ID Q22343_CAEEL Unreviewed; 737 AA.
AC Q22343;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 2.
DT 24-JAN-2024, entry version 164.
DE RecName: Full=Lysine-specific histone demethylase {ECO:0000256|PIRNR:PIRNR038051};
DE EC=1.14.99.66 {ECO:0000256|PIRNR:PIRNR038051};
GN Name=lsd-1 {ECO:0000313|EMBL:CAA90637.2,
GN ECO:0000313|WormBase:T08D10.2};
GN ORFNames=CELE_T08D10.2 {ECO:0000313|EMBL:CAA90637.2}, T08D10.2
GN {ECO:0000313|WormBase:T08D10.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA90637.2, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA90637.2, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA90637.2,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of
CC histone H3, a specific tag for epigenetic transcriptional activation,
CC thereby acting as a corepressor. Acts by oxidizing the substrate by FAD
CC to generate the corresponding imine that is subsequently hydrolyzed.
CC Demethylates both mono- and di-methylated 'Lys-4' of histone H3.
CC {ECO:0000256|PIRNR:PIRNR038051}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2
CC AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60244,
CC Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:61976; EC=1.14.99.66;
CC Evidence={ECO:0000256|PIRNR:PIRNR038051};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR038051,
CC ECO:0000256|PIRSR:PIRSR038051-1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038051}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|PIRNR:PIRNR038051}.
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DR EMBL; BX284606; CAA90637.2; -; Genomic_DNA.
DR PIR; T24685; T24685.
DR RefSeq; NP_510000.2; NM_077599.4.
DR AlphaFoldDB; Q22343; -.
DR SMR; Q22343; -.
DR STRING; 6239.T08D10.2.1; -.
DR EPD; Q22343; -.
DR PaxDb; 6239-T08D10-2; -.
DR EnsemblMetazoa; T08D10.2.1; T08D10.2.1; WBGene00011615.
DR GeneID; 181369; -.
DR UCSC; T08D10.2; c. elegans.
DR AGR; WB:WBGene00011615; -.
DR WormBase; T08D10.2; CE33174; WBGene00011615; lsd-1.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000172632; -.
DR HOGENOM; CLU_004498_5_1_1; -.
DR InParanoid; Q22343; -.
DR OMA; KMAHHAS; -.
DR OrthoDB; 5402444at2759; -.
DR PhylomeDB; Q22343; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00011615; Expressed in embryo and 4 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IEA:UniProt.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR017366; Hist_Lys-spec_deMease.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF351; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1-RELATED; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR PIRSF; PIRSF038051; Histone_Lys-demethylase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR038051};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW FAD {ECO:0000256|PIRNR:PIRNR038051, ECO:0000256|PIRSR:PIRSR038051-1};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR038051};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|PIRNR:PIRNR038051};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR038051};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repressor {ECO:0000256|PIRNR:PIRNR038051};
KW Transcription {ECO:0000256|PIRNR:PIRNR038051};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR038051};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 143..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..168
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 369..403
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 212
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 682
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
SQ SEQUENCE 737 AA; 82386 MW; 97A4A84F5A1D327E CRC64;
MASGTRRKAN DDSQSSSEGS SSTTPQFIPQ VPFDFNLGSI NEEVDDSNGL TGIASVPKDI
LTPLRDHYSL AEVARRHGIS ADRPTEIEAA FFPEVQMSRS FSDVFLMIRN TTLSIWLASA
TTECTAEDVI KHLTPPYNTE IHLVQNIVLF LSRFGMINIG FFFPKTELVN NMEKKFVVVI
GAGAAGIAAA TQLLTFGFDV AVVEASGLTG GRVRSLISKH GELIETGCDS LRNLDESVIT
TLLHQVPLNE NIMSENTIVF SKGKYVPVAR CHVINGLYAN LKAGLAHASH GPEQRGENGL
YISRQQAYEN YFNMIERSTL LSYYNFAKEK VNLNAERKHL YEVLKTNRLT ALLAEQKLKN
TPPSDELLLK SLQIDIEKAI RQFDEACERF EICEERIADL EKNPRCKQSM HPNDFIHYNF
LLGFEERLFG AQLEKVQFSC NVNELKLKSQ VARVQEGLAQ VLINVANERK VKIHHNQRVI
EIDTGSSDAV ILKLRKPDGS VGILNADYVV STLPIGVLKK TIIGDERAPV FRPPLPKSKF
AAIRSLGNGL INKIVFVFET RFWPESINQF AIVPDKISER AAMFTWSSLP ESRTLTTHYV
GENRFHDTPV TELITKALEM LKTVFKDCPS PIDAYVTNWH TDELAFGTGT FMSLRTEPQH
FDALKEPLKT RDGKPRVFFA GEHTSALEHG TLDGAFNSGL RAAADLANTC IEIPFINRSR
DLIFPPYPRA RYSNEGD
//