ID A0A2U4AGE9_TURTR Unreviewed; 1758 AA.
AC A0A2U4AGE9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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|RefSeq:XP_019780050.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019780050.1};
RN [1] {ECO:0000313|RefSeq:XP_019780050.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019780050.1};
RG RefSeq;
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 RefSeq; XP_019780050.1; XM_019924491.2.
DR STRING; 9739.ENSTTRP00000005174; -.
DR GeneID; 101316921; -.
DR InParanoid; A0A2U4AGE9; -.
DR OrthoDB; 3473445at2759; -.
DR Proteomes; UP000245320; Chromosome 3.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070988; P:demethylation; IEA:UniProtKB-UniRule.
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:UP000245320}.
FT DOMAIN 1495..1718
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 254..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1758 AA; 191054 MW; 1C9B88EB2D49A7D6 CRC64;
MADAAASPVG KRLLLLFADT AASSSASVPA AAAAAGGDPG PALRTRAWRA GTVRAMSGAV
PQDLAIFVEF DGCSWKQHSW VKVHAEEVIV LLLEGSLVWA PRKDPVLVQG TRVSIAQWPA
LTFTPLVDKL GLGSVVPVEY LLDRELRFLS DANGLHLFQM GTDSQNQILL EHAALRETVN
ALISDQKLQE IFSRGPYSVQ GHRVKVYQPE GEESWLCGVV SHQDSITRLM EVSVTESGEI
KSVDPRLIHV MLMDNSAPQS EGGTLKAVKS SKGKKKRESI EGKDGRRRKS ASDSGCDPAS
KKLKGDRGEV DSNGSDGGEA SRGPWKGGNA SGEPGLDQRA KQPPTTFVPQ INRNIRFATY
TKENGRTLVV QDEPIGGDTP VPFTPYSTAT GQTPLAPEVG GAENKEAGKT LEQVGQGMVA
SAAVVTTASS TPTTVRISDT GLAAGTGPEK QKGSWSQAPG ENSRNSVLAS SGFGASLPSS
SQALTFGSGR SQSNGVLATE NKPLGFSFGC SSAPESQKDS DLSKNLFFQC MSQTLPTSNY
FTTVSESLAD DSSSRDSFKQ SLESLCKGRS ALGADSKSGS KAGSSVDRKV PAESMPTLTP
AFPRSLLNAR TPDSHENLFL QPPKLSREEP PNPFLAFVEK VEHSPFSSFA SQASGSSSSA
TTVTSKAAPS WPESHSSTDS ASLAKKKTLF ITTDSSKLVS GVLGSALTTG GPSLSAMGNG
RSSSPTSSLT QPIEMPTLSS SPTEERPTVG PGQQDNPLLK TFSNVFGRHS GSFLSSPADF
SQENKAPFEA VKRFSLDERS LACRQDSDSS TNSDLSDLSD SEEQLQAKTG LKGIPEHLMG
KLGPNGERSA ELLLGKGKGK QAPKGRPRTA PLKVGQSVLK DVSKVKKLKQ SGEPFLQDGS
CINVAPHLHK CRECRLERYR KFKEQEQDDS TVACRFFHFR RLIFTRKGVL RVEGFLSPQQ
SDPDAMNLWI PSSSLAEGID LETSKYILAN VGDQFCQLVM SEKEAMMMVE PHQKVAWKRA
VRGVREMCDV CETTLFNIHW VCRKCGFGVC LDCYRLRKSR PRSETEEIGD EEVFSWLKCA
KGQSHEPENL MPTQIIPGTA LYNIGDMVHA ARGKWGIKAN CPCISRQNKS VLRPAVTNGM
SQLPSINPSA SSGNETTFSG GGGTASVTQP ETDHVAKADS TDIRSDEPLK ADSSASNSNS
ELKAIRPPCP DTGPPSSALH WLADLATQKA KEETKEAGSL RSVLNKESHS PFGLDSFNST
AKVSPLTPKL FNSLLLGPTA SNNKTEGSSL RDLLHSGPGK LPQTPLDTGI PFPPVFSTSS
AGVKNKASLP NFLDHIIASV VENKKTSDAA KRACNLTDTQ KEVKEMVMGL NVLDPHTSHS
WLCDGRLLCL HDPSNKNNWK IFRECWKQGQ PVLVSGVHKK LKSELWKPEA FSQEFGDQDV
DLVNCRNCAI ISDVKVRDFW DGFEIICKRL RSEDGQPMVL KLKDWPPGED FRDMMPTRFE
DLMENLPLPE YTKRDGRLNL ASRLPSYFVR PDLGPKMYNA YGLITAEDRR VGTTNLHLDV
SDAVNVMVYV GIPIGEGAHD EEVLKTIDEG DADEVTKQRI HDGKEKPGAL WHIYAAKDAE
KIRELLRKVG EEQGQENPPD HDPIHDQSWY LDQTLRKRLY EEYGVQGWAI VQFLGDAVFI
PAGAPHQVHN LYSCIKVAED FVSPEHVKHC FRLTQEFRHL SNTHTNHEDK LQVKNIIYHA
VKDAVGTLKA HESKLARS
//
