ID A0A182R6Z2_ANOFN Unreviewed; 872 AA.
AC A0A182R6Z2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Lysine-specific histone demethylase {ECO:0000256|PIRNR:PIRNR038051};
DE EC=1.14.99.66 {ECO:0000256|PIRNR:PIRNR038051};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN001940-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN001940-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN001940-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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|ARBA:ARBA00005995, ECO:0000256|PIRNR:PIRNR038051}.
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DR AlphaFoldDB; A0A182R6Z2; -.
DR STRING; 62324.A0A182R6Z2; -.
DR EnsemblMetazoa; AFUN001940-RA; AFUN001940-PA; AFUN001940.
DR VEuPathDB; VectorBase:AFUN001940; -.
DR VEuPathDB; VectorBase:AFUN2_008375; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000075900; 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:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
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; 2.
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 FAD {ECO:0000256|PIRNR:PIRNR038051, ECO:0000256|PIRSR:PIRSR038051-1};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR038051};
KW Nucleus {ECO:0000256|PIRNR:PIRNR038051};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR038051};
KW Repressor {ECO:0000256|PIRNR:PIRNR038051};
KW Transcription {ECO:0000256|PIRNR:PIRNR038051};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR038051}.
FT DOMAIN 132..231
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..267
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 268
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 274
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 290..291
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 827
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 836..837
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
SQ SEQUENCE 872 AA; 96175 MW; FC760C531AF6C282 CRC64;
MNGTTVAEQT RDDSGTAMDA VETVTLISDD SDVEMTDISV KRPSKSESDE GRRTSRRKKV
KVGYGDNGAK TNTATRPGSA CESGDPSGTG DRKGEGGTKP DPPTPKSKKR ETEEKSTTGP
DPNPYQELMT GLEGAAFQSR LPVDKMTAAE AVCFPHIIKH GLVTQRMFLN VRNRILQMWI
EEPTVQLTFE NALKKMESPF DSDPSLVRKV HAFLERHGFI NFGIFERLKP LPVKKHAKVI
VIGAGISGLA AARQLQQFGF DVIVLEARDR VGGRIATFRK NAYTADLGAM VVTGIWGNPL
TILSKQTGME MCPIKSTCPL YGAGGKPVPK HKDDMVEREF NRLLEATSYL SHQLDFNYAG
NHPVSLGQAL EWIIKLQEKH VKEKQVQHLA GIIGWQQKLL TNQHQLVETL ARIKDLKMKA
QHLIDTKPPK PPPSTKEGGG SGGATHDATG GDSTGSGKYY EHEFQLRVNA REEQLAWKEV
ERLQTYQTEV ETKVRELENE QVSEVYLSSK DRQILDWHFA NLEFANATPL SNLSLKHWDQ
DDDFEFIGSH TTVKNGYSCV PIALTENLDV RVNTAVTCIR YRPGGVEVTA DLKSNNSSVC
YRADLVLCTL TLGILKLAIA DESKQLNTVR FDPPLPEWKQ SAIRRLGFGN LNKVVLCFDR
IFWDPNTNLF GHVGSTTASR GELFLFWNIS QSPVLLALVA GQSAAIMENV SDDVIVGRCI
AVLKGIFGNS AVPQPKETVV TRWRADPWAR GSYSFVSVGS SGSDYDLLAA PVTPKAPDGE
AQATKPPAPQ QNPQQRHDKN GEKNENEDDG GDDGSPIDIP RLFFAGEHTI RNYPATVHGA
LLSGLREAGR IADYYLGFPN CYPEAPKEET KK
//
