ID A0A2I3HCT1_NOMLE Unreviewed; 1338 AA.
AC A0A2I3HCT1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN Name=KDM5C {ECO:0000313|Ensembl:ENSNLEP00000041266.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000041266.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000041266.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000041266.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000256|ARBA:ARBA00000604};
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 JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADFV01094092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01094093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01094094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01094095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01094096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01094097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01094098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01094099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSNLET00000052984.1; ENSNLEP00000041266.1; ENSNLEG00000015927.2.
DR GeneTree; ENSGT00940000161236; -.
DR Proteomes; UP000001073; Chromosome X.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15604; PHD1_KDM5C_5D; 1.
DR CDD; cd15608; PHD2_KDM5C_5D; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
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; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF43; LYSINE-SPECIFIC DEMETHYLASE 5C; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
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:UP000001073};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 11..102
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 14..55
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 257..307
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 401..567
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 140..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 150452 MW; AAFFACB9CCFEEB9E CRC64;
MEPGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA IVVEEGGYEA
ICKDRRWARV AQRLNYPPGK NIGSLLRSHY ERIVYPYEMY QSGANLVQCN TRPFDNEEKD
KEYKPHSIPL RQSVQPSKFN SYGRRAKRLQ PDPEPTEEDI EKNPELKKLQ IYGAGPKMMG
LGLMAKDKTL RKKDKEGPEC PPTVVVKEEL GGDVKVESTT PKTFLESKEE LSHSPEPCTK
MTMRLRRNHS NAQFIESYVC RMCSRGDEDD KLLLCDGCDD NYHIFCLLPP LPEIPKGVWR
CPKCVMAECK RPPEAFGFEQ ATREYTLQSF GEMADSFKAD YFNMPVHMVP TELVEKEFWR
LVNSIEEDVT VEYGADIHSK EFGSGFPVSD SKRHLTPEEE EYATSGWNLN VMPVLEQSVL
CHINADISGM KVPWLYVGMV FSAFCWHIED HWSYSINYLH WGEPKTWYGV PSLAAEHLEE
VMKKLTPELF DSQPDLLHQL VTLMNPNTLM SHGVPVVRTN QCAGEFVITF PRAYHSGFNQ
GYNFAEAVNF CTADWLPAGR QCIEHYRRLR RYCVFSHEEL ICKMAACPEK LDLNLAAAVH
KEMFIMVQEE RRLRKALLEK GITEAEREAF ELLPDDERQC IKCKTTCFLS ALACYDCPDG
LVCLSHINDL CKCSSSRQYL RYRYTLDELP AMLHKLKVRA ESFDTWANKV RVALEVEDGR
KRSLEELRAL ESEARERRFP NSELLQQLKN CLSEAEACVS RALGLVSGQE AGPHRVAGLQ
MTLAELRAFL DQMNNLPCAM HQIGDVKGIL EQVEAYQAEA REALASLPSS PGLLQSLLER
GRQLGVEVPE AQQLQRQVEQ ARWLDEVKRT LAPSARRGTL AVMRGLLVAG ASVAPSPAVD
KAQAELQELL TIAERWEEKA HLCLEARQKH PPATLEAIIR EAENIPVHLP NIQALKEALA
KARAWIADVD EIQNGDHYPC LDDLEGLVAV GRDLPVGLEE LRQLELQVLT ASKTFLKKNS
CYTLLEVLCP CADAGSDSTK RSRWMEKELG LYKSDTELLG LSAQDLRDPG SVIVAFKEGE
QKEKEGILQL RRTNSAKPSP LASSTTASST TSICVCGQVP AGAGALQCDL CQDWFHGRCV
SVPRLLSSPR PNPTSSPLLA WWEWDTKFLC PLCMRSRRPR LETILALLVA LQRLPVRLPE
GEALQCLTER AISWQGRARQ ALASEDVTAL LGRLAELRQR LQAEPRPEEP PNYPVAPASD
PLREGSGKDM PKVQGLLENG DSVTSPEKVA PEEGSGKRGR SRCGVGRLLT SLDFCILTPR
YCSDLSSWGP APGVFPPW
//
