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Database: UniProt
Entry: G3UG57_LOXAF
LinkDB: G3UG57_LOXAF
Original site: G3UG57_LOXAF 
ID   G3UG57_LOXAF            Unreviewed;      1161 AA.
AC   G3UG57;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Lysine demethylase 2A {ECO:0000313|Ensembl:ENSLAFP00000026815.1};
GN   Name=KDM2A {ECO:0000313|Ensembl:ENSLAFP00000026815.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000026815.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000026815.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000026815.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000026815.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000026815.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G3UG57; -.
DR   STRING; 9785.ENSLAFP00000026815; -.
DR   Ensembl; ENSLAFT00000035522.1; ENSLAFP00000026815.1; ENSLAFG00000006277.4.
DR   eggNOG; KOG1633; Eukaryota.
DR   eggNOG; KOG1947; Eukaryota.
DR   GeneTree; ENSGT00940000155484; -.
DR   InParanoid; G3UG57; -.
DR   OMA; XQDNRSK; -.
DR   TreeFam; TF106480; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:Ensembl.
DR   GO; GO:0045322; F:unmethylated CpG binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IEA:Ensembl.
DR   GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
DR   CDD; cd21784; CTD_KDM2A; 1.
DR   CDD; cd22181; F-box_FBXL11; 1.
DR   CDD; cd15643; PHD_KDM2A; 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; IPR019786; Zinc_finger_PHD-type_CS.
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; 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; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
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:UP000007646};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00509}.
FT   DOMAIN          147..315
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          564..610
FT                   /note="CXXC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51058"
FT   DOMAIN          617..678
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          369..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..789
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..871
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1161 AA;  132037 MW;  98C8FA1760BAA075 CRC64;
     KPVVSASCLF SPQRGTMRRR YEDDGISDDE IEGKRTFDLE EKLHTNKYNA NFVTFMEGKD
     FNVEYIQRGG LRDPLIFKNS DGLGIKMPDP DFTVNDVKMC VGSRRMVDVM DVNTQKGIEM
     TMAQWTRYYE TPEEEREKLY NVISLEFSHT RLENMVQRPS TVDLIDWVDN MWPRHLKESQ
     TESTNAILEM QYPKVQKYCL MSVRGCYTDF HVDFGGTSVW YHIHQGGKVF WLIPPTAHNL
     ELYENWLLSG KQGDIFLGDR VSDCQRIELK QGYTFVIPSG WIHAVYTPTD TLVFGGNFLH
     SFNIPMQLKI YNIEDRTRVP NKFRYPFYYE MCWYVLERYV YCITNRSHLT KEFQKESLSM
     DLELNGLESG NGDEDAAADR EPRRLSSRRS ILTSPVANGV NLDYDGLGKA SRSLPSLKKT
     LAGDTSSDSS RGSHNGQVWD PQCSPRKDRQ VHLTHFELEG LRCLVDKLES LPLHKKCVPT
     GIEDEDALIA DVKVLLEELA NSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP
     HTMKPAPRLT PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM
     KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH PGCLQMDGEG
     LLNEELPNCW ECPKCYQEDS SEKAQKRKME ESDDEAVQAK VLRPLRSCDE PLTPPPHSPT
     SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS ASRDERFKRR QLLRLQATER TMVREKENNP
     SGKKELSEVE KAKIRGSYLT VTLQRPTKEL HGTSIVPKLQ AITASSANLR HSPRVLVQHC
     PARAPQRGDE EGLGGEEEDE EEAEEDEDSA EEGGAARLNG RGSWAQDGDE SWMQREVWMS
     VFRYLSRRLC ECMRVCKTWY KWCCDKRLWT KIDLSRCKAI VPQALSGIIK RQPVSLDLSW
     TNISKKQLTW LVNRLPGLKD LLLAGCSWSA VSALSTSSCP LLRTLDLRWA VGIKDPQIRD
     LLTPPADKPG QDNRSKLRNM TDFRLAGLDI TDATLRLIIR HMPLLSRLDL SHCSHLTDQS
     SNLLTAVGSS TRYSLTELNM AGCNKLTDQT LIYLRRIANV TLIDLRGCKQ ITRKACEHFI
     SDLSINSLYC LSDEKLIQKI S
//
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