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Database: UniProt
Entry: H3DIP9_TETNG
LinkDB: H3DIP9_TETNG
Original site: H3DIP9_TETNG 
ID   H3DIP9_TETNG            Unreviewed;       840 AA.
AC   H3DIP9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Lysine-specific histone demethylase {ECO:0000256|PIRNR:PIRNR038051};
DE            EC=1.14.99.66 {ECO:0000256|PIRNR:PIRNR038051};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000020393.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000020393.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Histone demethylase that can demethylate both 'Lys-4'
CC       (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a
CC       coactivator or a corepressor, depending on the context. Acts by
CC       oxidizing the substrate by FAD to generate the corresponding imine that
CC       is subsequently hydrolyzed. Acts as a corepressor by mediating
CC       demethylation of H3K4me, a specific tag for epigenetic transcriptional
CC       activation. Demethylates both mono- (H3K4me1) and di-methylated
CC       (H3K4me2) H3K4me. May play a role in the repression of neuronal genes.
CC       Alone, it is unable to demethylate H3K4me on nucleosomes and requires
CC       the presence of RCOR1/CoREST to achieve such activity.
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|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR038051}.
CC   -!- DOMAIN: The SWIRM domain may act as an anchor site for a histone tail.
CC       {ECO:0000256|PIRNR:PIRNR038051}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|PIRNR:PIRNR038051}.
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DR   AlphaFoldDB; H3DIP9; -.
DR   STRING; 99883.ENSTNIP00000020393; -.
DR   Ensembl; ENSTNIT00000020625.1; ENSTNIP00000020393.1; ENSTNIG00000017255.1.
DR   GeneTree; ENSGT00940000157193; -.
DR   HOGENOM; CLU_004498_5_1_1; -.
DR   InParanoid; H3DIP9; -.
DR   OMA; SSRGEMF; -.
DR   TreeFam; TF312972; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IEA:UniProt.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 1.10.287.80; ATP synthase, gamma subunit, helix hairpin domain; 1.
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:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 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|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR038051};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR038051}; Nucleus {ECO:0000256|PIRNR:PIRNR038051};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR038051};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW   Repressor {ECO:0000256|PIRNR:PIRNR038051};
KW   Transcription {ECO:0000256|PIRNR:PIRNR038051};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR038051}.
FT   DOMAIN          154..253
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   REGION          1..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          420..500
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         261..289
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         290
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         296
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         312..313
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         787
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         796..797
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
SQ   SEQUENCE   840 AA;  92738 MW;  0E25E9E4E242B9EC CRC64;
     CGSFDQERPP TSSMMLSSKK SDAAEATGGE RVLVSDAMSG PSVSTIGPMD VKKKERSSPS
     GEAGGPPLPH QAGPGGVDPD SAEVRRTSRR KRAKVEYREM DESLANLSED EYYSEEERNA
     KAEKERKQVI PPPAPPVEEE NDSEPEEPSG RSGVEGAAFQ SRLPHDRMTS QEAACFPDII
     SGPQQTQKVF LYIRNRTLQL WLDNPKIQLT FEATAQQLEA PYNSDAVLVH RIHSYLERHG
     LINFGIYKRV KPLPTKKTGK VIVIGGGVSG LAAARQLQSF GMDVTVLEAR DRVGGRVATF
     RKGNYVADLG AMVVTGLGGN PMAVISKQVN MELAKIKQKC PLYEANGQAG ERCTSVPKEK
     DEMVEQEFNR LLEATSFLSH QLDFNFLNNK PVSLGQALEV VIQLQEKHVK DEQIEHWKKI
     VKTQEELRDL LNKMVNTKER VKELHQQYKE ASEVKPPRDI TAEFLVKSKH RDLTALCKEY
     DELVELQAKL EEKLQELEAN PPSDVYLSSR DRQILDWHFA NLEFANATPL STLSLKHWDQ
     DDDFEFTGSH LTVRNGYSCV PVALAEGLDI KLNTAVRQVR YTASGCEVIA VNTRSTTQTF
     IYKCDAVLCT LPLGVLKQQP PAVQFVPPLP EWKTSAIQRM GFGNLNKVVL CFDRVFWDPS
     VNLFGHVGST TASRGELFLF WNLYKAPILL ALMAGEAAGI MENISDDVIV GRCLAILKGI
     FGSSAVPQPK ETVVTRWRAD PWARGSYSYV AAGSSGNDYD LMAQPITPGP AIPGASQPVP
     RLFFAGEHTI RNYPATVHGA LLSGREAGRI ADQFLGAMYT LPRQATPTAS SNPQQAQPAP
//
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