PNKD_MOUSE
ID PNKD_MOUSE Reviewed; 385 AA.
AC Q69ZP3; Q3TLE6; Q6PD45; Q8BRV8; Q920D4; Q9CSF5; Q9D765; Q9JJA3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
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;
GN Name=Pnkd; Synonyms=Brp17, Kiaa1184, Mr1, Tahccp2;
GN ORFNames=Fksg19, MNCb-5687;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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 [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RA Hu Y., Li T., Wang Y.;
RT "Cloning and functional analysis of Mus musculus myofibrillogenesis
RT regulator 1 (MR-1).";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] (PARTIAL ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 TISSUE SPECIFICITY.
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 [9]
RP TRANSGENIC MICE, AND FUNCTION.
RX PubMed=17420335; DOI=10.1161/hypertensionaha.106.085399;
RA Li H.-L., She Z.-G., Li T.-B., Wang A.-B., Yang Q., Wei Y.-S., Wang Y.-G.,
RA Liu D.-P.;
RT "Overexpression of myofibrillogenesis regulator-1 aggravates cardiac
RT hypertrophy induced by angiotensin II in mice.";
RL Hypertension 49:1399-1408(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000269|PubMed:17420335}.
CC -!- SUBUNIT: Isoform 2 interacts with the sarcomeric proteins, MRLC2, MYOM1
CC and ENO3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Peripheral membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q69ZP3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZP3-2; Sequence=VSP_027743, VSP_027744;
CC Name=3;
CC IsoId=Q69ZP3-3; Sequence=VSP_027742;
CC Name=4;
CC IsoId=Q69ZP3-4; Sequence=VSP_027741;
CC -!- TISSUE SPECIFICITY: Expressed in many discrete areas of the brain.
CC {ECO:0000269|PubMed:15496428}.
CC -!- INDUCTION: By Hepatitis C virus core protein.
CC {ECO:0000269|PubMed:15188498}.
CC -!- MISCELLANEOUS: Mice overexpressing Pnkd infused with angiotensin II
CC develop greater cardiac hypertrophy as well as increased cardiac
CC inflammation and fibrosis, compared with angiotensin II-infused normal
CC mice. In these mice, Pnkd overexpression promote nuclear factor kappa B
CC activation.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30873.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD32403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY039041; AAK83447.1; -; mRNA.
DR EMBL; AY039042; AAK83448.1; -; Genomic_DNA.
DR EMBL; AB041609; BAA95092.1; -; mRNA.
DR EMBL; AF318058; AAL25717.1; -; mRNA.
DR EMBL; AY299972; AAP58373.1; -; mRNA.
DR EMBL; AK173125; BAD32403.1; ALT_INIT; mRNA.
DR EMBL; AK009545; BAB26351.1; -; mRNA.
DR EMBL; AK012976; BAB28577.2; -; mRNA.
DR EMBL; AK041238; BAC30873.1; ALT_INIT; mRNA.
DR EMBL; AK166548; BAE38846.1; -; mRNA.
DR EMBL; BC008274; AAH08274.1; -; mRNA.
DR EMBL; BC058945; AAH58945.1; -; mRNA.
DR EMBL; BC116236; AAI16237.1; -; mRNA.
DR EMBL; BC116237; AAI16238.1; -; mRNA.
DR CCDS; CCDS15045.1; -. [Q69ZP3-4]
DR CCDS; CCDS35613.1; -. [Q69ZP3-1]
DR CCDS; CCDS35614.1; -. [Q69ZP3-2]
DR RefSeq; NP_001034598.1; NM_001039509.1. [Q69ZP3-1]
DR RefSeq; NP_064383.1; NM_019999.2. [Q69ZP3-4]
DR RefSeq; NP_079856.2; NM_025580.2.
DR AlphaFoldDB; Q69ZP3; -.
DR SMR; Q69ZP3; -.
DR STRING; 10090.ENSMUSP00000027370; -.
DR iPTMnet; Q69ZP3; -.
DR PhosphoSitePlus; Q69ZP3; -.
DR SwissPalm; Q69ZP3; -.
DR EPD; Q69ZP3; -.
DR jPOST; Q69ZP3; -.
DR MaxQB; Q69ZP3; -.
DR PaxDb; Q69ZP3; -.
DR PeptideAtlas; Q69ZP3; -.
DR PRIDE; Q69ZP3; -.
DR ProteomicsDB; 289705; -. [Q69ZP3-1]
DR ProteomicsDB; 289706; -. [Q69ZP3-2]
DR ProteomicsDB; 289707; -. [Q69ZP3-3]
DR ProteomicsDB; 289708; -. [Q69ZP3-4]
DR Antibodypedia; 2431; 135 antibodies from 25 providers.
DR DNASU; 56695; -.
DR Ensembl; ENSMUST00000027370; ENSMUSP00000027370; ENSMUSG00000026179. [Q69ZP3-1]
DR Ensembl; ENSMUST00000087225; ENSMUSP00000084477; ENSMUSG00000026179. [Q69ZP3-4]
DR Ensembl; ENSMUST00000087226; ENSMUSP00000084478; ENSMUSG00000026179. [Q69ZP3-3]
DR GeneID; 56695; -.
DR KEGG; mmu:56695; -.
DR UCSC; uc007bls.1; mouse. [Q69ZP3-2]
DR UCSC; uc007blt.1; mouse. [Q69ZP3-1]
DR UCSC; uc007blu.1; mouse. [Q69ZP3-3]
DR UCSC; uc007blw.1; mouse. [Q69ZP3-4]
DR CTD; 25953; -.
DR MGI; MGI:1930773; Pnkd.
DR VEuPathDB; HostDB:ENSMUSG00000026179; -.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00940000158887; -.
DR HOGENOM; CLU_030571_4_3_1; -.
DR InParanoid; Q69ZP3; -.
DR OMA; CVWPGMR; -.
DR OrthoDB; 961826at2759; -.
DR PhylomeDB; Q69ZP3; -.
DR TreeFam; TF105273; -.
DR BioGRID-ORCS; 56695; 4 hits in 69 CRISPR screens.
DR ChiTaRS; Pnkd; mouse.
DR PRO; PR:Q69ZP3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q69ZP3; protein.
DR Bgee; ENSMUSG00000026179; Expressed in embryonic brain and 227 other tissues.
DR ExpressionAtlas; Q69ZP3; baseline and differential.
DR Genevisible; Q69ZP3; MM.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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; IGI:MGI.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; IMP:MGI.
DR GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; IMP:MGI.
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; Hydrolase; Membrane; Metal-binding;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..385
FT /note="Probable hydrolase PNKD"
FT /id="PRO_0000299550"
FT REGION 32..56
FT /note="Disordered"
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="MAAVVAATALKGRGARNARVLRGILSGATANKASQNRTRALQSHSSPECKEE
FT PEPLSPELEYIPRKRGKNPMKAVGLAW -> MAWQGWLAPWLWVSGCWLLFFAFVLLLS
FT PRSCQEQRGFRGLLMTRSQRLLFRIG (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_027741"
FT VAR_SEQ 79
FT /note="W -> WAIGFPCGILFFVLTKQEVDKDRLKQMKARQNMRVSNTGE (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027742"
FT VAR_SEQ 80..142
FT /note="YSLYTRTWLGYLFYRQQLRRARNRYPKGHSKTQPRLFNGVKVLPIPVLSDNY
FT SYLIIDTQAGL -> AIGFPCGILFFVLTKQEVDKDRLKQMKARQNMRVSNTGEYESQR
FT YRASPQQAQFPEVGSGAQT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15188498,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_027743"
FT VAR_SEQ 143..385
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15188498,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_027744"
FT CONFLICT 17
FT /note="N -> H (in Ref. 3; AAL25717)"
FT /evidence="ECO:0000305"
FT MOD_RES Q69ZP3-2:121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 385 AA; 43017 MW; 2327D63BFDDA849A CRC64;
MAAVVAATAL KGRGARNARV LRGILSGATA NKASQNRTRA LQSHSSPECK EEPEPLSPEL
EYIPRKRGKN PMKAVGLAWY SLYTRTWLGY LFYRQQLRRA RNRYPKGHSK TQPRLFNGVK
VLPIPVLSDN YSYLIIDTQA GLAVAVDPSD PRAVQASIEK ERVNLVAILC THKHWDHSGG
NRDLSRRHRD CRVYGSPQDG IPYLTHPLCH QDVVSVGRLQ IRALATPGHT QGHLVYLLDG
EPYKGPSCLF SGDLLFLSGC GRTFEGTAET MLSSLDTVLD LGDDTLLWPG HEYAEENLGF
AGVVEPENLA RERKMQWVQR QRMERKSTCP STLGEERAYN PFLRTHCLEL QEALGPGPGP
TSDDGCSRAQ LLEELRRLKD MHKSK
