GO; GO:1901909; P:diadenosine hexaphosphate catabolic process; IBA:GO_Central.
DR GO; GO:1901907; P:diadenosine pentaphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0071543; P:diphosphoinositol polyphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
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 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; Alternative splicing; Cytoplasm; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Reference proteome; RNA-binding.
FT CHAIN 1..180
FT /note="Diphosphoinositol polyphosphate phosphohydrolase 2"
FT /id="PRO_0000057058"
FT DOMAIN 18..144
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 51..72
FT /note="Nudix box"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 18..20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 39..41
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 89..91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3"
FT /id="VSP_014269"
FT VAR_SEQ 85
FT /note="E -> EQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10777568,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.5"
FT /id="VSP_014270"
FT CONFLICT 16
FT /note="G -> D (in Ref. 1; AAF68857)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="R -> Q (in Ref. 7; BAD97217)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="V -> D (in Ref. 3; AAF75563)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="A -> V (in Ref. 1; AAF68857)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="S -> P (in Ref. 1; AAF68858)"
FT /evidence="ECO:0000305"
FT STRAND 18..28
FT /evidence="ECO:0007829|PDB:5LTU"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:5LTU"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5LTU"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:5LTU"
FT STRAND 73..86
FT /evidence="ECO:0007829|PDB:5LTU"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:5LTU"
FT STRAND 91..103
FT /evidence="ECO:0007829|PDB:5LTU"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:5LTU"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:5LTU"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:5LTU"
SQ SEQUENCE 180 AA; 20306 MW; 86D766F8F5B22D13 CRC64;
MMKFKPNQTR TYDREGFKKR AACLCFRSEQ EDEVLLVSSS RYPDQWIVPG GGMEPEEEPG
GAAVREVYEE AGVKGKLGRL LGIFENQDRK HRTYVYVLTV TEILEDWEDS VNIGRKREWF
KVEDAIKVLQ CHKPVHAEYL EKLKLGCSPA NGNSTVPSLP DNNALFVTAA QTSGLPSSVR
