UTY_MOUSE
ID UTY_MOUSE Reviewed; 1212 AA.
AC P79457; O97979;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Histone demethylase UTY;
DE EC=1.14.11.68 {ECO:0000250|UniProtKB:O14607};
DE AltName: Full=Male-specific histocompatibility antigen H-YDB;
DE AltName: Full=Ubiquitously transcribed TPR protein on the Y chromosome;
DE AltName: Full=Ubiquitously transcribed Y chromosome tetratricopeptide repeat protein;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase UTY {ECO:0000305};
GN Name=Uty; Synonyms=Kdm6c;
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 [MRNA].
RC STRAIN=RIII; TISSUE=Testis;
RX PubMed=9736773; DOI=10.1093/hmg/7.11.1713;
RA Mazeyrat S., Saut N., Sargent C.A., Grimmond S., Longepied G.,
RA Ehrmann I.E., Ellis P.S., Greenfield A., Affara N.A., Mitchell M.J.;
RT "The mouse Y chromosome interval necessary for spermatogonial proliferation
RT is gene dense with syntenic homology to the human AZFa region.";
RL Hum. Mol. Genet. 7:1713-1724(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J;
RX PubMed=8944031; DOI=10.1038/ng1296-474;
RA Greenfield A., Scott D., Pennisi D., Ehrmann I., Ellis P.S., Cooper L.,
RA Simpson E., Koopman P.;
RT "An H-YDb epitope is encoded by a novel mouse Y chromosome gene.";
RL Nat. Genet. 14:474-478(1996).
RN [3]
RP INTERACTION WITH TLE1 AND TLE2.
RX PubMed=9854018; DOI=10.1042/bj3370013;
RA Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.;
RT "Groucho/transducin-like enhancer of split (TLE) family members interact
RT with the yeast transcriptional co-repressor SSN6 and mammalian SSN6-related
RT proteins: implications for evolutionary conservation of transcription
RT repression mechanisms.";
RL Biochem. J. 337:13-17(1999).
CC -!- FUNCTION: Male-specific histone demethylase that catalyzes
CC trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has
CC relatively low KDM activity. {ECO:0000250|UniProtKB:O14607}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224,
CC Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, 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=1.14.11.68; Evidence={ECO:0000250|UniProtKB:O14607};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC -!- SUBUNIT: Binds TLE1 and TLE2.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000305}.
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DR EMBL; AF057367; AAC67385.1; -; mRNA.
DR EMBL; Y09222; CAA70422.1; -; mRNA.
DR CCDS; CCDS41216.1; -.
DR PIR; T42387; T42387.
DR PIR; T42729; T42729.
DR AlphaFoldDB; P79457; -.
DR SMR; P79457; -.
DR STRING; 10090.ENSMUSP00000070012; -.
DR iPTMnet; P79457; -.
DR PhosphoSitePlus; P79457; -.
DR MaxQB; P79457; -.
DR PaxDb; P79457; -.
DR PRIDE; P79457; -.
DR ProteomicsDB; 297903; -.
DR MGI; MGI:894810; Uty.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG1246; Eukaryota.
DR InParanoid; P79457; -.
DR PhylomeDB; P79457; -.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR ChiTaRS; Uty; mouse.
DR PRO; PR:P79457; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P79457; protein.
DR GO; GO:0044666; C:MLL3/4 complex; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IMP:MGI.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IDA:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:MGI.
DR GO; GO:0071557; P:histone H3-K27 demethylation; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; TPR repeat;
KW Zinc.
FT CHAIN 1..1212
FT /note="Histone demethylase UTY"
FT /id="PRO_0000106413"
FT REPEAT 88..121
FT /note="TPR 1"
FT REPEAT 125..158
FT /note="TPR 2"
FT REPEAT 165..193
FT /note="TPR 3"
FT REPEAT 200..233
FT /note="TPR 4"
FT REPEAT 245..278
FT /note="TPR 5"
FT REPEAT 279..312
FT /note="TPR 6"
FT REPEAT 313..346
FT /note="TPR 7"
FT REPEAT 347..380
FT /note="TPR 8"
FT DOMAIN 907..1070
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 530..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 958
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 960
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 1038
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT MOD_RES 752
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT CONFLICT 1069
FT /note="E -> Q (in Ref. 2; CAA70422)"
FT /evidence="ECO:0000305"
FT CONFLICT 1149..1212
FT /note="EVFNLLFVTNESNSQKTYIVHCQNCARKTSGNLENFVVLEQYKMEDLIQVYD
FT QFTLAPSLSSAS -> STRDLLPQLHLRQCHLQGPTDKAAILEFHLTEGSGDMH (in
FT Ref. 2; CAA70422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1212 AA; 136737 MW; 2AE1A816F3D6ACB5 CRC64;
MKSYGLSLTT AALGNEEKKM AAEKARGEGE EGSFSLTVEE KKALCGLDSS FFGFLTRCKD
GAKMKTLLNK AIHFYESLIV KAEGKVESDF FCQLGHFNLL LEDYSKALSS YQRYYSLQTD
YWKNAAFLYG LGLVYFYYNA FQWAIRAFQE VLYVDPNFCR AKEIHLRLGF MFKMNTDYES
SLKHFQLALI DCNVCTLSSV EIQFHIAHLY ETQRKYHSAK AAYEQLLQIE SLPSQVKATV
LQQLGWMHHN MDLIGDNTTK ERYAIQYLQK SLEEDPNSGQ SWYFLGRCYS CIGKVQDAFV
SYRQSIDKSE ASADTWCSIG VLYQQQNQPM DALQAYICAV QLDHGHAAAW MDLGILYESC
NQPQDAIKCY LNAARSKSCN NTSALTSRIK FLQAQLCNLP QSSLQNKTKL LPSIEEAWSL
PIPAELTSRQ GAMNTAQQSV SDTWNSVQTA SHHSVQQKVY TQCFTAQKLQ SFGKDQQPPF
QTGSTRYLQA ASTNDQNQNG NHTLPQNSKG DAQNHFLRIP TSEEQKIINF TKESKDSRSK
SLTSKTSRKD RDTSNICVNA KKHSNHIYQI SSVPISSLNN KESVSPDLII VDNPQLSVLV
GETIDNVDHD IGTCNKVNNV HLAIHKKPDN LSASSPSSAI STETLSLKLT EQTHIVTSFI
SPHSGLHTIN GEGHENLESS ASVNVGLRPR SQIIPSMSVS IYSSSTEVLK ACRSLGKNGL
SNGHILLDIC PPPRPPTSPY PPLPKEKLNP PTPSIYLENK RDAFFPPLHQ FCINPKNPVT
VIRGLAGALK LDLGLFSTKT LVEANNEHIV EVRTQLLQPA DENWDPSGTK KIWRYENKSS
HTTIAKYAQY QACSFQESLR EENERRTQVK DYSDNESTCS DNSGRRQKAP FKTIKCGINI
DLSDNKKWKL QLHELTKLPA FVRVVSAGNL LSHVGYTILG MNSVQLCMKV PGSRIPGHQE
NNNFCSVNIN IGPGDCEWFV VPEDYWGVLN DFCEKNNLNF LMSSWWPNLE DLYEANVPVY
RFIQRPGDLV WINAGTVHWV QAIGWCNNIT WNVGPLTAFQ YKLAVERYEW NKLQSVKSVV
PMVHLSWNMA RNIKVSDPKL FEMIKYCLLK ILKHCQTLRE ALVAAGKEVL WHGRINDEPA
PYCSICEVEV FNLLFVTNES NSQKTYIVHC QNCARKTSGN LENFVVLEQY KMEDLIQVYD
QFTLAPSLSS AS
