PNKD_HUMAN
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 03-AUG-2022, entry version 147.
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}.
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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; 139.
DR IntAct; Q8N490; 100.
DR MINT; Q8N490; -.
DR STRING; 9606.ENSP00000273077; -.
DR iPTMnet; Q8N490; -.
DR PhosphoSitePlus; Q8N490; -.
DR BioMuta; PNKD; -.
DR DMDM; 158563846; -.
DR EPD; Q8N490; -.
DR jPOST; Q8N490; -.
DR MassIVE; Q8N490; -.
DR MaxQB; Q8N490; -.
DR PaxDb; Q8N490; -.
DR PeptideAtlas; Q8N490; -.
DR PRIDE; Q8N490; -.
DR ProteomicsDB; 71896; -. [Q8N490-1]
DR ProteomicsDB; 71897; -. [Q8N490-2]
DR ProteomicsDB; 71898; -. [Q8N490-3]
DR ProteomicsDB; 71899; -. [Q8N490-4]
DR Antibodypedia; 2431; 135 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 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; 961826at2759; -.
DR PhylomeDB; Q8N490; -.
DR TreeFam; TF105273; -.
DR PathwayCommons; Q8N490; -.
DR SignaLink; Q8N490; -.
DR BioGRID-ORCS; 25953; 17 hits in 1081 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 178 other tissues.
DR ExpressionAtlas; Q8N490; baseline and differential.
DR Genevisible; Q8N490; HS.
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:0016787; F:hydrolase activity; IBA:GO_Central.
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; -; 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 Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
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
