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Database: UniProt
Entry: G3TYK0_LOXAF
LinkDB: G3TYK0_LOXAF
Original site: G3TYK0_LOXAF 
ID   G3TYK0_LOXAF            Unreviewed;       814 AA.
AC   G3TYK0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Lysine-specific histone demethylase {ECO:0000256|PIRNR:PIRNR038051};
DE            EC=1.14.99.66 {ECO:0000256|PIRNR:PIRNR038051};
GN   Name=KDM1A {ECO:0000313|Ensembl:ENSLAFP00000020658.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000020658.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000020658.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000020658.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000020658.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000020658.1};
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; G3TYK0; -.
DR   Ensembl; ENSLAFT00000036581.1; ENSLAFP00000020658.1; ENSLAFG00000007981.3.
DR   GeneTree; ENSGT00940000157193; -.
DR   HOGENOM; CLU_004498_5_1_1; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IEA:RHEA.
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:UP000007646};
KW   Repressor {ECO:0000256|PIRNR:PIRNR038051};
KW   Transcription {ECO:0000256|PIRNR:PIRNR038051};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR038051}.
FT   DOMAIN          136..235
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   REGION          1..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          396..430
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        67..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         243..271
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         272
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         278
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         294..295
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         763
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         772..773
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
SQ   SEQUENCE   814 AA;  89573 MW;  C28BB0EA4BA07EB5 CRC64;
     TGSAALSAVG GQATRDVVGT EAGSGAAGGT ENGSEGERTP RKKEPQAGPT VVPGSATPME
     TGIAETPEGR RTSRRKRAKV EYREMDESLA NLSEDEYYSE EERNAKAEKE KKLPPPPPQA
     PPEEENESEP EEPSGVEGAA FQSRLPHDRM TSQEAACFPD IISGPQQTQK VFLFIRNRTL
     QLWLDNPKIQ LTFEAALQQL EAPCNGDTVL VHRVHSYLER HGLINFGIYK RIKPLPTKKT
     GKVIIIGSGV SGLAAARQLQ SFGMDVTLLE ARDRVGGRVA TFRKGNYVAD LGAMVVTGLG
     GNPMAVVSKQ VNMELAKIKQ KCPLYEANGQ AVPKEKDEMV EQEFNRLLEA TSYLSHQLDF
     NVLNNKPVSL GQALEVVIQL QEKHVKDEQI EHWKKIVKTQ EELKELLNKM VNLKEKIKEL
     HQQYKEASEV KPPRDITAEF LVKSKHRDLT ALCKEYDELA ETQGKLEEKL QELEANPPSD
     VYLSSRDRQI LDWHFANLEF ANATPLSTLS LKHWDQDDDF EFTGSHLTVR NGYSCVPVAL
     AEGLDIKLNT AVRQVRYTAS GCEVIAVNTR STSQTFIYKC DAVLCTLPLG VLKQQPPAVQ
     FVPPLPEWKT SAVQRMGFGN LNKVVLCFDR VFWDPSVNLF GHVGSTTASR GELFLFWNLY
     KAPILLALVA GEAAGIMENI SDDVIVGRCL AILKGIFGSS AVPQPKETVV SRWRADPWAR
     GSYSYVAAGS SGNDYDLMAQ PITPGPSIPG APQPIPRLFF AGEHTIRNYP ATVHGALLSG
     LREAGRIADQ FLGAMYTLPR QATPGVPAQQ SPSM
//
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