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Database: UniProt
Entry: H2UF78_TAKRU
LinkDB: H2UF78_TAKRU
Original site: H2UF78_TAKRU 
ID   H2UF78_TAKRU            Unreviewed;      1285 AA.
AC   H2UF78;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Lysine demethylase 2A {ECO:0000313|Ensembl:ENSTRUP00000035597.2};
GN   Name=KDM2A {ECO:0000313|Ensembl:ENSTRUP00000035597.2};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000035597.2, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000035597.2, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000035597.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC       subfamily. {ECO:0000256|ARBA:ARBA00006942}.
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DR   RefSeq; XP_011608910.1; XM_011610608.1.
DR   STRING; 31033.ENSTRUP00000035597; -.
DR   Ensembl; ENSTRUT00000035725.3; ENSTRUP00000035597.2; ENSTRUG00000013920.3.
DR   GeneID; 101067040; -.
DR   KEGG; tru:101067040; -.
DR   CTD; 799441; -.
DR   eggNOG; KOG1633; Eukaryota.
DR   eggNOG; KOG1947; Eukaryota.
DR   GeneTree; ENSGT00940000155484; -.
DR   InParanoid; H2UF78; -.
DR   OMA; MQMPDPD; -.
DR   OrthoDB; 2784357at2759; -.
DR   TreeFam; TF106480; -.
DR   Proteomes; UP000005226; Chromosome 14.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   CDD; cd22181; F-box_FBXL11; 1.
DR   CDD; cd15555; PHD_KDM2A_2B; 1.
DR   Gene3D; 1.20.58.1360; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR041070; JHD.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR002857; Znf_CXXC.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23123:SF3; LYSINE-SPECIFIC DEMETHYLASE 2A; 1.
DR   PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF17811; JHD; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF16866; PHD_4; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00367; LRR_CC; 3.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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:UP000005226};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00509}.
FT   DOMAIN          146..314
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          513..561
FT                   /note="CXXC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51058"
FT   DOMAIN          568..628
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          627..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..775
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..843
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..869
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..929
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        938..975
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..993
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1285 AA;  144393 MW;  44574B90C73622E6 CRC64;
     MEDPHTRYSK RLRTGTRRRY QDDGISDDEI EGKRTFDLDE KLLCDRFNSE LIKHMKGNEF
     TFEYIQREGL RDPIIFENSD GLGLQMPDPD FSVSDVNLCV GSRRIVDVMD VNTQKGIEMS
     MAQWRRYYET PPSEREKLYN VISLEFSHTR LENLVKRPAS VDLVDWVDNM WPRHLKERQR
     DSTNAIIDMH YPKVQKYCLM SVQGCFTDFH IDFGGTSVWY HILRGAKVFW LIPPTPQNLD
     MYENWVLSGK QGDIFLGDKC YDCQRIELRQ GNTFIIPSGW IHAVYTPEDT LVFGGNFLHS
     FNIPMQLNIY SIEDRTRVPA KFRYPFYYEM CWYVLERYLY CLTNVSHYTP EFQKYSLGLG
     LAPTDLENYD QSGNCAPDGV NAEAGSIDVS EDVKKEEEAT AVNKPKHVLT NFEMEGLWNL
     LGKLEELPDH KKCVPDGIRD PSALLNNIKA VLKQCALDDP KLSYTGEPIV KWPERPAWYQ
     PPAVPPPVLY RPRLGPTLHK SHGQKRTKSS SISALRRRRV RCKRCAGCCR KECGNCIYCH
     DMRKFGGPGR MKKGCIMRQC LAPALPNTAR CAICREGEFD ESDPSTYSLM ECSVCSQIAH
     RQCIKEPGEG KINKDLPSCW ECPKCYQGKD SGSESSSEEE SEESEGSSFL PPSKLGNREG
     IGVGEGLKKG SRNTPAARPT APPPSQKLLL QHQQSRKRAS ALELRFKKRI KLERSKVLMK
     HARLDRSPRL LGSRLLSRLR SPTSTLSQGR GRGSPYNGAP GGARSFQQQQ ASHNLVLEPL
     GEPRRGRGRG VRLRGGGAGR GIVRGRDLEE ESEDSSSSST SSSSSDDDEA EETGQRNGKG
     LDKENQPDLS QGRATKDGEE EKMEVGNQNS GEEEEEEMET QTGGKDGSYY KVTLQKPSRA
     ARDPSAIVPK LEAVTPQTAT STLHNQSRAL SRPPIRDRGP CSDQHSNRHR TSHAHSEHAV
     QRSSRPERAE KTKPSRTTKL GNVGSSSSAS ELGHPRVPLS ALQEGGSEAD RENGGAGPAC
     EREVWVSVFR YLSRADLCVC MAVCKNWYKW CLDKRLWSRI DLSIKRTVTP QALTGIIKRQ
     PVTLDLSWTN ISRKQLNWLV GRLPGLKDLM LAGCCWSSVS ALCSSGCPLL RSLDLRYADG
     VKDTQIRDLV TPPGCDNRSQ LRNMQSLRLA GLDISDSTVR LVIRHMPHLT KLDLSHCNSL
     TDHSINLLTA VGSSTRNTLS ELNLGGCSKL TDTCLKYLRR LSCMSVLDLR GCKGVSRKAC
     EAFISELSVN TLYCLSDEKL IQRIS
//
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