KD3AA_XENLA
ID KD3AA_XENLA Reviewed; 1331 AA.
AC Q6IRB8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Lysine-specific demethylase 3A-A;
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-A;
DE AltName: Full=[histone H3]-dimethyl-L-lysine(9) demethylase 3A-A {ECO:0000305};
GN Name=kdm3a-a; Synonyms=jhdm2a-a, jmjd1a-a;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) 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; BC070982; AAH70982.1; -; mRNA.
DR RefSeq; NP_001085045.1; NM_001091576.1.
DR AlphaFoldDB; Q6IRB8; -.
DR SMR; Q6IRB8; -.
DR DNASU; 432112; -.
DR GeneID; 432112; -.
DR KEGG; xla:432112; -.
DR CTD; 432112; -.
DR Xenbase; XB-GENE-6256006; kdm3a.L.
DR OrthoDB; 1185631at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 432112; 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..1331
FT /note="Lysine-specific demethylase 3A-A"
FT /id="PRO_0000234371"
FT DOMAIN 1086..1291
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 683..708
FT /note="C6-type"
FT /evidence="ECO:0000255"
FT REGION 243..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 894..898
FT /note="LXXLL motif"
FT COMPBIAS 243..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 1331 AA; 149611 MW; F768E8D685558847 CRC64;
MVLTQQENLS VLVGQRFTCL LGTDLQLDPD GVSKWPWKSG IVRAASHKDL HCPEIKIFVE
FDDEAWEKRT WIELYGATVK MFLVEHNLVL ADRVSPSNSV PVQCPAMVYK VLVGKFSLGT
ATCLQFLGDK DKLFLSKELV KPVRDRETLK QFMQENKTFN KAFQELIRKS VDESRLQQAT
RNIIGMPINV YSMDPSMQWF SATISNVRTA SRALEIKCEQ LPSLKIIDPA LLHVVLVHNY
GDLNDKSRKP RAPKRKSQDT ESEDQTELKQ TRNEEVPSKD VTQKTSFLTY RRDDGKTLVV
VDNPKATNNL FNYINTTTED QQKVQQQSLS SKQSVPVGFG EALLGCAATT PGILNAATPP
QANSPPSFGA ATPQGKGTQN LPGDTTLLNG EAKREETNLF LSAAASQGNK RSLGFGMMES
PSTFSSLSSM PSWSGQPKSE NGPKSENLFA AFTNSSTVFP KGFEFSVKSF PEQKMLSVTD
SPKTAPPMTC VQQQEQKVVK KPENNHTSVR AIKPQEPPYP KSPNKNDGVT YPRSILLDPQ
KLKRLQQSGD CFVQDGSCND IAPHLHKCRE CRLDRFGRSR EQRDSAVFCR FFHFRRLHFN
KHGMLKEGGF LTPNKYDAEA INLWLPLASN VVDLDLDTAK YILANIGDHF CKLVMSEKEV
MSATDPSKQV AWKRAVRGVR EMCDACDTTI FNLHWVCPKC GFGVCVDCYR MKKKSLSSGE
DGNETFSWLK CVKGQLHEPE NLMPTQIVPG KALYDVGDIV HSVRGRWGIK SNCLCSNKHV
RPVVKPVVKE EVKPSTPEPE PTKAPLAQPN VCTAPDPIAI PSTPPTPACS SPLSWLTNLS
QTTVNKENKD NLFASNLEHK PLPSFASFGK PVSALQTFGS SILTPTTSNN SGFLRNLLNS
STLKQETNEK STPKILDDIF ASLVQSRPLS DFARKPQGLP IQPSLMGFNT PHYWLCDNRL
LCLQDPNNKS NWNVFRECWK QGQPVIVSGI HNNLNSELWR PESFRREFGD QEADLVNCRT
NDIITGATVG DFWEGFEDIS ARLKNDKGEA MVLKLKDWPP GEDFRDTMLS RFEDLMNNIP
LPEYTRREGK LNLAARLPAY FVRPDLGPKM YNAYGLITPE DRKYGTTNLH LDVSDATNVM
VYVGIPKGEH DQEQEVIRTI QDGDADELTI KRYIEFKEKP GALWHIFAAK DTEKIRQFLK
KVAEEQGHEN PPDHDPIHDQ SWYLDNTLRK RLLQEHGVQG WAIVQFLGDA VFIPAGAPHQ
VHNLYSCIKV AEDFVSPEHV KHCFWLTQEF RYLSHTHTNH EDKLQVKNVI YHAVKDSIAI
LKANEASLGK L
