KDM3A_CHICK
ID KDM3A_CHICK Reviewed; 1325 AA.
AC Q5ZIX8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Lysine-specific demethylase 3A;
DE EC=1.14.11.65 {ECO:0000250|UniProtKB:Q9Y4C1};
DE AltName: Full=JmjC domain-containing histone demethylation protein 2A;
DE AltName: Full=Jumonji domain-containing protein 1A;
DE AltName: Full=[histone H3]-dimethyl-L-lysine(9) demethylase 3A {ECO:0000305};
GN Name=KDM3A; Synonyms=JHDM2A, JMJD1A; ORFNames=RCJMB04_22o22;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of
CC histone H3, thereby playing a central role in histone code.
CC Preferentially demethylates mono- and dimethylated H3 'Lys-9' residue,
CC with a preference for dimethylated residue, while it has weak or no
CC activity on trimethylated H3 'Lys-9'. Demethylation of Lys residue
CC generates formaldehyde and succinate (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000250|UniProtKB:Q9Y4C1};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC the demethylation activity. {ECO:0000250}.
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the
CC association with nuclear receptors. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; AJ720656; CAG32315.1; -; mRNA.
DR RefSeq; NP_001012909.1; NM_001012891.1.
DR AlphaFoldDB; Q5ZIX8; -.
DR SMR; Q5ZIX8; -.
DR STRING; 9031.ENSGALP00000036346; -.
DR PaxDb; Q5ZIX8; -.
DR GeneID; 422917; -.
DR KEGG; gga:422917; -.
DR CTD; 55818; -.
DR VEuPathDB; HostDB:geneid_422917; -.
DR eggNOG; KOG1356; Eukaryota.
DR InParanoid; Q5ZIX8; -.
DR OrthoDB; 1185631at2759; -.
DR PhylomeDB; Q5ZIX8; -.
DR PRO; PR:Q5ZIX8; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1325
FT /note="Lysine-specific demethylase 3A"
FT /id="PRO_0000234370"
FT DOMAIN 1062..1285
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 669..694
FT /note="C6-type"
FT /evidence="ECO:0000255"
FT REGION 249..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 888..892
FT /note="LXXLL motif"
FT COMPBIAS 249..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 1325 AA; 149333 MW; 9F4699CEE1960776 CRC64;
MVLRLEGSWS LLVGKRFLSL SGDDDGPWDT ERVAEWPWQA GRIRAVSHTD ISKPDLKICV
EFDDESWEKR RWIEVYSPKM KVFLVEQKLV LAERRSHGGS ISPVQWPAMT YKSLVDKAGL
GPMVSIRYLG EEKCVFLSKD LLTPIQDVES SRLPLKDDQT VNEEIQALVK KHLDETRLVQ
GGKNIIGSKI RIYSLDPSTQ WFTAVVVNGN PATRTLEVNC QEIPALKTLD PELIHVEIIY
DNNGKCDKSK RIGGVKRKPS ENSGSVDAKH TKSSPEVSQS QGHVHSVPTV FGEALLGCTP
ANKDQRHQGL PLPANSPPNL GAETPQGTCR RSVPEVHPSC LNAGTKPLKE NLTLFPKVTY
ITKEQTQNIN DQNGKYTSLI SSRSSSLSDS TNGKETGLKN ISEPLLKPTT NFPKECISAK
PLQHLNSSIA IPRVNSSVEL QRTLDCRPST SDAHLLPFTE AGVRSHSGSN SQKGNKVDEH
VEMEFFTRRN SNEAFYERNE NESFWTGSTK IQDNVIVRKS ILADASKVKK LQQSGEAFVQ
DGSCNNIAPH LHKCRECRLD SYRKNKDQKD STVFCRFFHF RRLQFNKHGI LREEGFLTPN
KYDPEAISLW LPLSKNVVGL DLDTAKYILA NIGDHFCQLV ISEKEVMSTI EPHRQVAWKR
AVRGVREMCD VCDTTIFNLR WVCSKCGFGV CVDCYRMRKK GIHEDDDSDT FSWFKCVKGQ
EHEPENLMPT QIIPGRALYD VGDIVHSVRT KWGIKANCPC ANKQFKALSK PTLKEDSKQN
LVPGERTSLQ QSNLVLSPQL PTHEPPVKPA AGSKQTASVT TSPSLSWLSN ITSGNVNKEN
KEKLLVPISK NENKALQTLP SLAKPAAALQ TFNSAILTPV SNNNTGFLRN LLNSSGGKTD
NGLKSTPKIL DDIFASLVQN RTVTDMPKKP QGLTIKPTIM GFDTPHYWLC DNRLLCLQDP
NNESNWNVFR ECWKQGQPVM VSGVHHKLNA DLWRPESFRK EFGQQEVDLV NCRTNEIITG
ATVGDFWDGF EDISSRLRTE EGEPMVLKLK DWPPGEDFRD MMPSRFDDLM KNIPLPEYTR
RGGKLNLASR LPNYFVRPDL GPKMYNAYGL ITPEDRKYGT TNLHLDVSDA ANVMVYVGIP
KGQADQEEEV LKTIQDGDSD ELTIKRFTES REKPGALWHI YAAKDTEKIR EFLKKVAEEQ
GQENPVDHDP IHDQSWYLDR SLRKRLHQEY GVQGWAIVQF LGDVVFIPAG APHQVHNLYS
CIKVAEDFVS PEHVKHCFWL TQEFRYLSHT HTNHEDKLQV KNVIYHAVKD AVGILRANES
SLSRS
