ID G1L165_AILME Unreviewed; 1162 AA.
AC G1L165;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Lysine demethylase 2A {ECO:0000313|Ensembl:ENSAMEP00000000617.2};
GN Name=KDM2A {ECO:0000313|Ensembl:ENSAMEP00000000617.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000000617.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000000617.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000000617.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_011225839.1; XM_011227537.2.
DR RefSeq; XP_019657413.1; XM_019801854.1.
DR AlphaFoldDB; G1L165; -.
DR STRING; 9646.ENSAMEP00000000617; -.
DR Ensembl; ENSAMET00000000637.2; ENSAMEP00000000617.2; ENSAMEG00000000531.2.
DR GeneID; 100469601; -.
DR KEGG; aml:100469601; -.
DR CTD; 22992; -.
DR eggNOG; KOG1633; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000155484; -.
DR HOGENOM; CLU_003540_0_1_1; -.
DR InParanoid; G1L165; -.
DR TreeFam; TF106480; -.
DR Proteomes; UP000008912; 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; 6.10.280.250; -; 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 Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
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:UP000008912};
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 148..316
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 365..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..444
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 704..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 422..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 1162 AA; 132877 MW; 4985B2ED7A5E4B93 CRC64;
MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLHTNKYN ANFVTFMEGK
DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM CVGSRRMVDV MDVNTQKGIE
MTMAQWTRYY ETPEEEREKL YNVISLEFSH TRLENMVQRP STVDFIDWVD NMWPRHLKES
QTESTNAILE MQYPKVQKYC LMSVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN
LELYENWLLS GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL
HSFNIPMQLK IYNIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL TKEFQKESLS
MDLELNGLES GNGDEEAVDR EPRRLSNRRS VLTSPVANGV NLDYDGLGKT CRSLPSLKKT
LSADSSSDSS RGSHNGQVWD PQCSPRKDRK VHLTHFELEG LRCLVDKLES LPLHKKCVPT
GIEDEDALIA DVKILLEELA NSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP
HTMKPAPRLT PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM
KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH PGCLQMDGEG
LLNEELPNCW ECPKCYQEDN SEKAQKRKME ESDEEAVQAK VLRPLRSCDE PLTPPPHSPT
SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS ASRDERFKRR QLLRLQATER TMVREKENNP
SGKKELSEVE KAKIRGSYLT VTLQRPTKEL HGTSIVPKLQ AITASSANLR HSPRVLVQHC
PARTPQRGDE EGLGGEEEEE EEEEEEDDSA EEGGAARLNG RGSWAQDGDE SWMQREVWMS
VFRYLSRREL CECMRVCKTW YKWCCDKRLW TKIDLSRCKA IVPQALSGII KRQPVSLDLS
WTNISKKQLT WLVNRLPGLK DLLLAGCSWS AVSALSTSSC PLLRTLDLRW AVGIKDPQIR
DLLTPPADKP GQDNRSKLRN MTDFRLAGLD ITDATLRLII RHMPLLSRLD LSHCSHLTDQ
SSNLLTAVGS STRYSLTELN MAGCNKLTDQ TLIYLRRIAN VTLIDLRGCK QITRKACEHF
ISDLSINSLY CLSDEKLIQK IS
//
