GenomeNet

Database: UniProt
Entry: Q22343_CAEEL
LinkDB: Q22343_CAEEL
Original site: Q22343_CAEEL 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system