LSD1_SCHPO
ID LSD1_SCHPO Reviewed; 1000 AA.
AC Q9Y802; Q9UTV0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Lysine-specific histone demethylase 1;
DE EC=1.-.-.-;
GN Name=lsd1; Synonyms=saf110, swm1; ORFNames=SPBC146.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 694-873, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, INTERACTION WITH LSD2, AND SUBCELLULAR LOCATION.
RX PubMed=16990277; DOI=10.1074/jbc.m606349200;
RA Nicolas E., Lee M.G., Hakimi M.-A., Cam H.P., Grewal S.I.S.,
RA Shiekhattar R.;
RT "Fission yeast homologs of human histone H3 lysine 4 demethylase regulate a
RT common set of genes with diverse functions.";
RL J. Biol. Chem. 281:35983-35988(2006).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE SWM HISTONE DEMETHYLASE COMPLEX, AND
RP INTERACTION WITH LSD2.
RX PubMed=17434129; DOI=10.1016/j.molcel.2007.02.023;
RA Lan F., Zaratiegui M., Villen J., Vaughn M.W., Verdel A., Huarte M.,
RA Shi Y., Gygi S.P., Moazed D., Martienssen R.A., Shi Y.;
RT "S. pombe LSD1 homologs regulate heterochromatin propagation and
RT euchromatic gene transcription.";
RL Mol. Cell 26:89-101(2007).
RN [6]
RP IDENTIFICATION IN THE SWM HISTONE DEMETHYLASE COMPLEX, AND FUNCTION OF THE
RP SWM COMPLEX.
RX PubMed=17440621; DOI=10.1371/journal.pone.0000386;
RA Opel M., Lando D., Bonilla C., Trewick S.C., Boukaba A., Walfridsson J.,
RA Cauwood J., Werler P.J., Carr A.M., Kouzarides T., Murzina N.V.,
RA Allshire R.C., Ekwall K., Laue E.D.;
RT "Genome-wide studies of histone demethylation catalysed by the fission
RT yeast homologues of mammalian LSD1.";
RL PLoS ONE 2:E386-E386(2007).
CC -!- FUNCTION: Catalytic component of the SWM histone demethylase complex
CC that specifically demethylates H3K9me2, a specific tag for epigenetic
CC transcriptional activation, thereby acting as a corepressor. Acts by
CC oxidizing the substrate by FAD to generate the corresponding imine that
CC is subsequently hydrolyzed. Has a role in regulating heterochromatin
CC propagation and euchromatic transcription. Also has a gene activating
CC role. {ECO:0000269|PubMed:16990277, ECO:0000269|PubMed:17434129,
CC ECO:0000269|PubMed:17440621}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBUNIT: Component of the SWM histone demethylase complex composed of
CC at least lsd1, lsd2, phf1 and phf2. Interacts directly with lsd2.
CC {ECO:0000269|PubMed:16990277, ECO:0000269|PubMed:17434129,
CC ECO:0000269|PubMed:17440621}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:16990277}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB46762.1; -; Genomic_DNA.
DR EMBL; AB027980; BAA87284.1; -; Genomic_DNA.
DR PIR; T39423; T39423.
DR RefSeq; NP_595398.1; NM_001021305.2.
DR AlphaFoldDB; Q9Y802; -.
DR SMR; Q9Y802; -.
DR BioGRID; 276355; 10.
DR STRING; 4896.SPBC146.09c.1; -.
DR iPTMnet; Q9Y802; -.
DR MaxQB; Q9Y802; -.
DR PaxDb; Q9Y802; -.
DR PRIDE; Q9Y802; -.
DR EnsemblFungi; SPBC146.09c.1; SPBC146.09c.1:pep; SPBC146.09c.
DR GeneID; 2539805; -.
DR KEGG; spo:SPBC146.09c; -.
DR PomBase; SPBC146.09c; lsd1.
DR VEuPathDB; FungiDB:SPBC146.09c; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_1_2_1; -.
DR InParanoid; Q9Y802; -.
DR OMA; KTQWHVC; -.
DR PhylomeDB; Q9Y802; -.
DR BRENDA; 1.14.11.65; 5613.
DR PRO; PR:Q9Y802; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0033193; C:Lsd1/2 complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; NAS:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; IDA:PomBase.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IMP:PomBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IMP:PomBase.
DR GO; GO:0016570; P:histone modification; IEA:UniProt.
DR GO; GO:0071515; P:mating-type locus imprinting; IMP:PomBase.
DR GO; GO:1902681; P:regulation of replication fork arrest at rDNA repeats; IMP:PomBase.
DR GO; GO:0011000; P:replication fork arrest at mating type locus; IMP:PomBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; DNA-binding; FAD; Flavoprotein; Nucleus;
KW Oxidoreductase; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1000
FT /note="Lysine-specific histone demethylase 1"
FT /id="PRO_0000363001"
FT DOMAIN 153..249
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DNA_BIND 841..921
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 104..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..950
FT /note="Demethylase activity"
FT /evidence="ECO:0000250"
FT REGION 780..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..137
FT /evidence="ECO:0000255"
FT COILED 434..529
FT /evidence="ECO:0000255"
FT COMPBIAS 959..978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 260..302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 328..329
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 908..909
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1000 AA; 112829 MW; 4E97DD0145FD4211 CRC64;
MMDLSSKDAL SDVLKDTHAQ SSDPSLWAIF GHQSSDNVHE GGNESVSVEQ EIFDLSQLSE
RPVSETVSKA SIPTNINGLS QVKPSALEKS QEVLSLQKLP IKGRRPAGRR GRPALNTSNS
LERNGTRYVS AEAPISVKSS IPAIPRVTFE RLCYESAIAS NLPPNALSPL EAEMLSEILE
NPTWLSLYLS IRNGICYLWH RNPTLYVSFN EALGIVREKK AFPLASLAFE FLSRNGHINY
GCIYIISSLK LDESLSQKTV AIIGAGMAGI SCARQLTNLF AQYEQDFLSR GEKPPRIVIY
EASERLGGHI YTHMVPLSDN EVSEKSSLAT TVNATNECMV NLLTDSLIGM PTLDSDPLYI
ISSQQLSLDA VHTRNREFIL HDIENGRIDT EHVQRIFRLF DALLFYFNAS ASKQPLHSLI
TPPEQEFIQK LDQIGWYISI EAFPLQIKDT LSEFLGNSAN TLTSLLHLTV LDLKIFEWFK
EYLSQSLSVS LENVYPGSIP NLNLLLGENV ASYSFKHGMA DMLNSLASTP SPLPILFDQC
VHTVKLEDNT VNLSFVNETT VSVDKVVICI PMDKLNTHLI TFEPPLEEKK LKAIDRCHFT
NVKKVILIFK TQFWEPNISI FGSLPQDSGR NFIFNDCTRF YEHPTLSVFV KVEGIDFMKD
DDIVNGIVSQ LKKVYKPKSE AINPIRTIIS NWENNSYTNH SSYQISNLFL EEDYAILSEP
IDNTVFFASE AISQKNSGSI RGAFDSGILA ARDVLASLIG NVVLPNTLVI EENLEQPRKT
YGTKRNAQQA LGKEGERENK EKRISYHTEY LRLRQKRLDK EQQECDLLIA ELLGPSPVPP
SRPSANPYLL YQKTQWHVCK TLADQDKQRV TGDPEARATK NEIRAKLGKT WRALDSLGKQ
PWVDEINARR ANYSTRLEEY QRQINSYNVR VAQIKSEHQR RCESQPIPED EAKLKLLAEQ
EDEHLHPEKE GMSVENSDDD YHDDLDYEDS ISEVFPDNFS
