LSD1_ARATH
ID LSD1_ARATH Reviewed; 189 AA.
AC P94077; C0Z316; Q8RXL2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein LSD1;
DE AltName: Full=Protein CHILLING SENSITIVE 4;
DE AltName: Full=Protein LESION SIMULATING DISEASE 1;
DE Short=AtLSD1;
DE AltName: Full=Putative zinc finger LSD1;
GN Name=LSD1; Synonyms=CHS4; OrderedLocusNames=At4g20380; ORFNames=F9F13.30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=cv. Wassilewskija;
RX PubMed=9054508; DOI=10.1016/s0092-8674(00)81911-x;
RA Dietrich R.A., Richberg M.H., Schmidt R., Dean C., Dangl J.L.;
RT "A novel zinc finger protein is encoded by the Arabidopsis LSD1 gene and
RT functions as a negative regulator of plant cell death.";
RL Cell 88:685-694(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=10550898; DOI=10.1094/mpmi.1999.12.11.1022;
RA Kliebenstein D.J., Dietrich R.A., Martin A.C., Last R.L., Dangl J.L.;
RT "LSD1 regulates salicylic acid induction of copper zinc superoxide
RT dismutase in Arabidopsis thaliana.";
RL Mol. Plant Microbe Interact. 12:1022-1026(1999).
RN [8]
RP FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11595797; DOI=10.2307/3871503;
RA Rusterucci C., Aviv D.H., Holt B.F. III, Dangl J.L., Parker J.E.;
RT "The disease resistance signaling components EDS1 and PAD4 are essential
RT regulators of the cell death pathway controlled by LSD1 in Arabidopsis.";
RL Plant Cell 13:2211-2224(2001).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11844114; DOI=10.1046/j.0960-7412.2001.01225.x;
RA Aviv D.H., Rusterucci C., Holt B.F. III, Dietrich R.A., Parker J.E.,
RA Dangl J.L.;
RT "Runaway cell death, but not basal disease resistance, in lsd1 is SA- and
RT NIM1/NPR1-dependent.";
RL Plant J. 29:381-391(2002).
RN [10]
RP FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12732715; DOI=10.1073/pnas.1130421100;
RA Epple P., Mack A.A., Morris V.R., Dangl J.L.;
RT "Antagonistic control of oxidative stress-induced cell death in Arabidopsis
RT by two related, plant-specific zinc finger proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6831-6836(2003).
RN [11]
RP INTERACTION WITH BZIP63.
RX PubMed=15469500; DOI=10.1111/j.1365-313x.2004.02219.x;
RA Walter M., Chaban C., Schuetze K., Batistic O., Weckermann K., Naeke C.,
RA Blazevic D., Grefen C., Schumacher K., Oecking C., Harter K., Kudla J.;
RT "Visualization of protein interactions in living plant cells using
RT bimolecular fluorescence complementation.";
RL Plant J. 40:428-438(2004).
RN [12]
RP FUNCTION.
RX PubMed=15347794; DOI=10.1104/pp.104.043646;
RA Mateo A., Muhlenbock P., Rusterucci C., Chang C.C., Miszalski Z.,
RA Karpinska B., Parker J.E., Mullineaux P.M., Karpinski S.;
RT "LESION SIMULATING DISEASE 1 is required for acclimation to conditions that
RT promote excess excitation energy.";
RL Plant Physiol. 136:2818-2830(2004).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BZIP10.
RX PubMed=16957775; DOI=10.1038/sj.emboj.7601312;
RA Kaminaka H., Naeke C., Epple P., Dittgen J., Schuetze K., Chaban C.,
RA Holt B.F. III, Merkle T., Schaefer E., Harter K., Dangl J.L.;
RT "bZIP10-LSD1 antagonism modulates basal defense and cell death in
RT Arabidopsis following infection.";
RL EMBO J. 25:4400-4411(2006).
RN [14]
RP FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=18055613; DOI=10.1105/tpc.106.048843;
RA Muehlenbock P., Plaszczyca M., Plaszczyca M., Mellerowicz E., Karpinski S.;
RT "Lysigenous aerenchyma formation in Arabidopsis is controlled by LESION
RT SIMULATING DISEASE1.";
RL Plant Cell 19:3819-3830(2007).
RN [15]
RP FUNCTION.
RX PubMed=18790826; DOI=10.1105/tpc.108.059618;
RA Muehlenbock P., Szechynska-Hebda M., Plaszczyca M., Baudo M., Mateo A.,
RA Mullineaux P.M., Parker J.E., Karpinska B., Karpinski S.;
RT "Chloroplast signaling and LESION SIMULATING DISEASE1 regulate crosstalk
RT between light acclimation and immunity in Arabidopsis.";
RL Plant Cell 20:2339-2356(2008).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY METHYL VIOLOGEN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20456049; DOI=10.1111/j.1469-8137.2010.03275.x;
RA Huang X., Li Y., Zhang X., Zuo J., Yang S.;
RT "The Arabidopsis LSD1 gene plays an important role in the regulation of low
RT temperature-dependent cell death.";
RL New Phytol. 187:301-312(2010).
RN [17]
RP FUNCTION, AND INTERACTION WITH AMC1.
RX PubMed=21097903; DOI=10.1126/science.1194980;
RA Coll N.S., Vercammen D., Smidler A., Clover C., Van Breusegem F.,
RA Dangl J.L., Epple P.;
RT "Arabidopsis type I metacaspases control cell death.";
RL Science 330:1393-1397(2010).
RN [18]
RP INTERACTION WITH GILP.
RX PubMed=21526181; DOI=10.1371/journal.pone.0018750;
RA He S., Tan G., Liu Q., Huang K., Ren J., Zhang X., Yu X., Huang P., An C.;
RT "The LSD1-interacting protein GILP is a LITAF domain protein that
RT negatively regulates hypersensitive cell death in Arabidopsis.";
RL PLoS ONE 6:E18750-E18750(2011).
RN [19]
RP MISCELLANEOUS.
RX PubMed=21811563; DOI=10.1371/journal.pone.0022131;
RA He S., Huang K., Zhang X., Yu X., Huang P., An C.;
RT "The LSD1-type zinc finger motifs of Pisum sativa LSD1 are a novel nuclear
RT localization signal and interact with importin alpha.";
RL PLoS ONE 6:E22131-E22131(2011).
RN [20]
RP INTERACTION WITH CAT1; CAT2 AND CAT3.
RX PubMed=23958864; DOI=10.1104/pp.113.225805;
RA Li Y., Chen L., Mu J., Zuo J.;
RT "LESION SIMULATING DISEASE1 interacts with catalases to regulate
RT hypersensitive cell death in Arabidopsis.";
RL Plant Physiol. 163:1059-1070(2013).
CC -!- FUNCTION: Negative regulator of reactive oxygen-induced cell death,
CC cold stress-induced cell death, pathogen-induced hypersensitive
CC response (HR), basal disease resistance. May be involved in the
CC induction of the copper/zinc superoxide dismutase CSD1 and CSD2 that
CC detoxify accumulating superoxide before the reactive oxygen species
CC (ROS) can trigger a cell death cascade. LSD1 and LOL1 have antagonistic
CC effects on CSD1 and CSD2 accumulation to regulate oxidative stress-
CC induced cell death. Antagonizes the function of BZIP10, a positive
CC regulator of cell death, by interacting in the cytoplasm and preventing
CC its nuclear localization. Controls lysigenous aerenchyma in hypocotyls
CC under root hypoxia. Required for leaf acclimation in response to excess
CC excitation energy. {ECO:0000269|PubMed:10550898,
CC ECO:0000269|PubMed:11595797, ECO:0000269|PubMed:11844114,
CC ECO:0000269|PubMed:12732715, ECO:0000269|PubMed:15347794,
CC ECO:0000269|PubMed:16957775, ECO:0000269|PubMed:18055613,
CC ECO:0000269|PubMed:18790826, ECO:0000269|PubMed:20456049,
CC ECO:0000269|PubMed:21097903}.
CC -!- SUBUNIT: Interacts with BZIP10 and AMC1 (via N-terminus). Binds to
CC BZIP63. Interacts with CAT1, CAT2 and CAT3 in a zinc-finger-dependent
CC manner (PubMed:23958864). Interacts (via N-terminus) with GILP
CC (PubMed:21526181). {ECO:0000269|PubMed:15469500,
CC ECO:0000269|PubMed:16957775, ECO:0000269|PubMed:21097903,
CC ECO:0000269|PubMed:21526181, ECO:0000269|PubMed:23958864}.
CC -!- INTERACTION:
CC P94077; Q7XJE6: AMC1; NbExp=3; IntAct=EBI-5849461, EBI-5849501;
CC P94077; O80748: B-box domain protein 26; NbExp=3; IntAct=EBI-5849461, EBI-15191535;
CC P94077; Q8S944: DRP3A; NbExp=7; IntAct=EBI-5849461, EBI-2265428;
CC P94077; Q8LFT2: DRP3B; NbExp=3; IntAct=EBI-5849461, EBI-2265511;
CC P94077; Q94ID6: ERF12; NbExp=3; IntAct=EBI-5849461, EBI-4446727;
CC P94077; Q94CD4: GILP; NbExp=3; IntAct=EBI-5849461, EBI-6274018;
CC P94077; Q4PSE2: NFYC8; NbExp=4; IntAct=EBI-5849461, EBI-15191571;
CC P94077; Q8L4B2: NFYC9; NbExp=4; IntAct=EBI-5849461, EBI-2466050;
CC P94077; Q9FNN6: SRM1; NbExp=5; IntAct=EBI-5849461, EBI-15195055;
CC P94077; Q8W245: ZIP10; NbExp=3; IntAct=EBI-5849461, EBI-6956003;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16957775}. Nucleus
CC {ECO:0000269|PubMed:16957775}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P94077-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P94077-2; Sequence=VSP_041104;
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, roots, rosette leaves,
CC stems, inflorescences and flowers. {ECO:0000269|PubMed:20456049}.
CC -!- INDUCTION: By methyl viologen. {ECO:0000269|PubMed:20456049}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, however cold treatment induces the development of yellowish
CC leaves with necrosis, and treatment with salicylic acid or infection
CC with avirulent pathogen causes a runaway cell death and plant death.
CC {ECO:0000269|PubMed:11844114, ECO:0000269|PubMed:20456049}.
CC -!- MISCELLANEOUS: When expressed in Arabidopsis, Pisum sativa LSD1
CC interacts with importin alpha via the LSD1-type zinc finger motifs,
CC suggesting that the nuclear import of LSD1 may rely on the interaction
CC between its zinc finger motifs and importin alpha.
CC {ECO:0000269|PubMed:21811563}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH57095.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; U87833; AAC49660.1; -; mRNA.
DR EMBL; U87834; AAC49661.1; -; Genomic_DNA.
DR EMBL; AL080253; CAB45804.1; -; Genomic_DNA.
DR EMBL; AL161553; CAB79038.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84315.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84316.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84317.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84318.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84319.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84320.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84321.1; -; Genomic_DNA.
DR EMBL; AY080824; AAL87301.1; -; mRNA.
DR EMBL; AY117316; AAM51391.1; -; mRNA.
DR EMBL; AK318980; BAH57095.1; ALT_SEQ; mRNA.
DR EMBL; AY087794; AAM65330.1; -; mRNA.
DR PIR; T10580; T10580.
DR RefSeq; NP_001031678.1; NM_001036601.1. [P94077-2]
DR RefSeq; NP_001031679.1; NM_001036602.2. [P94077-2]
DR RefSeq; NP_001031680.2; NM_001036603.2. [P94077-2]
DR RefSeq; NP_001078413.1; NM_001084944.2. [P94077-1]
DR RefSeq; NP_567599.3; NM_118157.5. [P94077-2]
DR RefSeq; NP_849548.1; NM_179217.4. [P94077-2]
DR RefSeq; NP_849549.1; NM_179218.4. [P94077-1]
DR AlphaFoldDB; P94077; -.
DR BioGRID; 13077; 33.
DR IntAct; P94077; 69.
DR MINT; P94077; -.
DR PRIDE; P94077; -.
DR ProteomicsDB; 238780; -. [P94077-1]
DR EnsemblPlants; AT4G20380.1; AT4G20380.1; AT4G20380. [P94077-2]
DR EnsemblPlants; AT4G20380.2; AT4G20380.2; AT4G20380. [P94077-1]
DR EnsemblPlants; AT4G20380.3; AT4G20380.3; AT4G20380. [P94077-2]
DR EnsemblPlants; AT4G20380.4; AT4G20380.4; AT4G20380. [P94077-2]
DR EnsemblPlants; AT4G20380.5; AT4G20380.5; AT4G20380. [P94077-2]
DR EnsemblPlants; AT4G20380.6; AT4G20380.6; AT4G20380. [P94077-2]
DR EnsemblPlants; AT4G20380.7; AT4G20380.7; AT4G20380. [P94077-1]
DR GeneID; 827786; -.
DR Gramene; AT4G20380.1; AT4G20380.1; AT4G20380. [P94077-2]
DR Gramene; AT4G20380.2; AT4G20380.2; AT4G20380. [P94077-1]
DR Gramene; AT4G20380.3; AT4G20380.3; AT4G20380. [P94077-2]
DR Gramene; AT4G20380.4; AT4G20380.4; AT4G20380. [P94077-2]
DR Gramene; AT4G20380.5; AT4G20380.5; AT4G20380. [P94077-2]
DR Gramene; AT4G20380.6; AT4G20380.6; AT4G20380. [P94077-2]
DR Gramene; AT4G20380.7; AT4G20380.7; AT4G20380. [P94077-1]
DR KEGG; ath:AT4G20380; -.
DR Araport; AT4G20380; -.
DR InParanoid; P94077; -.
DR PhylomeDB; P94077; -.
DR PRO; PR:P94077; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P94077; baseline and differential.
DR Genevisible; P94077; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IGI:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR InterPro; IPR040319; LSD1-like.
DR InterPro; IPR005735; Znf_LSD1.
DR PANTHER; PTHR31747; PTHR31747; 1.
DR Pfam; PF06943; zf-LSD1; 3.
DR TIGRFAMs; TIGR01053; LSD1; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; Hypersensitive response;
KW Nucleus; Plant defense; Reference proteome.
FT CHAIN 1..189
FT /note="Protein LSD1"
FT /id="PRO_0000408483"
FT REGION 9..39
FT /note="LSD1-type zinc-finger"
FT /evidence="ECO:0000255"
FT REGION 50..80
FT /note="LSD1-type zinc-finger"
FT /evidence="ECO:0000255"
FT REGION 97..127
FT /note="LSD1-type zinc-finger"
FT /evidence="ECO:0000255"
FT REGION 136..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..5
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:19423640, ECO:0000303|Ref.6"
FT /id="VSP_041104"
SQ SEQUENCE 189 AA; 20107 MW; 5EBEE628A30F1550 CRC64;
MKVADMQDQL VCHGCRNLLM YPRGASNVRC ALCNTINMVP PPPPPHDMAH IICGGCRTML
MYTRGASSVR CSCCQTTNLV PAHSNQVAHA PSSQVAQINC GHCRTTLMYP YGASSVKCAV
CQFVTNVNMS NGRVPLPTNR PNGTACPPST STSTPPSQTQ TVVVENPMSV DESGKLVSNV
VVGVTTDKK
