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   27-MAR-2024, entry version 162.
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; 10090-ENSMUSP00000070012; -.
DR   ProteomicsDB; 297903; -.
DR   AGR; MGI:894810; -.
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:0071558; F:histone H3K27me2/H3K27me3 demethylase activity; IBA:GO_Central.
DR   GO; GO:0051864; F:histone H3K36 demethylase activity; IMP:MGI.
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 formation; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   Gene3D; 1.20.58.1370; -; 2.
DR   Gene3D; 2.10.110.20; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR046941; KDM6_GATAL_sf.
DR   InterPro; IPR048562; KDM6A_B-like_C-hel.
DR   InterPro; IPR048560; KDM6A_B-like_GATAL.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR14017:SF25; HISTONE DEMETHYLASE UTY; 1.
DR   PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF21322; KDM6_C-hel; 1.
DR   Pfam; PF21326; KDM6_GATAL; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00028; TPR; 7.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF81901; HCP-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 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
//