ID A0A4W3HMC2_CALMI Unreviewed; 1093 AA.
AC A0A4W3HMC2;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN Name=KDM4C {ECO:0000313|Ensembl:ENSCMIP00000017216.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|Ensembl:ENSCMIP00000017216.1, ECO:0000313|Proteomes:UP000314986};
RN [1] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17185593; DOI=10.1126/science.1130708;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Ancient noncoding elements conserved in the human genome.";
RL Science 314:1892-1892(2006).
RN [2] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17407382;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Survey sequencing and comparative analysis of the elephant shark
RT (Callorhinchus milii) genome.";
RL PLoS Biol. 5:E101-E101(2007).
RN [3] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
RN [4] {ECO:0000313|Ensembl:ENSCMIP00000017216.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000040};
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 JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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DR RefSeq; XP_007902172.1; XM_007903981.1.
DR AlphaFoldDB; A0A4W3HMC2; -.
DR STRING; 7868.ENSCMIP00000017216; -.
DR Ensembl; ENSCMIT00000017554.1; ENSCMIP00000017216.1; ENSCMIG00000008216.1.
DR GeneID; 103185468; -.
DR KEGG; cmk:103185468; -.
DR GeneTree; ENSGT00940000154930; -.
DR InParanoid; A0A4W3HMC2; -.
DR OMA; VAKMEPH; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000314986; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20465; Tudor_JMJD2C_rpt1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.10.330.70; -; 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; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF104; LYSINE-SPECIFIC DEMETHYLASE 4C; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 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:UP000314986};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 27..69
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 156..322
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 791..904
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 571..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 124115 MW; C82A10A17B73904B CRC64;
MDRKKSRAAV TMATEDTNSP SKSACKIMTF QPTLEEFKHF SKYIARMECQ GAHRAGLAKV
IPPKGWKPRR NYDNIDNLII PAPIQQMVTG QSGLFTQYNI QKKPMTVLEF RRLANSDNRY
CTPRYQDYED LERKYWKNLT FVAPIYGADV SGSLYDEDID EWNITRLNTI LDVVAEESGI
AIEGVNTPYL YFGMWKTTFA WHTEDMDLYS INYLHFGEPK SWYAIPPEHG KRLERLAQGF
FPSSSQGCDA FLRHKMTLIS PSILKKYGIP FDKITQEAGE FMVTFPYGYH AGFNHGFNCA
ESTNFATIRW VDYGKIAKQC TCRKDMVKIS MDVFVQKFQP SRYELWKRGK DVQTIDHTKP
TPESTPEFEA WQKKRKVIQK KSGMALRSRT FCSLHQFKSR SKKLKTLEDE RSYSEPVATE
TTAAKIFTDG INVKEEPSRE GLEEEFSNTE VMTTGEESIK NIQVDKVQSP EYNSTETFSH
LANAKCKSKA DEKRKEDACF TSSPVDKVNA GTNSSECTKA NITIGVESNT ASDLEKCKEE
DLDHEGKLYQ SIATETQQTC WKQCEIGGVS TEEETSEAES GENGLEPGEI PSFPEQFIRS
VGKKKAAKSR RHPLCKPPAR SPSTFVKQES NSDEEMPDSN SNEEEVNETQ PWAKPLVQLW
QNKSLNIQAE KEYNGEASKM EPYCAICSLF FPYYQPDNPT ERKSEIKTDT SELPGMTKHK
TKPLIPEMCF TYSEENNEPS PGNSFIEEDG TSALISCAKC CMQVHASCYG VPLHEIHDGW
TCSRCIIGAW TADCCLCNLR GGALKQTTDN RWAHVMCAVA IPEARFVNVA DRGPVDVTRI
PLQRLKLKCV FCRKRAKKTS GACIQCSYGR CPTSFHVTCA HAAGVVMEPD DWPYVVLITC
FRHKTNPSVK NKTLFQDLSI GQTVISKHKN GRYYSCRVTG VSSQTFYQVI FDDGSFSDDL
YPEDIASKNC LELGPPAEGE VVQVRWTDGL LYGAKYVASN IIYMYQVEFE DGSQFVVKRD
DVYTLNEELP KRVKSRLSSA SNMRYEATFS NESIQAKKRP RVLNSKFMNE YVNDPGYRTF
LGNFFQTHCR QGQ
//
