KDM7A_XENTR
ID KDM7A_XENTR Reviewed; 922 AA.
AC Q08D35;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Lysine-specific demethylase 7A;
DE EC=1.14.11.-;
DE AltName: Full=JmjC domain-containing histone demethylation protein 1D;
DE AltName: Full=Lysine-specific demethylase 7;
GN Name=kdm7a; Synonyms=jhdm1d, kdm7;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone demethylase required for brain development.
CC Specifically demethylates dimethylated 'Lys-9' and 'Lys-27' (H3K9me2
CC and H3K27me2, respectively) of histone H3 and monomethylated histone H4
CC 'Lys-20' residue (H4K20Me1), thereby playing a central role in histone
CC code (By similarity). {ECO:0000250}.
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: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC Binding to H3K4me3 prevents its access to H3K9me2 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000305}.
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DR EMBL; BC123960; AAI23961.1; -; mRNA.
DR RefSeq; NP_001072664.1; NM_001079196.1.
DR AlphaFoldDB; Q08D35; -.
DR SMR; Q08D35; -.
DR PRIDE; Q08D35; -.
DR GeneID; 780121; -.
DR KEGG; xtr:780121; -.
DR CTD; 80853; -.
DR Xenbase; XB-GENE-5900920; kdm7a.
DR InParanoid; Q08D35; -.
DR OrthoDB; 1384737at2759; -.
DR Reactome; R-XTR-3214842; HDMs demethylate histones.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; ISS:UniProtKB.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; ISS:UniProtKB.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; ISS:UniProtKB.
DR GO; GO:0035575; F:histone H4-methyl-lysine-20 demethylase activity; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071557; P:histone H3-K27 demethylation; ISS:UniProtKB.
DR GO; GO:0070544; P:histone H3-K36 demethylation; ISS:UniProtKB.
DR GO; GO:0033169; P:histone H3-K9 demethylation; ISS:UniProtKB.
DR GO; GO:0035574; P:histone H4-K20 demethylation; ISS:UniProtKB.
DR GO; GO:0030901; P:midbrain development; ISS:UniProtKB.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Neurogenesis;
KW Nucleus; Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..922
FT /note="Lysine-specific demethylase 7A"
FT /id="PRO_0000391905"
FT DOMAIN 199..355
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 6..57
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 445..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..666
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 922 AA; 105557 MW; C33984F8FF1B7C40 CRC64;
MAGAAPVYCV CRQPYDVSRF MIECDICKDW FHSSCVKVEE HQAADIDLYH CPNCEVLHGP
SQLKKRRNWH RHDYTEPDDG TKPVQAGTRT FIQQLQARSF PSADDLLLKM NGSQLTQRYL
EKQGFNLPIM VPRLDDLGLR LPPPTFSVMD VERYVGGEKI IDVIDVARQA DSKMKLKNFV
KYFMNPDRPK VLNVISLEFS DTKMADLVKV PDISKKLSWV ENYWPDDSFF TKPFVQKYCL
MGVQDSYTDF HIDFGGTSVW YHVLWGEKVF YLIKPSDENL ALYESWSSSV TQSEEFFGDK
VDKCYKCVVK QGHTLFVPTG WIHAVLTSQD CMAFGGNFLH NLNIGMQLRC YEMEKRLKTP
DLFKFPFFEA ICWFVAKNLL ETLKELKEDG FHPPNYLKHG VKALISALKS WMKKESVAEH
AFEIPDNIRP GHLIKELSKV IRSVEEEGNR PVKSQGIHGH CPVSRSSHEK SSHHSGRKAR
RLRDHSTKTP TNLDILEHHT REVLKRLEMS PWEEDAGTYK LNMRFNKPLL PSSTEPDQKV
RDNGIRLLLS NGRIIRDERQ PFTDRSLYTA DSEDEDDRAR SRKAKDIKQE KPCSTSGMED
KAETQKPLNM FFESVKSELR NGSSEYSDIS DSEGSEDNCT NQKHFSEESE SSGDDDDEEE
EEEEERQEPI RNLKEEHSGR RLPCDPNFPW PDHDSPQKRE CPTSTSMEQE AVQGMLSMAS
LHYPSALPTP AKSTDCNIRG GYPQLHIRVS QGNGKEHLDS HSHKAANSDH HVKDEGEFSA
LDWIRQPDAS CRLSPQDSCQ VPQSLRREFA HEEYEKAPED KHYLEIEHWD SAEYQPEKYD
PESSMSSGEC HLSDGSLSPT RIYGDTAAAV PLHPTKRPAS NPPPISNQAT KGKRPKKGMA
TAKQRLGKIL KLNRNGHARF FV
