UniProt: A0A8J0UC30

Database: UniProt
Entry: A0A8J0UC30_XENLA

LinkDB:  A0A8J0UC30_XENLA 
Original site:  A0A8J0UC30_XENLA

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   XENBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (20)   
   InterPro (8)   
   Pfam (5)   
   PROSITE (3)   
   SMART (4)   
All databases (31)   

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ID   A0A8J0UC30_XENLA        Unreviewed;      1141 AA.
AC   A0A8J0UC30;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   28-JAN-2026, entry version 19.
DE   RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE            EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN   Name=kdm4c.S {ECO:0000313|RefSeq:XP_018099298.1,
GN   ECO:0000313|Xenbase:XB-GENE-17341707};
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 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018099298.1};
RN   [1] {ECO:0000313|RefSeq:XP_018099298.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018099298.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018099298.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 2-
CC         oxoglutarate + 2 O2 = N(6)-methyl-L-lysyl(9)-[histone H3] + 2
CC         formaldehyde + 2 succinate + 2 CO2; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC         COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC         EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00049349};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC       {ECO:0000256|ARBA:ARBA00009711}.
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DR   RefSeq; XP_018099298.1; XM_018243809.2.
DR   AlphaFoldDB; A0A8J0UC30; -.
DR   GeneID; 108706953; -.
DR   KEGG; xla:108706953; -.
DR   AGR; Xenbase:XB-GENE-17341707; -.
DR   CTD; 108706953; -.
DR   Xenbase; XB-GENE-17341707; kdm4c.S.
DR   OrthoDB; 9547406at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:TreeGrafter.
DR   GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR   CDD; cd20465; Tudor_JMJD2C_rpt1; 1.
DR   FunFam; 2.60.120.650:FF:000048; Lysine-specific demethylase 4A; 1.
DR   FunFam; 3.30.40.10:FF:000029; lysine-specific demethylase 4C isoform X1; 1.
DR   FunFam; 3.10.330.70:FF:000001; Putative lysine-specific demethylase 4a; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.10.330.70; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR040477; KDM4-like_Tudor.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   PANTHER; PTHR10694:SF104; LYSINE-SPECIFIC DEMETHYLASE 4C; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02375; JmjN; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF18104; Tudor_2; 2.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00545; JmjN; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00333; TUDOR; 2.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51183; JMJN; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          91..133
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          219..385
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          837..950
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          65..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..459
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1141 AA;  129529 MW;  B5E465C27C654D64 CRC64;
     MDLGNASPNN NREPRTRALC LKDAHPRLIN SLQAGRRHQA QPGVAAVKTP ETCCGLNGQA
     FTRRKGLESE KKNSLKMTSS DSDEQNPNCK IMTFRPTFEE FKDFNKYLVY MESKGAHRAG
     LAKVIPPKEW KPKRHYDDID DLVIPAPIQQ MVTGQSGLFT QYNIQKKPMT VKEFRHMANS
     GRYCTPTYID YEDLERKYWK NVTFVPPIYG ADVNGSLYEK DVNEWNISRL NTILDVVEEE
     CGISIEGVNT PYLYFGMWKT TFAWHTEDMD LYSINYLHFG EPKSWYTVPP EHGKRLERLA
     QGFFPSSFQG CDAFLRHKMT LISPSILKKY GIPFSKITQE SGEFMITFPY GYHAGFNHGF
     NCAESTNFAT VRWIDYGKIA KLCSCSNDMV KISMDIFVKM FQKSRYQLWK QGKDICTIDH
     TKPTTGPTQE VIAWKMKRSR RRKGPVKSLQ HTRSRSKKLK TPEDKKAVVA GAEIVVTEAA
     DDFKVNHKPA VKAELEEKEK PTGCMMNIKA ENVNQSGSNT IQASSGMGSS LQEQKVIAEQ
     NGGSNLNLAS SGSDALAGTF ATSTDLKVQE GRYIQEETEK NVQDYHASEL ESTEKDDTIS
     NCSEEDTSDL DIAENSLEPG EIPNVNNDEK PVSEISSPCV THLVEKRGKL KQTTKSRRLP
     LSNPPCGSPM MVLKEDAISD GELSESPCMD DVAETESWAK PLFYLWQTKS QSFAAEKAYN
     QSVSGRKPYC AVCTLFLPYN KSETYNDDVQ AYWDDLSNSI ISSHSKTKCL IPELCFKYKK
     GKKQHSSQKS YIKDDERSLL VTCVKCCVQV HSSCYGVPSH EIHDGWMCAR CRIGVWAAEC
     CLCNLRGGAL KQTTDDKWAH VMCAIAVPEV KFQNLTERSE IDTSTIPLER LKLRCVFCRE
     RVNRVSGACI QCSYGRCPTS FHVTCAHAAG VLMEPDDWPF VVYTTCFRHM INQNMRSKIV
     KKAISIGQTV IAKHRNTRYY NCQLKEMTSQ TFYEIVFDDG STSKDTFPED IVNRDCLTQG
     PPAEGEAVEV KWSDGLLYGG KYIGKNIVYM YHVEFEDGSQ IVTKREDIYT LDEELPKKIK
     SRYSRASDMK FEDEFYGEEV ICGQKKRQRV LNVKLENDYV NDPLYHTFLK SSFQKTCQQT
     L
//

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