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   02-SEP-2026, entry version 137.
DE   RecName: Full=Probable thioesterase PNKD {ECO:0000250|UniProtKB:Q8N490};
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:Q8N490};
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 thioesterase that may play a role in cellular
CC       detoxification processes; it likely acts on a yet-unknown alpha-
CC       hydroxythioester substrate. In vitro, it is able to catalyze the
CC       hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic
CC       acid at very low rate, though this reaction is not physiologically
CC       relevant in vivo. {ECO:0000250|UniProtKB:Q8N490}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a thioester + H2O = a thiol + a carboxylate + H(+);
CC         Xref=Rhea:RHEA:82919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:29256, ChEBI:CHEBI:51277;
CC         Evidence={ECO:0000250|UniProtKB:Q8N490};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q16775};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q16775};
CC   -!- SUBUNIT: Isoform 2 interacts with the sarcomeric proteins, MRLC2, MYOM1
CC       and ENO3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC       {ECO:0000250|UniProtKB:Q8N490}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q8N490}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q8N490}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8N490}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q8N490}.
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   -!- PTM: Undergoes cleavage at the N-terminus.
CC       {ECO:0000250|UniProtKB:Q8N490}.
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   BioGRID; 208125; 1.
DR   FunCoup; Q69ZP3; 93.
DR   STRING; 10090.ENSMUSP00000027370; -.
DR   GlyGen; Q69ZP3; 2 sites.
DR   iPTMnet; Q69ZP3; -.
DR   PhosphoSitePlus; Q69ZP3; -.
DR   SwissPalm; Q69ZP3; -.
DR   jPOST; Q69ZP3; -.
DR   PaxDb; 10090-ENSMUSP00000027370; -.
DR   PeptideAtlas; Q69ZP3; -.
DR   ProteomicsDB; 289705; -. [Q69ZP3-1]
DR   ProteomicsDB; 289706; -. [Q69ZP3-2]
DR   ProteomicsDB; 289707; -. [Q69ZP3-3]
DR   ProteomicsDB; 289708; -. [Q69ZP3-4]
DR   Pumba; Q69ZP3; -.
DR   Antibodypedia; 2431; 132 antibodies from 26 providers.
DR   DNASU; 56695; -.
DR   Ensembl; ENSMUST00000027370.13; ENSMUSP00000027370.7; ENSMUSG00000026179.15. [Q69ZP3-1]
DR   Ensembl; ENSMUST00000087225.6; ENSMUSP00000084477.6; ENSMUSG00000026179.15. [Q69ZP3-4]
DR   Ensembl; ENSMUST00000087226.11; ENSMUSP00000084478.5; ENSMUSG00000026179.15. [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   AGR; MGI:1930773; -.
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; 32047at9989; -.
DR   PhylomeDB; Q69ZP3; -.
DR   BioGRID-ORCS; 56695; 4 hits in 74 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:Q69ZP3; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q69ZP3; protein.
DR   Bgee; ENSMUSG00000026179; Expressed in embryonic brain and 230 other cell types or tissues.
DR   ExpressionAtlas; Q69ZP3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:GO_Central.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR   GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:InterPro.
DR   GO; GO:0051596; P:methylglyoxal catabolic process; 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   FunFam; 3.60.15.10:FF:000015; probable hydrolase PNKD isoform X1; 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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Hydrolase; Membrane;
KW   Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..385
FT                   /note="Probable thioesterase PNKD"
FT                   /id="PRO_0000299550"
FT   REGION          32..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..42
FT                   /note="Polar 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|UniProtKB:Q16775"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
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
//