NUD22_HUMAN
ID NUD22_HUMAN Reviewed; 303 AA.
AC Q9BRQ3; C9JY06; Q71RD5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Uridine diphosphate glucose pyrophosphatase NUDT22;
DE Short=UDPG pyrophosphatase;
DE Short=UGPPase;
DE EC=3.6.1.45;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 22;
DE Short=Nudix motif 22;
GN Name=NUDT22; ORFNames=PP11246;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-260
RP AND PRO-263.
RC TISSUE=Uterus;
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 [4] {ECO:0007744|PDB:5LF9}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "Crystal structure of human NUDT22.";
RL Submitted (JUN-2016) to the PDB data bank.
RN [5] {ECO:0007744|PDB:5LOR, ECO:0007744|PDB:5LOU}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE AND
RP MAGNESIUM IONS, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, MOTIF NUDIX BOX, AND MUTAGENESIS OF HIS-156; GLU-189
RP AND GLU-193.
RX PubMed=29413322; DOI=10.1016/j.str.2018.01.004;
RA Carter M., Jemth A.S., Carreras-Puigvert J., Herr P., Martinez Carranza M.,
RA Vallin K.S.A., Throup A., Helleday T., Stenmark P.;
RT "Human NUDT22 is a UDP-glucose/galactose hydrolase exhibiting a unique
RT structural fold.";
RL Structure 26:295-303(2018).
CC -!- FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and
CC UDP-galactose to galactose 1-phosphate and UMP. Preferred substrate is
CC UDP-glucose. {ECO:0000269|PubMed:29413322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.;
CC EC=3.6.1.45; Evidence={ECO:0000269|PubMed:29413322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:29413322};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.5 uM for UDP-glucose {ECO:0000269|PubMed:29413322};
CC KM=51.4 uM for UDP-galactose {ECO:0000269|PubMed:29413322};
CC Note=kcat is 0.69 sec(-1) for UDP-glucose. kcat is 0.55 sec(-1) for
CC UDP-galactose. {ECO:0000269|PubMed:29413322};
CC -!- INTERACTION:
CC Q9BRQ3; Q03989: ARID5A; NbExp=3; IntAct=EBI-10297093, EBI-948603;
CC Q9BRQ3; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-10297093, EBI-742054;
CC Q9BRQ3; O96015: DNAL4; NbExp=7; IntAct=EBI-10297093, EBI-742362;
CC Q9BRQ3; Q0VD86: INCA1; NbExp=3; IntAct=EBI-10297093, EBI-6509505;
CC Q9BRQ3; Q53HC5: KLHL26; NbExp=3; IntAct=EBI-10297093, EBI-724915;
CC Q9BRQ3; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-10297093, EBI-12039345;
CC Q9BRQ3; Q9BVN2: RUSC1; NbExp=4; IntAct=EBI-10297093, EBI-6257312;
CC Q9BRQ3; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-10297093, EBI-3957636;
CC Q9BRQ3; P15884-3: TCF4; NbExp=3; IntAct=EBI-10297093, EBI-13636688;
CC Q9BRQ3; Q08117: TLE5; NbExp=4; IntAct=EBI-10297093, EBI-717810;
CC Q9BRQ3; Q08117-2: TLE5; NbExp=3; IntAct=EBI-10297093, EBI-11741437;
CC Q9BRQ3; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-10297093, EBI-11975223;
CC Q9BRQ3; Q9H977-4: WDR54; NbExp=5; IntAct=EBI-10297093, EBI-23279779;
CC Q9BRQ3; Q86T24: ZBTB33; NbExp=3; IntAct=EBI-10297093, EBI-2515625;
CC Q9BRQ3; Q9H0C1: ZMYND12; NbExp=5; IntAct=EBI-10297093, EBI-12030590;
CC Q9BRQ3; P52747: ZNF143; NbExp=3; IntAct=EBI-10297093, EBI-2849334;
CC Q9BRQ3; P17023: ZNF19; NbExp=3; IntAct=EBI-10297093, EBI-12884200;
CC Q9BRQ3; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-10297093, EBI-10252492;
CC Q9BRQ3; Q8TD17: ZNF398; NbExp=3; IntAct=EBI-10297093, EBI-8643207;
CC Q9BRQ3; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-10297093, EBI-745520;
CC Q9BRQ3; Q5T619: ZNF648; NbExp=3; IntAct=EBI-10297093, EBI-11985915;
CC Q9BRQ3; Q8N720: ZNF655; NbExp=3; IntAct=EBI-10297093, EBI-625509;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BRQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRQ3-2; Sequence=VSP_021884;
CC Name=3;
CC IsoId=Q9BRQ3-3; Sequence=VSP_053790;
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AF370402; AAQ15238.1; -; mRNA.
DR EMBL; AP001453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP006334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006129; AAH06129.1; -; mRNA.
DR CCDS; CCDS44640.1; -. [Q9BRQ3-3]
DR CCDS; CCDS8061.1; -. [Q9BRQ3-1]
DR RefSeq; NP_001122084.1; NM_001128612.2.
DR RefSeq; NP_001122085.1; NM_001128613.2. [Q9BRQ3-3]
DR RefSeq; NP_001258760.1; NM_001271831.1.
DR RefSeq; NP_115720.1; NM_032344.3. [Q9BRQ3-1]
DR PDB; 5LF9; X-ray; 1.45 A; A=1-303.
DR PDB; 5LOR; X-ray; 2.19 A; A/B=1-303.
DR PDB; 5LOU; X-ray; 1.80 A; A/B=1-303.
DR PDB; 5R50; X-ray; 1.87 A; A=1-303.
DR PDB; 5R51; X-ray; 1.65 A; A=1-303.
DR PDB; 5R52; X-ray; 1.48 A; A=1-303.
DR PDB; 5R53; X-ray; 1.40 A; A=1-303.
DR PDB; 5R54; X-ray; 1.79 A; A=1-303.
DR PDB; 5R55; X-ray; 1.48 A; A=1-303.
DR PDB; 5R56; X-ray; 1.51 A; A=1-303.
DR PDB; 5R57; X-ray; 1.44 A; A=1-303.
DR PDB; 5R58; X-ray; 1.98 A; A=1-303.
DR PDB; 5R59; X-ray; 2.11 A; A=1-303.
DR PDB; 5R5A; X-ray; 1.44 A; A=1-303.
DR PDB; 5R5B; X-ray; 1.53 A; A=1-303.
DR PDB; 5R5C; X-ray; 1.68 A; A=1-303.
DR PDB; 5R5D; X-ray; 1.65 A; A=1-303.
DR PDB; 5R5E; X-ray; 1.58 A; A=1-303.
DR PDB; 5R5F; X-ray; 1.63 A; A=1-303.
DR PDB; 5R5G; X-ray; 1.77 A; A=1-303.
DR PDB; 5R5H; X-ray; 1.79 A; A=1-303.
DR PDB; 5R5I; X-ray; 1.70 A; A=1-303.
DR PDB; 5R5J; X-ray; 1.98 A; A=1-303.
DR PDB; 5R5K; X-ray; 1.60 A; A=1-303.
DR PDB; 5R5L; X-ray; 1.63 A; A=1-303.
DR PDB; 5R5M; X-ray; 1.60 A; A=1-303.
DR PDB; 5R5N; X-ray; 1.87 A; A=1-303.
DR PDB; 5R5O; X-ray; 1.79 A; A=1-303.
DR PDB; 5R5P; X-ray; 1.53 A; A=1-303.
DR PDB; 5R5Q; X-ray; 1.71 A; A=1-303.
DR PDB; 5R5R; X-ray; 1.65 A; A=1-303.
DR PDB; 5R5S; X-ray; 1.50 A; A=1-303.
DR PDB; 5RKZ; X-ray; 1.38 A; A=1-303.
DR PDBsum; 5LF9; -.
DR PDBsum; 5LOR; -.
DR PDBsum; 5LOU; -.
DR PDBsum; 5R50; -.
DR PDBsum; 5R51; -.
DR PDBsum; 5R52; -.
DR PDBsum; 5R53; -.
DR PDBsum; 5R54; -.
DR PDBsum; 5R55; -.
DR PDBsum; 5R56; -.
DR PDBsum; 5R57; -.
DR PDBsum; 5R58; -.
DR PDBsum; 5R59; -.
DR PDBsum; 5R5A; -.
DR PDBsum; 5R5B; -.
DR PDBsum; 5R5C; -.
DR PDBsum; 5R5D; -.
DR PDBsum; 5R5E; -.
DR PDBsum; 5R5F; -.
DR PDBsum; 5R5G; -.
DR PDBsum; 5R5H; -.
DR PDBsum; 5R5I; -.
DR PDBsum; 5R5J; -.
DR PDBsum; 5R5K; -.
DR PDBsum; 5R5L; -.
DR PDBsum; 5R5M; -.
DR PDBsum; 5R5N; -.
DR PDBsum; 5R5O; -.
DR PDBsum; 5R5P; -.
DR PDBsum; 5R5Q; -.
DR PDBsum; 5R5R; -.
DR PDBsum; 5R5S; -.
DR PDBsum; 5RKZ; -.
DR AlphaFoldDB; Q9BRQ3; -.
DR SMR; Q9BRQ3; -.
DR BioGRID; 124030; 25.
DR IntAct; Q9BRQ3; 22.
DR STRING; 9606.ENSP00000279206; -.
DR iPTMnet; Q9BRQ3; -.
DR PhosphoSitePlus; Q9BRQ3; -.
DR BioMuta; NUDT22; -.
DR DMDM; 317373407; -.
DR EPD; Q9BRQ3; -.
DR jPOST; Q9BRQ3; -.
DR MassIVE; Q9BRQ3; -.
DR MaxQB; Q9BRQ3; -.
DR PaxDb; Q9BRQ3; -.
DR PeptideAtlas; Q9BRQ3; -.
DR PRIDE; Q9BRQ3; -.
DR ProteomicsDB; 12190; -.
DR ProteomicsDB; 78802; -. [Q9BRQ3-1]
DR ProteomicsDB; 78803; -. [Q9BRQ3-2]
DR Antibodypedia; 51889; 91 antibodies from 18 providers.
DR DNASU; 84304; -.
DR Ensembl; ENST00000279206.8; ENSP00000279206.3; ENSG00000149761.9. [Q9BRQ3-1]
DR Ensembl; ENST00000441250.6; ENSP00000407970.2; ENSG00000149761.9. [Q9BRQ3-3]
DR GeneID; 84304; -.
DR KEGG; hsa:84304; -.
DR MANE-Select; ENST00000279206.8; ENSP00000279206.3; NM_032344.4; NP_115720.2.
DR UCSC; uc001nyp.6; human. [Q9BRQ3-1]
DR CTD; 84304; -.
DR GeneCards; NUDT22; -.
DR HGNC; HGNC:28189; NUDT22.
DR HPA; ENSG00000149761; Low tissue specificity.
DR neXtProt; NX_Q9BRQ3; -.
DR OpenTargets; ENSG00000149761; -.
DR PharmGKB; PA142671240; -.
DR VEuPathDB; HostDB:ENSG00000149761; -.
DR eggNOG; ENOG502QRSW; Eukaryota.
DR GeneTree; ENSGT00390000017869; -.
DR InParanoid; Q9BRQ3; -.
DR OMA; PEPQAVC; -.
DR OrthoDB; 1587403at2759; -.
DR PhylomeDB; Q9BRQ3; -.
DR TreeFam; TF106357; -.
DR PathwayCommons; Q9BRQ3; -.
DR SignaLink; Q9BRQ3; -.
DR BioGRID-ORCS; 84304; 16 hits in 1075 CRISPR screens.
DR ChiTaRS; NUDT22; human.
DR GenomeRNAi; 84304; -.
DR Pharos; Q9BRQ3; Tbio.
DR PRO; PR:Q9BRQ3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BRQ3; protein.
DR Bgee; ENSG00000149761; Expressed in mucosa of transverse colon and 162 other tissues.
DR ExpressionAtlas; Q9BRQ3; baseline and differential.
DR Genevisible; Q9BRQ3; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0052751; F:GDP-mannose hydrolase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IMP:UniProtKB.
DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IDA:UniProtKB.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..303
FT /note="Uridine diphosphate glucose pyrophosphatase NUDT22"
FT /id="PRO_0000263731"
FT DOMAIN 118..285
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 175..196
FT /note="Nudix box"
FT /evidence="ECO:0000305|PubMed:29413322"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:5LOR"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:5LOR"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:5LOR"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:5LOR"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:5LOR"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:5LOR"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:5LOR"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:29413322"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:29413322"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:5LOR"
FT VAR_SEQ 160..193
FT /note="QALCPGGSPQHQDLAGQLVVHELFSSVLQEICDE -> Q (in isoform
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053790"
FT VAR_SEQ 161..303
FT /note="ALCPGGSPQHQDLAGQLVVHELFSSVLQEICDEVNLPLLTLSQPLLLGIARN
FT ETSAGRASAEFYVQCSLTSEQVRKHYLSGGPEAHESTGIFFVETQNVQRLLETEMWAEL
FT CPSAKGAIILYNRVQGSPTGAALGSPALLPPL -> VRFQAGHKDPDSSRELQLSTLPI
FT LPALVSPSLKGKLAWYFSGSLLRAVHLPPH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_021884"
FT VARIANT 36
FT /note="G -> C (in dbSNP:rs2286612)"
FT /id="VAR_029616"
FT VARIANT 129
FT /note="T -> R (in dbSNP:rs34448455)"
FT /id="VAR_050414"
FT VARIANT 260
FT /note="Q -> R (in dbSNP:rs633561)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029617"
FT VARIANT 263
FT /note="L -> P (in dbSNP:rs633557)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029618"
FT MUTAGEN 156
FT /note="H->A: Abolishes enzyme activity with UDP-galactose."
FT /evidence="ECO:0000269|PubMed:29413322"
FT MUTAGEN 189
FT /note="E->A: Abolishes enzyme activity with UDP-galactose."
FT /evidence="ECO:0000269|PubMed:29413322"
FT MUTAGEN 193
FT /note="E->A: Abolishes enzyme activity with UDP-galactose."
FT /evidence="ECO:0000269|PubMed:29413322"
FT CONFLICT 9
FT /note="L -> V (in Ref. 1; AAQ15238)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:5RKZ"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:5RKZ"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:5RKZ"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:5RKZ"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:5RKZ"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:5RKZ"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:5RKZ"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:5RKZ"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:5RKZ"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5LOR"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5LOU"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5LF9"
FT HELIX 175..194
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:5RKZ"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5RKZ"
FT STRAND 219..229
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:5RKZ"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:5RKZ"
FT HELIX 273..285
FT /evidence="ECO:0007829|PDB:5RKZ"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:5RKZ"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:5RKZ"
SQ SEQUENCE 303 AA; 32580 MW; C26958E8BB90B02F CRC64;
MDPEVTLLLQ CPGGGLPQEQ IQAELSPAHD RRPLPGGDEA ITAIWETRLK AQPWLFDAPK
FRLHSATLAP IGSRGPQLLL RLGLTSYRDF LGTNWSSSAA WLRQQGATDW GDTQAYLADP
LGVGAALATA DDFLVFLRRS RQVAEAPGLV DVPGGHPEPQ ALCPGGSPQH QDLAGQLVVH
ELFSSVLQEI CDEVNLPLLT LSQPLLLGIA RNETSAGRAS AEFYVQCSLT SEQVRKHYLS
GGPEAHESTG IFFVETQNVQ RLLETEMWAE LCPSAKGAII LYNRVQGSPT GAALGSPALL
PPL
