ID A0A2I3HUA1_NOMLE Unreviewed; 1343 AA.
AC A0A2I3HUA1;
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:ENSNLEP00000047163.1};
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:ENSNLEP00000047163.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000047163.1, 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:ENSNLEP00000047163.1}
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}.
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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; ENSNLET00000057671.1; ENSNLEP00000047163.1; 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; cd16875; ARID_KDM5C_5D; 1.
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; 1.
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 14..55
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 79..169
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 308..358
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 452..618
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1289..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1343 AA; 151527 MW; 6647BC55D8D9A0DE CRC64;
MEPGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV
DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERRIL DLYSLSKIVV
EEGGYEAICK DRRWARVAQR LNYPPGKNIG SLLRSHYERI VYPYEMYQSG ANLVQCNTRP
FDNEEKDKEY KPHSIPLRQS VQPSKFNSYG RRAKRLQPDP EPTEEDIEKN PELKKLQIYG
AGPKMMGLGL MAKDKTLRKK GKCPPTVVVK EELGGDVKVE STTHSPEPCT KMTMRLRRNH
SNAQFIESYV CRMCSRGDED DKLLLCDGCD DNYHIFCLLP PLPEIPKGVW RCPKCVMAEC
KRPPEAFGFE QATREYTLQS FGEMADSFKA DYFNMPVHMV PTELVEKEFW RLVNSIEEDV
TVEYGADIHS KEFGSGFPVS DSKRHLTPEE EEYATSGWNL NVMPVLEQSV LCHINADISG
MKVPWLYVGM VFSAFCWHIE DHWSYSINYL HWGEPKTWYG VPSLAAEHLE EVMKKLTPEL
FDSQPDLLHQ LVTLMNPNTL MSHGVPVVRT NQCAGEFVIT FPRAYHSGFN QGYNFAEAVN
FCTADWLPAG RQCIEHYRRL RRYCVFSHEE LICKMAACPE KLDLNLAAAV HKEMFIMVQE
ERRLRKALLE KGITEAEREA FELLPDDERQ CIKCKTTCFL SALACYDCPD GLVCLSHIND
LCKCSSSRQY LRYRYTLDEL PAMLHKLKVR AESFDTWANK VRVALEVEDG RKRSLEELRA
LESEARERRF PNSELLQQLK NCLSEAEACV SRALGLVSGQ EAGVAGLQMT LAELRAFLDQ
MNNLPCAMHQ IGDVKGILEQ VEAYQAEARE ALASLPSSPG LLQSLLERGR QLGVEVPEAQ
QLQRQVEQAR WLDEVKRTLA PSARRGTLAV MRGLLVAGAS VAPSPAVDKA QAELQELLTI
AERWEEKAHL CLEARQKHPP ATLEAIIREA ENIPVHLPNI QALKEALAKA RAWIADVDEI
QNGDHYPCLD DLEGLVAVGR DLPVGLEELR QLELQVLTAS KTFLKKNSCY TLLEVLCPCA
DAGSDSTKRS RWMEKELGLY KSDTELLGLS AQDLRDPGSV IVAFKEGEQK EKEGILQLRR
TNSAKPSPLA SSTTASSTTS ICVCGQVPAG AGALQCDLCQ DWFHGRCVSV PRLLSSPRPN
PTSSPLLAWW EWDTKFLCPL CMRSRRPRLE TILALLVALQ RLPVRLPEGE ALQCLTERAI
SWQGRARQAL ASEDVTALLG RLAELRQRLQ AEPRPEEPPN YPVAPASDPL REGSGKDMPK
VQGLLENGDS VTSPEKVAPE EGS
//
