ID   KD3AB_XENLA             Reviewed;        1334 AA.
AC   Q5HZN1;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Lysine-specific demethylase 3A-B;
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-B;
DE   AltName: Full=[histone H3]-dimethyl-L-lysine(9) demethylase 3A-B {ECO:0000305};
GN   Name=kdm3a-b; Synonyms=jhdm2a-b, jmjd1a-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
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; BC088951; AAH88951.1; -; mRNA.
DR   RefSeq; NP_001088971.1; NM_001095502.1.
DR   AlphaFoldDB; Q5HZN1; -.
DR   SMR; Q5HZN1; -.
DR   BioGRID; 106431; 1.
DR   IntAct; Q5HZN1; 1.
DR   DNASU; 496351; -.
DR   GeneID; 496351; -.
DR   KEGG; xla:496351; -.
DR   CTD; 496351; -.
DR   Xenbase; XB-GENE-1012805; kdm3a.S.
DR   OrthoDB; 1185631at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 496351; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0033169; P:histone H3-K9 demethylation; IEA:InterPro.
DR   InterPro; IPR045109; JHDM2-like.
DR   InterPro; IPR003347; JmjC_dom.
DR   PANTHER; PTHR12549; PTHR12549; 2.
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..1334
FT                   /note="Lysine-specific demethylase 3A-B"
FT                   /id="PRO_0000234372"
FT   DOMAIN          1089..1294
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   ZN_FING         684..709
FT                   /note="C6-type"
FT                   /evidence="ECO:0000255"
FT   REGION          243..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           897..901
FT                   /note="LXXLL motif"
FT   COMPBIAS        243..280
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1133
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         1135
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         1262
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ   SEQUENCE   1334 AA;  149945 MW;  DDC24504C21104B2 CRC64;
     MVLTQQENLS VLVGQRFVCL LGKDLQVDPD TVSKWPWKSG IVRAASHKDL HCPEIKIFVE
     YDDESWENRT WLELYGPTVK MFLVEHNLVL ADHASPSNPS VSVQCPAMVY KVLVGKFSLG
     STACLQFLGE KDKVFLSKEL VKPVRDRETL KQFMQDNKTF NKAFQELIRK SVDESRLLQA
     ARNIISMPIN VYSMDPSMQW FSGTITNVRT ASRALEIKCE QLPSLKIIDP ALLHVVLVHN
     YGDQNDKSKK PRASKRKSQD TESEDQTEVK QTRNEEVPSK DVTQKTSFLT YRRDDGKTLV
     VVDNPKATTN NLFNYMTPAT EDQQKVQQSL SSKQSVPVGF GETLLGCAAT TPGIQNAATP
     PPANSPPSFG AATPQGKGSQ NLPGDTTVLN GDANREETNL FLSAAASQGN KRSMGFGIME
     SPSTFSSLST MPSWSGQPNS ENGLKSENLF AAFTKSSTVF PKGFEFSVKS FPEQKMLSVT
     DSPKTALQKT CVPQQEQNVI RKPENNHTSV KAIKPQEPPY TKSPNKTDGV TYPKSILLNP
     QKLKRLQQSG DCFVQDGSCN NIAPHLHKCR ECRLDRFGRS REQRDSAVFC RFFHFRRLHF
     NKHGMLKEGG FLTPNKYDAE AINLWLPLAS SVVDLDLDTA KYILANIGDH FCKLVMSEKE
     VMSSTDPSKQ VAWKRAVRGV REMCDACDTT IFNLHWVCPK CGFGVCVDCY RMRKKSLSSG
     EEGNEMFSWL KCMKGQLHEP ENLMPTQIVP GKALYDVCDI VHSVRGRWGI KSNCSCSNKH
     MRPVSKPVVK EEVKPSTPEP EPIKSLLAQP NVCTVPDPPA IPNKPPTPAC SSPLSWLTNF
     PQTIVNKENK DNLFASTSKS EHKPLPSFAS FGKPVSALQT FGSSILTPTT SNNSGFLRNL
     LNASTLKQET SDKSTPKILD DIFASLVQSR PLSDFDRKPQ GLPIQPSLMG FNTPHYWLCD
     NRLLCLQDPN NKSNWNVFRE CWKQGQPVMV SGVHNNLNSE LWRPESFRRE FGDQEADLVN
     CRTNDIITGA TVGDFWDGFE DIPGRLKNDT GESMVLKLKD WPPGEDFRDT MLSRFEDLMN
     NIPLPEYTRR EGKLNLAARL PTYFVRPDLG PKMYNAYGLI TPEDRKYGTT NLHLDVSDAA
     NVMVYVGIPK GEHDQDQEVL RTIQDGDADE LTIKRFIEFK EKPGALWHIY AAKDTEKIRQ
     FLKKVAEEEG HENPPDHDPI HDQSWYLDNI LRKRLLQEHG VQGWAIVQFL GDAVFIPAGA
     PHQVHNLYSC IKVAEDFVSP EHVKHCFCLT QEFRYLSHTH TNHEDKLQVK NVIYHAVKDS
     IAILKANESS LGKL