UTY_PANTR
ID UTY_PANTR Reviewed; 1079 AA.
AC Q6B4Z3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Histone demethylase UTY;
DE EC=1.14.11.68 {ECO:0000250|UniProtKB:O14607};
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hughes J.F., Pyntikova T., Skaletsky H., Minx P.J., Rozen S., Wilson R.K.,
RA Page D.C.;
RT "The DNA sequence of the chimpanzee Y chromosome.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Male-specific histone demethylase that catalyzes
CC trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has
CC relatively low lysine demethylase activity.
CC {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: Interacts with TLE1 and TLE2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000305}.
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DR EMBL; AY679781; AAT84369.1; -; mRNA.
DR RefSeq; NP_001009002.1; NM_001009002.1.
DR AlphaFoldDB; Q6B4Z3; -.
DR SMR; Q6B4Z3; -.
DR STRING; 9598.ENSPTRP00000058594; -.
DR PaxDb; Q6B4Z3; -.
DR GeneID; 449579; -.
DR KEGG; ptr:449579; -.
DR CTD; 7404; -.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG1246; Eukaryota.
DR InParanoid; Q6B4Z3; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0044666; C:MLL3/4 complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0071557; P:histone H3-K27 demethylation; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..1079
FT /note="Histone demethylase UTY"
FT /id="PRO_0000106412"
FT REPEAT 90..123
FT /note="TPR 1"
FT REPEAT 127..160
FT /note="TPR 2"
FT REPEAT 164..198
FT /note="TPR 3"
FT REPEAT 202..235
FT /note="TPR 4"
FT REPEAT 240..280
FT /note="TPR 5"
FT REPEAT 281..314
FT /note="TPR 6"
FT REPEAT 316..348
FT /note="TPR 7"
FT REPEAT 349..382
FT /note="TPR 8"
FT REGION 558..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14607"
SQ SEQUENCE 1079 AA; 118032 MW; 013410EE18CF2EE0 CRC64;
MKSCGVSLTT AAVAFGDEAK KMAAGKASRE GEEEPLSLTV EEREALGDMD SRLFGFVRLH
EDGARTKTLL GKAVRCYESL ILKAEGKVES DFFCQLGHFN LLLEDYSKAL SAYQRYYSLQ
ADYWKNAAFL YGLGLVYFYY NAFHWAIKAF QDVLYVDPSF CRAKEIHLRL GLMFKVNTDY
KSSLKHFQLA LIDCNPCTLS SAEIQFHIAH LYETQRKYHS AKEAYEQLLQ TENLPAQVKA
TVLQQLGWMH HNMDLVGDKA TKESYAIPYL QKSLEADPNS GQSWYFLGRC YSSIGKVQDA
FVSYRQSIDR SEASADTWCS IGVLYQQQNQ PIDALQAYIC AVQLDHGHAA AWMDLGTLYE
SCNQPQDAIK CYLNAARSKR CSNTSTLAAR IKFLQNGSDN WNGGQSLSHH PVQQVYSLCL
TPQKLQHLEQ LRANRDNLNP AQKHQLEQLE SQFVLMQQMR HKEVAQVRTT GIHNGAIADS
SLPTNSVSNR QPHAALTRVS SVSQPGVRPA CVEKLLSNGA FSAGCIPCGT SKILGSTDTI
LLGSNCIAGS ESNGNVPYLQ QNTHTLPHSH TDLNSSTEEP WRKQLSNSTQ GLHKSQSSCL
SGPNEEQPLF STGSAQYHQA TSTGIKKSNE HLTLPSNSVP QGDADSHLSS HTATSGGQQG
IMFTKESKPS KNRSLVPETS RHTGDPSNGC ADVKGLSNHV HQLIADAVSS PNHGDSPNLL
IADNPQLSAL LIGKANGNVG TGTCDKVNNI HPAVHTKTDH SVASSPSSAI STATPSPKST
EQRSINSVTS LNSPHSGLHT VNGEGLGNSQ SSTKVDLPLV SHRSTSQIIP SMSVSICPSS
TEVLKACRNP GKNGLSNSCI LLDKCPPPRP PTSPYPPLPK DKLNPPTPSI YLENKRDAFF
PPLHQFCTNP KNPVTVIRGL AGALKLDLGL FSTKTLVEAN NEHIVEVRTQ LLQPADENWD
PTGTKKIWRC ESNRSHTTIA KYAQYQASSF QESLRAGMQW CDLSSLQPPP PGFKRFSHLS
LPNSWNYRHL PSCPTNFCIF VETGFHHVGQ AHLELLTSGG LLASASQSAG ITGVSHHAR
