HAIR_RAT
ID HAIR_RAT Reviewed; 1181 AA.
AC P97609;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Lysine-specific demethylase hairless;
DE EC=1.14.11.65 {ECO:0000250|UniProtKB:O43593};
DE AltName: Full=[histone H3]-dimethyl-L-lysine(9) demethylase hairless {ECO:0000305};
GN Name=Hr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=8987811; DOI=10.1523/jneurosci.16-24-07832.1996;
RA Thompson C.C.;
RT "Thyroid hormone-responsive genes in developing cerebellum include a novel
RT synaptotagmin and a hairless homolog.";
RL J. Neurosci. 16:7832-7840(1996).
RN [2]
RP DOMAIN, AND MUTAGENESIS OF 563-LEU-LEU-564 AND 756-LEU-LEU-756.
RX PubMed=14570920; DOI=10.1074/jbc.m308152200;
RA Moraitis A.N., Giguere V.;
RT "The co-repressor hairless protects RORalpha orphan nuclear receptor from
RT proteasome-mediated degradation.";
RL J. Biol. Chem. 278:52511-52518(2003).
CC -!- FUNCTION: Histone demethylase that specifically demethylates both
CC mono- and dimethylated 'Lys-9' of histone H3. May act as a
CC transcription regulator controlling hair biology (via targeting of
CC collagens), neural activity, and cell cycle.
CC {ECO:0000250|UniProtKB:O43593}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000250|UniProtKB:O43593};
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.
CC -!- DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL
CC motifs are essential for the association with nuclear receptors
CC (PubMed:14570920). {ECO:0000269|PubMed:14570920}.
CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC the demethylation activity. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53018.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U71293; AAC53018.1; ALT_INIT; mRNA.
DR AlphaFoldDB; P97609; -.
DR SMR; P97609; -.
DR STRING; 10116.ENSRNOP00000015716; -.
DR CarbonylDB; P97609; -.
DR iPTMnet; P97609; -.
DR PhosphoSitePlus; P97609; -.
DR PaxDb; P97609; -.
DR PRIDE; P97609; -.
DR UCSC; RGD:620634; rat.
DR RGD; 620634; Hr.
DR eggNOG; KOG1356; Eukaryota.
DR InParanoid; P97609; -.
DR PhylomeDB; P97609; -.
DR PRO; PR:P97609; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:RGD.
DR GO; GO:0016604; C:nuclear body; ISO:RGD.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:RGD.
DR GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:RGD.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:RGD.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IBA:GO_Central.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1181
FT /note="Lysine-specific demethylase hairless"
FT /id="PRO_0000083892"
FT DOMAIN 938..1149
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 594..619
FT /note="C6-type"
FT REGION 311..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 560..564
FT /note="LXXLL motif 1"
FT MOTIF 752..756
FT /note="LXXLL motif 2"
FT COMPBIAS 311..326
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 999
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1001
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1117
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MUTAGEN 563..564
FT /note="LL->AA: Decreases RORA protein stability. Strongly
FT decreases RORA protein stability; when associated with 752-
FT L--A-756."
FT /evidence="ECO:0000269|PubMed:14570920"
FT MUTAGEN 755..756
FT /note="LL->AA: Decreases RORA protein stability. Strongly
FT decreases RORA protein stability; when associated with 560-
FT L--A-564."
SQ SEQUENCE 1181 AA; 127307 MW; 834B7029CF8E88F0 CRC64;
MESMPSFLKD TPAWEKTAPV NGIVGQEPGT SPQDGLHHGA LCLGEPVPFW RGVLSAPDSW
LPPGFLQGPK DTLSVVEGEG SRNGERKANW LGSKEGLRWK EAMLAHPLAF CGPACPPRYG
PLIPEHSSGH PKSDPVAFRP LHCPFLLETK ILERAPFWVP TCLPPYLMSS LPPERSYDWP
LAPSPWVYSG SQPKVPSAFS LGSKGFYHKD PNILRPAKEP LAASESGMLG LAPGGHLQQA
CDAEGPSLHQ RDGETGAGRQ QNLCPVFLGY PDTVPRTPWP SCPPGLVHTL GNVWAGPGSN
SFGYQLGPPV TPRCPSPGPP TPPGGCCSSH LPAREGDPGP CRKCQDSPEG SSSGPGESSE
ERNKAGSRAS PPSHHTKLKK TWLTRHSEQF ECPGGCPGKG ESPATGLRAL KRAGSPEVQG
ARGPAPKRPS HTFPGTGRQG ARAWQETPET STGSKAEAQQ QEEQRGPRDG RIRLRESRLE
DTSCQHHLAG VTQCPSCVQA AGEVEILTSH SQKSHKLPLE EKPLEEDSCA TSEEGGGSSP
EASINKGLAK HLLSGLGDRL CRLLRKEREA LAWAQREGQG PAMTEDSPGI PHCCSRCHHG
LFNTHWRCSH CSHRLCVACG RIAGAGKNRE KTGSREQRTD DCAQEAGHAA CSLILTQFVS
SQALAELSTV MHQVWAKFDI RGHCFCQVDA RVWAPGDGGQ QKEPTEKTPP APQLSCNGDS
NRTKDIKEET PDSTESPAED RAGRSPLPCP SLCELLASTA VKLCLGHERI HMAFAPVTPA
LPSDDRITNI LDSIIAQVVE RKIQEKALGP GLRAGSGLRK GLSLPLSPVR TQLSPPGALL
WLQEPRPKHG FRLFQEHWRQ GQPVLVSGIQ KTLRLSLWGM EALGTLGGQV QTLTALGPPQ
PTSLDSTAFW KGFSHPEARP KLDEGSVLLL HRPLGDKDES RVENLASSLP LPEYCAHQGK
LNLASYLPLG LTLHPLEPQL WAAYGVNSHR GHLGTKNLCV EVSDLISILV HAEAQLPPWY
RAQKDFLSGL DGEGLWSPGS QTSTVWHVFR AQDAQRIRRF LQMVCPAGAG TLEPGAPGSC
YLDSGLRRRL REEWGVSCWT LLQAPGEAVL VPAGAPHQVQ GLVSTISVTQ HFLSPETSAL
SAQLCHQGAS LPPDHRMLYA QMDRAVFQAV KVAVGTLQEA K
