HAIR_MOUSE
ID HAIR_MOUSE Reviewed; 1182 AA.
AC Q61645; Q80Y47;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 141.
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 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=BALB/cJ; TISSUE=Skin;
RX PubMed=8052649; DOI=10.1073/pnas.91.16.7717;
RA Cachon-Gonzalez M.B., Fenner S., Coffin J.M., Moran C., Best S.,
RA Stoye J.P.;
RT "Structure and expression of the hairless gene of mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7717-7721(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- TISSUE SPECIFICITY: Expressed predominantly in brain, hair follicles
CC and interfollicular epidermis. No expression in dermis.
CC -!- DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL
CC motifs are essential for the association with nuclear receptors (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC the demethylation activity. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Hr are the cause of a number of pleiotropic
CC effects including structural abnormalities of epithelial cells in the
CC hair follicles, hair loss towards the end of the first hair growth
CC cycle, and the failure of subsequent hair growth cycles. Older mice
CC carrying a hr mutation have been reported to possess altered ratios of
CC T-cell-dependent B-cell responses. Mice homozygous for hr mutation are
CC uniquely sensitive to UV and chemically induced skin tumors.
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DR EMBL; Z32675; CAA83587.1; -; mRNA.
DR EMBL; BC049182; AAH49182.1; -; mRNA.
DR CCDS; CCDS27257.1; -.
DR PIR; I48378; I48378.
DR RefSeq; NP_068677.2; NM_021877.3.
DR RefSeq; XP_011243268.1; XM_011244966.1.
DR AlphaFoldDB; Q61645; -.
DR SMR; Q61645; -.
DR BioGRID; 200415; 3.
DR IntAct; Q61645; 3.
DR STRING; 10090.ENSMUSP00000022691; -.
DR iPTMnet; Q61645; -.
DR PhosphoSitePlus; Q61645; -.
DR PaxDb; Q61645; -.
DR PRIDE; Q61645; -.
DR ProteomicsDB; 269763; -.
DR Antibodypedia; 9297; 190 antibodies from 27 providers.
DR DNASU; 15460; -.
DR Ensembl; ENSMUST00000022691; ENSMUSP00000022691; ENSMUSG00000022096.
DR Ensembl; ENSMUST00000161069; ENSMUSP00000124816; ENSMUSG00000022096.
DR GeneID; 15460; -.
DR KEGG; mmu:15460; -.
DR UCSC; uc007uoj.2; mouse.
DR CTD; 55806; -.
DR MGI; MGI:96223; Hr.
DR VEuPathDB; HostDB:ENSMUSG00000022096; -.
DR eggNOG; KOG1356; Eukaryota.
DR GeneTree; ENSGT00940000161687; -.
DR InParanoid; Q61645; -.
DR OrthoDB; 1185631at2759; -.
DR PhylomeDB; Q61645; -.
DR TreeFam; TF324723; -.
DR BioGRID-ORCS; 15460; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Hr; mouse.
DR PRO; PR:Q61645; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q61645; protein.
DR Bgee; ENSMUSG00000022096; Expressed in lip and 140 other tissues.
DR ExpressionAtlas; Q61645; baseline and differential.
DR Genevisible; Q61645; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
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 2: Evidence at transcript level;
KW DNA-binding; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1182
FT /note="Lysine-specific demethylase hairless"
FT /id="PRO_0000083891"
FT DOMAIN 939..1150
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 595..620
FT /note="C6-type"
FT REGION 227..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 561..565
FT /note="LXXLL motif 1"
FT MOTIF 753..757
FT /note="LXXLL motif 2"
FT COMPBIAS 308..324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1000
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1002
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT CONFLICT 401
FT /note="P -> S (in Ref. 1; CAA83587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1182 AA; 127193 MW; 3AFABE96C6EB3241 CRC64;
MESMPSFLKD TPAWEKTAPV NGIVGQEPGT SPQDGLRHGA LCLGEPAPFW RGVLSTPDSW
LPPGFLQGPK DTLSLVEGEG PRNGERKGSW LGGKEGLRWK EAMLAHPLAF CGPACPPRYG
PLIPEHSGGH PKSDPVAFRP LHCPFLLETK ILERAPFWVP TCLPPYLMSS LPPERPYDWP
LAPNPWVYSG SQPKVPSAFG LGSKGFYHKD PNILRPAKEP LAESGMLGLA PGGHLQQACE
SEGPSLHQRD GETGAGRQQN LCPVFLGYPD TVPRAPWPSC PPGLVHSLGN IWAGPGSNSL
GYQLGPPATP RCPSPGPPTP PGGCCSSHLP AREGDLGPCR KCQDSPEGGS SGPGESSEER
NKADSRACPP SHHTKLKKTW LTRHSEQFEC PGGCSGKEES PATGLRALKR AGSPEVQGAS
RGPAPKRPSH PFPGTGRQGA RAWQETPETI IGSKAEAEQQ EEQRGPRDGR IRLQESRLVD
TSCQHHLAGV TQCQSCVQAA GEVGVLTGHS QKSRRSPLEE KQLEEEDSSA TSEEGGGGPG
PEASLNKGLA KHLLSGLGDR LCRLLRKERE ALAWAQREGQ GPAMTEDSPG IPHCCSRCHH
GLFNTHWRCS HCSHRLCVAC GRIAGAGKNR EKTGSQEQHT DDCAQEAGHA ACSLILTQFV
SSQALAELST VMHQVWAKFD IRGHCFCQVD ARVWAPGDGG QQKEPTEKTP PTPQPSCNGD
SNRTKDIKEE TPDSTESPAE DGAGRSPLPC PSLCELLAST AVKLCLGHDR IHMAFAPVTP
ALPSDDRITN ILDSIIAQVV ERKIQEKALG PGLRAGSGLR KGLSLPLSPV RTRLSPPGAL
LWLQEPRPKH GFHLFQEHWR QGQPVLVSGI QKTLRLSLWG MEALGTLGGQ VQTLTALGPP
QPTNLDSTAF WEGFSHPETR PKLDEGSVLL LHRTLGDKDA SRVQNLASSL PLPEYCAHQG
KLNLASYLPL GLTLHPLEPQ LWAAYGVNSH RGHLGTKNLC VEVSDLISIL VHAEAQLPPW
YRAQKDFLSG LDGEGLWSPG SQTSTVWHVF RAQDAQRIRR FLQMVCPAGA GTLEPGAPGS
CYLDAGLRRR LREEWGVSCW TLLQAPGEAV LVPAGAPHQV QGLVSTISVT QHFLSPETSA
LSAQLYHQGA SLPPDHRMLY AQMDRAVFQA VKAAVGALQE AK
