ID PNKD_HUMAN Reviewed; 385 AA. AC Q8N490; A8K1F2; Q96A48; Q9BU26; Q9NSX4; Q9ULN6; Q9Y4T1; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 24-JAN-2024, entry version 155. DE RecName: Full=Probable hydrolase PNKD; DE EC=3.-.-.-; DE AltName: Full=Myofibrillogenesis regulator 1; DE Short=MR-1; DE AltName: Full=Paroxysmal nonkinesiogenic dyskinesia protein; DE AltName: Full=Trans-activated by hepatitis C virus core protein 2; GN Name=PNKD; Synonyms=KIAA1184, MR1, TAHCCP2; GN ORFNames=FKSG19, UNQ2491/PRO5778; 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] (ISOFORM 2), TISSUE SPECIFICITY, AND INTERACTION RP WITH MRLC2; MYOM1 AND ENO3. RX PubMed=15188056; DOI=10.1093/abbs/36.6.412; RA Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G., RA Gong L.-M.; RT "Characterization of MR-1, a novel myofibrillogenesis regulator in human RT muscle."; RL Acta Biochim. Biophys. Sin. 36:412-418(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION. RX PubMed=15188498; DOI=10.3748/wjg.v10.i12.1746; RA Liu M., Liu Y., Cheng J., Zhang S.-L., Wang L., Shao Q., Zhang J., Yang Q.; RT "Transactivating effect of hepatitis C virus core protein: a suppression RT subtractive hybridization study."; RL World J. Gastroenterol. 10:1746-1749(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Wang Y.-G., Gong L.; RT "Cloning of FKSG19, a novel gene expressed in ovarian tumour tissue."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). RA Liu Y., Cheng J., Wang G., Li K., Dong J., Li L., Chen J., Zhang L.; RT "Identification of human genomic DNA structure of the gene trans-activated RT by hepatitis C virus core protein 2."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Caudate nucleus; 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] (ISOFORMS 2 AND 4). RC TISSUE=Brain; 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 [8] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Brain; 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-385 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10574461; DOI=10.1093/dnares/6.5.329; RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.; RT "Characterization of cDNA clones selected by the GeneMark analysis from RT size-fractionated cDNA libraries from human brain."; RL DNA Res. 6:329-336(1999). RN [11] RP INVOLVEMENT IN DYT8. RX PubMed=16717228; DOI=10.1212/01.wnl.0000217332.51740.7c; RA Spacey S.D., Adams P.J., Lam P.C., Materek L.A., Stoessl A.J., Snutch T.P., RA Hsiung G.Y.; RT "Genetic heterogeneity in paroxysmal nonkinesigenic dyskinesia."; RL Neurology 66:1588-1590(2006). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [14] 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP VARIANTS DYT8 VAL-7 AND VAL-9, AND TISSUE SPECIFICITY. RX PubMed=15262732; DOI=10.1001/archneur.61.7.1025; RA Rainier S., Thomas D., Tokarz D., Ming L., Bui M., Plein E., Zhao X., RA Lemons R., Albin R., Delaney C., Alvarado D., Fink J.K.; RT "Myofibrillogenesis regulator 1 gene mutations cause paroxysmal dystonic RT choreoathetosis."; RL Arch. Neurol. 61:1025-1029(2004). RN [17] RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING. RX PubMed=15496428; DOI=10.1093/hmg/ddh330; RA Lee H.-Y., Xu Y., Huang Y., Ahn A.H., Auburger G.W., Pandolfo M., RA Kwiecinski H., Grimes D.A., Lang A.E., Nielsen J.E., Averyanov Y., RA Servidei S., Friedman A., Van Bogaert P., Abramowicz M.J., Bruno M.K., RA Sorensen B.F., Tang L., Fu Y.-H., Ptacek L.J.; RT "The gene for paroxysmal non-kinesigenic dyskinesia encodes an enzyme in a RT stress response pathway."; RL Hum. Mol. Genet. 13:3161-3170(2004). RN [18] RP VARIANTS DYT8 VAL-7 AND VAL-9. RX PubMed=15824259; DOI=10.1001/archneur.62.4.597; RA Chen D.-H., Matsushita M., Rainier S., Meaney B., Tisch L., Feleke A., RA Wolff J., Lipe H., Fink J., Bird T.D., Raskind W.H.; RT "Presence of alanine-to-valine substitutions in myofibrillogenesis RT regulator 1 in paroxysmal nonkinesigenic dyskinesia: confirmation in 2 RT kindreds."; RL Arch. Neurol. 62:597-600(2005). RN [19] RP VARIANT DYT8 VAL-9. RX PubMed=16972263; DOI=10.1002/mds.21095; RA Stefanova E., Djarmati A., Momcilovic D., Dragasevic N., Svetel M., RA Klein C., Kostic V.S.; RT "Clinical characteristics of paroxysmal nonkinesigenic dyskinesia in RT Serbian family with Myofibrillogenesis regulator 1 gene mutation."; RL Mov. Disord. 21:2010-2015(2006). RN [20] RP VARIANT DYT8 VAL-7. RX PubMed=16632198; DOI=10.1016/j.neulet.2006.03.048; RA Hempelmann A., Kumar S., Muralitharan S., Sander T.; RT "Myofibrillogenesis regulator 1 gene (MR-1) mutation in an Omani family RT with paroxysmal nonkinesigenic dyskinesia."; RL Neurosci. Lett. 402:118-120(2006). CC -!- FUNCTION: Probable hydrolase that plays an aggravative role in the CC development of cardiac hypertrophy via activation of the NF-kappa-B CC signaling pathway. {ECO:0000250}. CC -!- SUBUNIT: Isoform 2 interacts with the sarcomeric proteins, MRLC2, MYOM1 CC and ENO3. {ECO:0000269|PubMed:15188056}. CC -!- INTERACTION: CC Q8N490; Q7L273: KCTD9; NbExp=3; IntAct=EBI-746368, EBI-4397613; CC Q8N490; G5E962: MAGEA11; NbExp=3; IntAct=EBI-746368, EBI-11525615; CC Q8N490; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-746368, EBI-10178634; CC Q8N490; P27361: MAPK3; NbExp=4; IntAct=EBI-746368, EBI-73995; CC Q8N490-3; O14901: KLF11; NbExp=3; IntAct=EBI-25879276, EBI-948266; CC Q8N490-3; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-25879276, EBI-2811583; CC Q8N490-3; Q13153: PAK1; NbExp=3; IntAct=EBI-25879276, EBI-1307; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Peripheral membrane CC protein. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=MR-1L; CC IsoId=Q8N490-1; Sequence=Displayed; CC Name=2; Synonyms=MR-1S; CC IsoId=Q8N490-2; Sequence=VSP_027739, VSP_027740; CC Name=3; Synonyms=MR-1M; CC IsoId=Q8N490-3; Sequence=VSP_027736; CC Name=4; CC IsoId=Q8N490-4; Sequence=VSP_027737, VSP_027738; CC -!- TISSUE SPECIFICITY: Isoform 1 is only expressed in the brain. Isoform 2 CC is ubiquitously detected with highest expression in skeletal muscle and CC detected in myocardial myofibrils. Variant Val-7 and Val-9 are detected CC in the brain only. {ECO:0000269|PubMed:15188056, CC ECO:0000269|PubMed:15262732, ECO:0000269|PubMed:15496428}. CC -!- INDUCTION: By Hepatitis C virus core protein. CC {ECO:0000269|PubMed:15188498}. CC -!- DISEASE: Dystonia 8 (DYT8) [MIM:118800]: A paroxysmal non-kinesigenic CC dystonia/dyskinesia. Dystonia is defined by the presence of sustained CC involuntary muscle contractions, often leading to abnormal postures. CC Dystonia type 8 is characterized by attacks of involuntary movements CC brought on by stress, alcohol, fatigue or caffeine. The attacks CC generally last between a few seconds and four hours or longer. The CC attacks may begin in one limb and spread throughout the body, including CC the face. {ECO:0000269|PubMed:15262732, ECO:0000269|PubMed:15824259, CC ECO:0000269|PubMed:16632198, ECO:0000269|PubMed:16717228, CC ECO:0000269|PubMed:16972263}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC Glyoxalase II family. {ECO:0000305}. 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; AF417001; AAL08573.1; -; mRNA. DR EMBL; AY039043; AAK83449.1; -; mRNA. DR EMBL; AF318057; AAL25716.1; -; mRNA. DR EMBL; AF390031; AAM73649.1; -; Genomic_DNA. DR EMBL; AY358753; AAQ89113.1; -; mRNA. DR EMBL; AK289867; BAF82556.1; -; mRNA. DR EMBL; AL080092; CAB45707.2; -; mRNA. DR EMBL; AL137675; CAB70870.2; -; mRNA. DR EMBL; CH471063; EAW70602.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70604.1; -; Genomic_DNA. DR EMBL; BC002937; AAH02937.1; -; mRNA. DR EMBL; BC021118; AAH21118.1; -; mRNA. DR EMBL; BC036457; AAH36457.1; -; mRNA. DR EMBL; AB033010; BAA86498.1; -; mRNA. DR CCDS; CCDS2411.1; -. [Q8N490-1] DR CCDS; CCDS2413.1; -. [Q8N490-3] DR CCDS; CCDS42816.1; -. [Q8N490-2] DR PIR; T46495; T46495. DR RefSeq; NP_001070867.1; NM_001077399.2. [Q8N490-2] DR RefSeq; NP_056303.3; NM_015488.4. [Q8N490-1] DR RefSeq; NP_072094.1; NM_022572.4. [Q8N490-3] DR AlphaFoldDB; Q8N490; -. DR SMR; Q8N490; -. DR BioGRID; 117446; 140. DR IntAct; Q8N490; 101. DR MINT; Q8N490; -. DR STRING; 9606.ENSP00000273077; -. DR iPTMnet; Q8N490; -. DR PhosphoSitePlus; Q8N490; -. DR SwissPalm; Q8N490; -. DR BioMuta; PNKD; -. DR DMDM; 158563846; -. DR EPD; Q8N490; -. DR jPOST; Q8N490; -. DR MassIVE; Q8N490; -. DR MaxQB; Q8N490; -. DR PaxDb; 9606-ENSP00000273077; -. DR PeptideAtlas; Q8N490; -. DR ProteomicsDB; 71896; -. [Q8N490-1] DR ProteomicsDB; 71897; -. [Q8N490-2] DR ProteomicsDB; 71898; -. [Q8N490-3] DR ProteomicsDB; 71899; -. [Q8N490-4] DR Pumba; Q8N490; -. DR Antibodypedia; 2431; 148 antibodies from 25 providers. DR DNASU; 25953; -. DR Ensembl; ENST00000248451.7; ENSP00000248451.3; ENSG00000127838.15. [Q8N490-2] DR Ensembl; ENST00000258362.7; ENSP00000258362.3; ENSG00000127838.15. [Q8N490-3] DR Ensembl; ENST00000273077.9; ENSP00000273077.4; ENSG00000127838.15. [Q8N490-1] DR GeneID; 25953; -. DR KEGG; hsa:25953; -. DR MANE-Select; ENST00000273077.9; ENSP00000273077.4; NM_015488.5; NP_056303.3. DR UCSC; uc002vhm.2; human. [Q8N490-1] DR AGR; HGNC:9153; -. DR CTD; 25953; -. DR DisGeNET; 25953; -. DR GeneCards; PNKD; -. DR GeneReviews; PNKD; -. DR HGNC; HGNC:9153; PNKD. DR HPA; ENSG00000127838; Low tissue specificity. DR MalaCards; PNKD; -. DR MIM; 118800; phenotype. DR MIM; 609023; gene. DR neXtProt; NX_Q8N490; -. DR OpenTargets; ENSG00000127838; -. DR Orphanet; 98810; Paroxysmal non-kinesigenic dyskinesia. DR PharmGKB; PA33476; -. DR VEuPathDB; HostDB:ENSG00000127838; -. DR eggNOG; KOG0813; Eukaryota. DR GeneTree; ENSGT00940000158887; -. DR HOGENOM; CLU_1815131_0_0_1; -. DR InParanoid; Q8N490; -. DR OMA; CVWPGMR; -. DR OrthoDB; 5471651at2759; -. DR PhylomeDB; Q8N490; -. DR TreeFam; TF105273; -. DR PathwayCommons; Q8N490; -. DR SignaLink; Q8N490; -. DR BioGRID-ORCS; 25953; 19 hits in 1150 CRISPR screens. DR ChiTaRS; PNKD; human. DR GeneWiki; PNKD; -. DR GenomeRNAi; 25953; -. DR Pharos; Q8N490; Tbio. DR PRO; PR:Q8N490; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8N490; Protein. DR Bgee; ENSG00000127838; Expressed in metanephros cortex and 180 other cell types or tissues. DR ExpressionAtlas; Q8N490; baseline and differential. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl. DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro. DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IMP:SynGO-UCL. DR GO; GO:0050884; P:neuromuscular process controlling posture; IEA:Ensembl. DR GO; GO:0042053; P:regulation of dopamine metabolic process; IEA:Ensembl. DR GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; IEA:Ensembl. DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1. DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1. DR HAMAP; MF_01374; Glyoxalase_2; 1. DR InterPro; IPR035680; Clx_II_MBL. DR InterPro; IPR032282; HAGH_C. DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro. DR NCBIfam; TIGR03413; GSH_gloB; 1. DR PANTHER; PTHR11935; BETA LACTAMASE DOMAIN; 1. DR PANTHER; PTHR11935:SF116; HYDROLASE PNKD-RELATED; 1. DR Pfam; PF16123; HAGH_C; 1. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1. DR Genevisible; Q8N490; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Disease variant; Dystonia; Hydrolase; KW Membrane; Metal-binding; Mitochondrion; Nucleus; Reference proteome; Zinc. FT CHAIN 1..385 FT /note="Probable hydrolase PNKD" FT /id="PRO_0000299549" FT REGION 32..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 44..58 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 172 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 176 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 229 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 253 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 253 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 291..293 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 291 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 376..379 FT /ligand="substrate" FT /evidence="ECO:0000250" FT VAR_SEQ 1..79 FT /note="MAAVVAATALKGRGARNARVLRGILAGATANKASHNRTRALQSHSSPEGKEE FT PEPLSPELEYIPRKRGKNPMKAVGLAW -> MAWQGWPAAWQWVAGCWLLLVLVLVLLV FT SPRGCRARRGLRGLLMAHSQRLLFRIG (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:15489334" FT /id="VSP_027736" FT VAR_SEQ 1..60 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_027737" FT VAR_SEQ 61..78 FT /note="EYIPRKRGKNPMKAVGLA -> MPSSVHHTKRQMMSIYCY (in isoform FT 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_027738" FT VAR_SEQ 80..142 FT /note="YSLYTRTWLGYLFYRQQLRRARNRYPKGHSKTQPRLFNGVKVLPIPVLSDNY FT SYLIIDTQAQL -> AIGFPCGILLFILTKREVDKDRVKQMKARQNMRLSNTGEYESQR FT FRASSQSAPSPDVGSGVQT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15188056, FT ECO:0000303|PubMed:15188498, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3" FT /id="VSP_027739" FT VAR_SEQ 143..385 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15188056, FT ECO:0000303|PubMed:15188498, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3" FT /id="VSP_027740" FT VARIANT 7 FT /note="A -> V (in DYT8; dbSNP:rs121434512)" FT /evidence="ECO:0000269|PubMed:15262732, FT ECO:0000269|PubMed:15824259, ECO:0000269|PubMed:16632198" FT /id="VAR_034844" FT VARIANT 9 FT /note="A -> V (in DYT8; dbSNP:rs121434511)" FT /evidence="ECO:0000269|PubMed:15262732, FT ECO:0000269|PubMed:15824259, ECO:0000269|PubMed:16972263" FT /id="VAR_034845" FT CONFLICT 12 FT /note="G -> S (in Ref. 9; AAH36457)" FT /evidence="ECO:0000305" FT CONFLICT 33 FT /note="A -> V (in Ref. 9; AAH36457)" FT /evidence="ECO:0000305" FT CONFLICT 47 FT /note="P -> S (in Ref. 9; AAH36457)" FT /evidence="ECO:0000305" FT CONFLICT 377 FT /note="R -> L (in Ref. 7; CAB70870)" FT /evidence="ECO:0000305" SQ SEQUENCE 385 AA; 42876 MW; A4D631D3A4319A2C CRC64; MAAVVAATAL KGRGARNARV LRGILAGATA NKASHNRTRA LQSHSSPEGK EEPEPLSPEL EYIPRKRGKN PMKAVGLAWY SLYTRTWLGY LFYRQQLRRA RNRYPKGHSK TQPRLFNGVK VLPIPVLSDN YSYLIIDTQA QLAVAVDPSD PRAVQASIEK EGVTLVAILC THKHWDHSGG NRDLSRRHRD CRVYGSPQDG IPYLTHPLCH QDVVSVGRLQ IRALATPGHT QGHLVYLLDG EPYKGPSCLF SGDLLFLSGC GRTFEGNAET MLSSLDTVLG LGDDTLLWPG HEYAEENLGF AGVVEPENLA RERKMQWVQR QRLERKGTCP STLGEERSYN PFLRTHCLAL QEALGPGPGP TGDDDYSRAQ LLEELRRLKD MHKSK //