ID U3FVK5_CALJA Unreviewed; 1559 AA.
AC U3FVK5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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|EMBL:JAB49250.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB49250.1};
RN [1] {ECO:0000313|EMBL:JAB49250.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:JAB49250.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB31311.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB20735.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB39237.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
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; GAMS01002401; JAB20735.1; -; mRNA.
DR EMBL; GAMR01002621; JAB31311.1; -; mRNA.
DR EMBL; GAMQ01002614; JAB39237.1; -; mRNA.
DR EMBL; GAMP01003505; JAB49250.1; -; mRNA.
DR Bgee; ENSCJAG00000005870; Expressed in cerebellum and 6 other cell types or tissues.
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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; 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:SF141; LYSINE-SPECIFIC DEMETHYLASE 5D; 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 2: Evidence at transcript level;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:JAB49250.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:JAB49250.1};
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 323..373
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 467..633
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 197..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1559 AA; 175513 MW; 42FC52A32B14CB3E CRC64;
MDPGSDDFLP 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 DKEGPECPPT VVVKEELGGD MKDSTSPKSF LESKEELSHS
PEPCTKMTMR LRRNHSNAQF IESYVCRMCS RGDEDDKLLL CDGCDDNYHI FCLLPPLPEI
PKGVWRCPKC VMAECKRPPE AFGFEQATRE YTLQSFGEMA DSFKADYFNM PVHMVPTELV
EKEFWRLVNS IEEDVTVEYG ADIHSKEFGS GFPVSDSKRH LTPEEEEYAT SGWNLNVMPV
LEQSVLCHIN ADISGMKVPW LYVGMVFSAF CWHIEDHWSY SINYLHWGEP KTWYGVPSLA
AEHLEEVMKK LTPELFDSQP DLLHQLVTLM NPNTLMSHGV PVVRTNQCAG EFVITFPRAY
HSGFNQGYNF AEAVNFCTAD WLPAGRQCIE HYRRLRRYCV FSHEELICKM AACPEKLDLN
LAAAVHKEMF IMVQEERRLR KALLEKGITE AEREAFELLP DDERQCIKCK TTCFLSALAC
YDCPDGLVCL SHINDLCKCS SSRQYLRYRY TLDELPAMLH KLKVRAESFD TWANKVRVAL
EVEDGRKRSL EELRALESEA RERRFPNSEL LQRLKNCLSE AEACVSRALG LVSGQEAGPH
RVAGLQMTLA ELQAFLDQMN NLPCAMHQIG DVKGVLEQVE AYQAEAREAL ASQPSSPGLL
QSLLERGRQL GVEVPEAQQL QRQVEQARWL DEVKRTLAPS ARRGTLAVMR GLLVAGASVA
PSPAVDKAQA ELQELLTIAE RWEEKADLCL EARQKHPPAT LEAIIREAEN IPVHLPNIQA
LKEALAKARA WIADVDEIQN GDHYPCLDDL EGLVAVGRDL PVGLEELRQL ELQVLTAHSW
REKASKTFLK KNSCYTLLEV LCPCADAGSD STKRSRWMEK ELGLYKSDTE LLGLSAQDLR
DPGSVIVAFK EGEQKEKEGI LQLRRTNSAK PSPLASSTTA ASTTSICVCG QVPAGAGALQ
CDLCQDWFHG RCVSVPRLLS SPRPNPTSSP LLAWWEWDTK FLCPLCMRSR RPRLETILAL
LVALQRLPVR LPEGEALQCL TERAISWQGR ARQALASDDV TALLGRLAEL RQRLQPEPRP
EEPPNYPSAP ASDPLKEGSG KDMPKVQGLL ENGDSVTSPE KVAPEEGSGK RDLELLSSLL
PQLTGPVLEL PEATRAPLEE LMMEGDLLEV TLDENHSIWQ LLQAGQPPDL ERIRTLLELE
KAERHGSRAR GRALERRRRR KVDRGGEGDD PAREELEPKR VRSSGPEAEE AQEEEELEEE
TGGEGPPAPI PTSGSPSTQE NQNGLEPAQG TTSGPSAPFS TLTPRLHLPC PQQPPQQQL
//
