ID A0A3Q2HUV1_HORSE Unreviewed; 1890 AA.
AC A0A3Q2HUV1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Lysine-specific demethylase {ECO:0000256|RuleBase:RU369087};
DE EC=1.14.11.65 {ECO:0000256|RuleBase:RU369087};
GN Name=KDM3B {ECO:0000313|VGNC:VGNC:19336};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000038078.1, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000038078.1, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000038078.1,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000038078.1}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000038078.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of
CC histone H3, thereby playing a central role in histone code.
CC {ECO:0000256|RuleBase:RU369087}.
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:0000256|RuleBase:RU369087};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|RuleBase:RU369087};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|RuleBase:RU369087};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU369087}.
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the
CC association with nuclear receptors. {ECO:0000256|RuleBase:RU369087}.
CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC the demethylation activity. {ECO:0000256|RuleBase:RU369087}.
CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC {ECO:0000256|RuleBase:RU369087}.
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DR SMR; A0A3Q2HUV1; -.
DR STRING; 9796.ENSECAP00000038078; -.
DR PaxDb; 9796-ENSECAP00000038078; -.
DR Ensembl; ENSECAT00000051158.2; ENSECAP00000038078.1; ENSECAG00000018062.4.
DR VGNC; VGNC:19336; KDM3B.
DR GeneTree; ENSGT00940000158095; -.
DR InParanoid; A0A3Q2HUV1; -.
DR OMA; ENSWVSA; -.
DR Proteomes; UP000002281; Chromosome 14.
DR Bgee; ENSECAG00000018062; Expressed in retina and 23 other cell types or tissues.
DR ExpressionAtlas; A0A3Q2HUV1; baseline.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0070988; P:demethylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR PANTHER; PTHR12549:SF8; LYSINE-SPECIFIC DEMETHYLASE 3B; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|RuleBase:RU369087};
KW Metal-binding {ECO:0000256|RuleBase:RU369087};
KW Nucleus {ECO:0000256|RuleBase:RU369087};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281}.
FT DOMAIN 1627..1850
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1890 AA; 204722 MW; 18CCBA0221D7DFF7 CRC64;
MGPPEERLGP GWCHGGLKDP PTSLPRPKLQ FPSLPQGALQ APGRLGRSAA RGPELSPRSG
ARGALCGARA AAPLPATGGA ARRRWLVVAV GGGGGESRPR VVRREALRED RALGGGGGGR
RRAGARVRPA LAMADAAASP VGKRLLLLFA DTAASASASV PAAAAAAAGG DPGPALRTRA
WRAGTVRAMS GAVPQDLAIF VEFDGCNWKQ HSWVKVHAEE VIVLLLEGSL VWAPRKDPVL
VQGARVSIAQ WPALTFTPLV DKLGLGSVVP VEYLLDRELR FLSDANGLHL FQMGTDSQNQ
ILLEHAALRE TVNALISDQK LQEIFSRGPY SVQGHRVKVY QPEGEESWLY GIVSHQDSIT
RLMEVSITES GEIKSVDPRL IHVMLMDNST PQSEGGTLKA VKSSKGKKKR ESIEGKDGRR
RKSASDSGCD SASKKLKGDR GEVDSNGSDG GEASRGPWKG GNTSGEPGLD QRAKQPPTTF
VPQINRNIRF ATYTKENGRT LVVQDEPVGG DTPVPFTSYS TATGQTSLAP EVGGAENKEA
GKTLEQVGQG LVASAAVVTT TSSTPTTVRI SDTGLGAGAG PEKQKGSRLQ APGENSRNSV
LASSGFGASL PSSSQPLTFG SGRSQSNGIL ATENKPLGFS FGCSSAPESQ KDTDLSKNLF
FQCMSQTLPT SNYFTTVSES LPDDSSSRDS FKQSLENLCK GRSTLGADTK SGSKAGSSVD
RKMPAESMPT LTPAFPRSLL NARTPESHEN LFLQPPKLSR EEPSNPFLAF VEKVEHSPFS
SFASQASGSS SSATTVTSKA APSWPESHSA DSTSLAKKKT LFITTDSSKL VPGVLGSALT
TGGPSLSAMG NGRSSSPTSS LTQPIEMPTL SSSPTEERPT VGPGQQDNPL LKTFSNVFGR
HSGSFLSPPA DFSQENKAPF EAVKRFSLDE RSLACRQDSD SSTNSDLSDL SDSEEQLQAK
TGLKGIPEHL MGKLGPNGER SAELLLGKGK GKQAPKGRPR TAPLKVGQSV LKDVSKVKKL
KQSGEPFLQD GSCINVAPHL HKCRECRLER YRKFKEQEQD DSTVACRFFH FRRLIFTRKG
VLRVEGFLSP QQSDPDAMNL WIPSSSLAEG IDLETSKYIL ANVGDQFCQL VMSEKEAMMM
VEPHQKVAWK RAVRGVREMC DVCETTLFNI HWVCRKCGFG VCLDCYRLRK SRPRSETEEM
GDEEVFSWLK CAKGQSHEPE NLMPTQIIPG TALYNIGDMV HAARGKWGIK ANCPCISRQN
KSVLRPAVTN GMSQLPSINP SASSGNETPF SGGGGTAAVT TPEPDHLPKA DGTDIRSDEP
LKADGSASNS NSELKAIRPP CPDTAPPSSA LHWLADLATQ KAKEETKEAG SLRSVLNKES
HSPFGLDSFN STAKVSPLTP KLFNSLLLGP TASNNKTEGS SLRDLLHSGP GKLPQTPLDT
GIPFPPVFST SSAGVKNKAS LPNFLDHIIA SVVENKKTSD AAKRACNLTD TQKEVKEMVM
GLNVLDPHTS HSWLCDGRLL CLHDPSNKNN WKIFRECWKQ GQPVLVSGVH KKLRSELWKP
EAFSQEFGDQ DVDLVNCRNC AIISDVKVRD FWDGFEIICK RLRSEDGQPM VLKLKDWPPG
EDFRDMMPTR FEDLMENLPL PEYTKRDGRL NLASRLPSYF VRPDLGPKMY NAYGLITAED
RRVGTTNLHL DVSDAVNVMV YVGIPIGEGA HDEEVLKTID EGDADEVTKQ RIHDGKEKPG
ALWHIYAAKD AEKIRELLRK VGEEQGQENP PDHDPIHDQS WYLDQTLRKR LYEEYGVQGW
AIVQFLGDAV FIPAGAPHQV HNLYSCIKVA EDFVSPEHVK HCFRLTQEFR HLSNTHTNHE
DKLQVKNIIY HAVKDAVGTL KAHESKLARS
//
