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 27-MAR-2024, entry version 76.
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 AGR; Xenbase:XB-GENE-1012805; -.
DR CTD; 496351; -.
DR Xenbase; XB-GENE-1012805; kdm3a.S.
DR OrthoDB; 3473445at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 496351; Expressed in egg cell and 19 other cell types or 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 H3K9me/H3K9me2 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02208; cupin_RmlC-like; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR PANTHER; PTHR12549:SF7; LYSINE-SPECIFIC DEMETHYLASE 3A; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 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
//
