ID A0A3Q0RVB9_AMPCI Unreviewed; 1478 AA.
AC A0A3Q0RVB9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000013623.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000013623.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 61819.ENSACIP00000013623; -.
DR Ensembl; ENSACIT00000013992.1; ENSACIP00000013623.1; ENSACIG00000010559.1.
DR GeneTree; ENSGT00940000164196; -.
DR OMA; MASGKMM; -.
DR Proteomes; UP000261340; Unplaced.
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 GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR CDD; cd16875; ARID_KDM5C_5D; 1.
DR CDD; cd15604; PHD1_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; 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 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 12..53
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 81..171
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 325..375
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 468..634
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 184..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1419
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1478 AA; 169331 MW; 569395463586406F CRC64;
MEGEEFVPPP ECPVFEPSWE EFQDPLGYIA KIRPIAEKSG ICKIRPPPDW QPPFSVELDN
FHFTPRIQRL NEXFFLILAE TRVKLNYLDR IARFWEIQGS SLKIPHIERR ILDLFSLSKI
VTDEGGFEMV CKERRWARIA QRLGYPPGKN IGSLLRSHYE RIVYPYEMFQ SGASLQHCKP
KHYDGEDVDK EYKPHSIPLR QSVQPSKMSS YGRRANRCQP DPEPTEEDIE KNPELKKLQI
YGAGPKMMGL GLVARDKGIR KKGKCSSGPQ LPPPSVTVKM AVKKEEPVEE NGKRHKEEED
DTDGPCTKMT MRLRRNLSNP QCVDSFVCRM CGRGDDDDKL MLCDGCDDNY HTYCLLPPLA
DPPKGNWRCP KCVAECKKPT EAFGFEQATR EYTLQSFGEM ADTFKADYFN MPVHMVPTEL
VEREFWRLVS SIEEDVTVEY GADIHSKEFG SGFPMNNGKR KLTKEEEEYA RCGWNLNVMP
VLEQSLLCHI NGDISGMKVP WLYVGMVFSA FCWHIEDHWS YSINYLHWGE PKTWYGVPSM
AAERLEEVMK KLTPELFEFQ PDLLHQLVTI MNPNILMAHG VPVVRTNQCA GEFVITFPRA
YHSGFNQGYN FAEALPAGRS CIEHYRRLRR YCVFSHEELT CKMAASPEKL DLNLAAATHR
EMFIIVQEER KLRKGLMERG ITEAEREAFE LLPDDERQCD KCKTTCFLSA LACSNCPERL
VCLYHTQDLC NCPTEKLYLR YRYTLDELLA MLHRLKVRSE SFDSWANRVK EALEQEEGNK
IEIDYLEMLK MEAAEKKFPD NELLRKLNTV LKDIVHCQQK STELLNNSAT TPRMTLDELK
SLVETMQNLP CVMNQLEGVL TVEDFQSRAQ VLVNDKDWRK DSPPAEQLQT FLEEGAKMPV
LVPECNLLQG LKEQGHWLAE VRRTLGTEGG ERQEVTLDVL RNLMEAGCNV PQSVSVETAM
AELQELLTIA ERWEEKAQIC LEQRQKHPLS TLEAIVNEAQ LIPVTLPNIL ALQGCLTRAR
AWVTDLEEIQ NGEHYPCLDD LEGLVAIGRD LPVFMEELRQ LELQVASAHS WRDKASKTFL
KKSSQHSLLE VLCPCAKRRE RRDQTGPVDD PLDDSDTNTL GLSAQDLRDP AAIVMAFKEG
EHQEKEALLR LQKANIWDDQ PRAPQLRCHL CKDWFHGGCV PFPSLLPSSG PPINPLCWWD
WDSRFLCPRC QRSRRPRLET ILALLVALQR LPVRLPEGEA LQCLTERAIT WQGRAKEALE
TPEVQQVLQR LQELKETLHH EPEKEKSEKE TEGSSVIVLS DSEGGEGDDG VIDLTEENSP
KKNTEESTGS LLPLLPLLKG RVVELSPATR ARLEELQLEG DLLEVSLDQM HTIHRVLLAV
SDPPKETLHT LIQVLENKVQ RRTSRGRAKE SRRKRKSHRG GSGEGTGQRS LDASETKKTC
PFRHTSSPHI PVQTHPEVTY PFFLFFYKTF SFTWKCML
//
