KDM4C_MOUSE
ID KDM4C_MOUSE Reviewed; 1054 AA.
AC Q8VCD7; Q3UNP7; Q69ZZ5; Q8BUY6; Q8BWA1;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Lysine-specific demethylase 4C;
DE EC=1.14.11.66 {ECO:0000250|UniProtKB:Q9H3R0};
DE AltName: Full=JmjC domain-containing histone demethylation protein 3C;
DE AltName: Full=Jumonji domain-containing protein 2C;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase 4C {ECO:0000305};
GN Name=Kdm4c; Synonyms=Jhdm3c, Jmjd2c, Kiaa0780;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/HeJ, and C57BL/6J; TISSUE=Brain, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 815-829, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9'
CC and 'Lys-36' residues of histone H3, thereby playing a central role in
CC histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor
CC H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36'
CC residue, while it has no activity on mono- and dimethylated residues.
CC Demethylation of Lys residue generates formaldehyde and succinate.
CC {ECO:0000250|UniProtKB:Q9H3R0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000250|UniProtKB:Q9H3R0};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}.
CC -!- DOMAIN: The 2 Tudor domains recognize and bind methylated histones.
CC Double Tudor domain has an interdigitated structure and the unusual
CC fold is required for its ability to bind methylated histone tails (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32301.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173023; BAD32301.1; ALT_INIT; mRNA.
DR EMBL; AK053104; BAC35267.1; -; mRNA.
DR EMBL; AK081769; BAC38327.1; -; mRNA.
DR EMBL; AK144103; BAE25700.1; -; mRNA.
DR EMBL; BC020180; AAH20180.1; -; mRNA.
DR EMBL; BC042424; AAH42424.1; -; mRNA.
DR CCDS; CCDS18287.1; -.
DR RefSeq; NP_001165566.1; NM_001172095.1.
DR RefSeq; NP_659036.1; NM_144787.2.
DR RefSeq; XP_006538415.1; XM_006538352.3.
DR AlphaFoldDB; Q8VCD7; -.
DR SMR; Q8VCD7; -.
DR BioGRID; 218326; 11.
DR IntAct; Q8VCD7; 1.
DR STRING; 10090.ENSMUSP00000030102; -.
DR iPTMnet; Q8VCD7; -.
DR PhosphoSitePlus; Q8VCD7; -.
DR EPD; Q8VCD7; -.
DR jPOST; Q8VCD7; -.
DR MaxQB; Q8VCD7; -.
DR PaxDb; Q8VCD7; -.
DR PeptideAtlas; Q8VCD7; -.
DR PRIDE; Q8VCD7; -.
DR ProteomicsDB; 263522; -.
DR Antibodypedia; 24299; 354 antibodies from 28 providers.
DR DNASU; 76804; -.
DR Ensembl; ENSMUST00000030102; ENSMUSP00000030102; ENSMUSG00000028397.
DR Ensembl; ENSMUST00000077851; ENSMUSP00000077017; ENSMUSG00000028397.
DR GeneID; 76804; -.
DR KEGG; mmu:76804; -.
DR UCSC; uc008tjj.2; mouse.
DR CTD; 23081; -.
DR MGI; MGI:1924054; Kdm4c.
DR VEuPathDB; HostDB:ENSMUSG00000028397; -.
DR eggNOG; KOG0958; Eukaryota.
DR GeneTree; ENSGT00940000154930; -.
DR HOGENOM; CLU_001442_0_0_1; -.
DR InParanoid; Q8VCD7; -.
DR OMA; VPSHEIC; -.
DR OrthoDB; 1186832at2759; -.
DR PhylomeDB; Q8VCD7; -.
DR TreeFam; TF106449; -.
DR BRENDA; 1.14.11.66; 3474.
DR BRENDA; 1.14.11.69; 3474.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR BioGRID-ORCS; 76804; 3 hits in 76 CRISPR screens.
DR PRO; PR:Q8VCD7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VCD7; protein.
DR Bgee; ENSMUSG00000028397; Expressed in saccule of membranous labyrinth and 249 other tissues.
DR ExpressionAtlas; Q8VCD7; baseline and differential.
DR Genevisible; Q8VCD7; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0032452; F:histone demethylase activity; IDA:MGI.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; ISO:MGI.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; ISS:UniProtKB.
DR GO; GO:0140684; F:histone H3-tri/dimethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0070544; P:histone H3-K36 demethylation; ISO:MGI.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IMP:MGI.
DR GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0019827; P:stem cell population maintenance; IGI:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4_Tudor_2.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Dioxygenase; Direct protein sequencing; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1054
FT /note="Lysine-specific demethylase 4C"
FT /id="PRO_0000183178"
FT DOMAIN 16..58
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 144..310
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT DOMAIN 875..932
FT /note="Tudor 1"
FT DOMAIN 933..989
FT /note="Tudor 2"
FT ZN_FING 687..745
FT /note="PHD-type 1"
FT ZN_FING 750..783
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 806..863
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 361..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 200
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 278
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 300
FT /note="D -> V (in Ref. 2; BAC35267)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="M -> V (in Ref. 2; BAE25700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1054 AA; 119966 MW; 86F275FC428B8EDA CRC64;
MEVVEVESPL NPSCKIMTFR PSMEEFREFN KYLAYMESKG AHRAGLAKVI PPKEWKPRQC
YDDIDNLLIP APIQQMVTGQ SGLFTQYNIQ KKAMTVKEFR QLANSSKYCT PRYLDYEDLE
RKYWKNLTFV APIYGADING SIYDEGVDEW NIARLNTVLD VVEEECGISI EGVNTPYLYF
GMWKTTFAWH TEDMDLYSIN YLHFGEPKSW YAIPPEHGKR LERLAQGFFP SSSQGCDAFL
RHKMTLISPS VLKKYGIPFD KITQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID
YGKVAKLCTC RNDMVKISMD IFVKKFQPDR YQIWKQGKDI YTIDHTKPTP ESTPEVKTWL
QRKKKLRKPP KSLQGNKPLC KRPKPEEDEE FAEFSGEEGA NPAMGPRHLK VTEKPEKALK
LGKLEESSAK EALDTRIQVD QSLLNDTKLS GKGCISSSVT AEIPPEDNRA SAVISPSQLK
EGADCIPLSH GHQAGKESHL LKILKLESPK IPSPLPESNK VLTEGEENDE EGHGSNLEPG
EIPEALSEER NGLNIPKIIE GQPKTTKSWR HPLGKPPARS PMTLVKQQVA SDEELPEVLS
IDEEVEETES WAKPLIHLWQ TKSPNFMAEQ EYNATVAKME PNCAICTLLM PYYKPDSSKE
ENDSRWETAV NEVVQSGRKT KPIIPEMCFI YSEENVDYSP PNAFLEEDGT SLLISCAKCF
VRVHASCYGV PSHEVCDGWL CARCKRNAWT AECCLCNLRG GALKQTKNNQ WAHVICAVAV
PEVRFTNVPE RTQIDVDRIP LQRLKLKCIF CRHRVKKVSG ACIQCSYGRC PASFHVTCAH
AAGVLMEPDD WPYVVNITCF RHRVNSNAKS KTCEKAISVG QTVITKHRNT RYYSCRVIDV
TSQTFYEVMF DDGSFSRDTF PEDIVSRNCV KLGPPAEGEV IQVKWPDGKL YGAKYLGSNV
AYMYQVEFED GSQIAMKRED IYTLDEELPK RVKARFSTAS DMRFEDTFYG ADVIQGERKR
QRVLSSRLKN EYVDDPVYRT FLKSSFQKKC QKRQ
