ID A0A452EE80_CAPHI Unreviewed; 1362 AA.
AC A0A452EE80;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Lysine-specific demethylase {ECO:0000256|RuleBase:RU369087};
DE EC=1.14.11.65 {ECO:0000256|RuleBase:RU369087};
GN Name=KDM3A {ECO:0000313|Ensembl:ENSCHIP00000010327.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000010327.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000010327.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000010327.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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|ARBA:ARBA00036306,
CC 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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, 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|ARBA:ARBA00037987, ECO:0000256|RuleBase:RU369087}.
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DR EMBL; LWLT01000009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9925.ENSCHIP00000010327; -.
DR Ensembl; ENSCHIT00000018104.1; ENSCHIP00000010327.1; ENSCHIG00000012854.1.
DR GeneTree; ENSGT00940000160135; -.
DR Proteomes; UP000291000; Chromosome 11.
DR Bgee; ENSCHIG00000012854; Expressed in fallopian tube and 16 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140683; F:histone H3K9me/H3K9me2 demethylase activity; IEA:Ensembl.
DR GO; GO:0005506; F:iron ion binding; IEA:Ensembl.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IEA:Ensembl.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:Ensembl.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0070988; P:demethylation; IEA:UniProtKB-UniRule.
DR GO; GO:0046293; P:formaldehyde biosynthetic process; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0007290; P:spermatid nucleus elongation; IEA:Ensembl.
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:SF7; LYSINE-SPECIFIC DEMETHYLASE 3A; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000291000}.
FT DOMAIN 1099..1322
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1362 AA; 152016 MW; 79F661B63DCEF2D3 CRC64;
MGGRGRRGWR DRVLSLTSSP PPPGVRSSER GRSPSCSVET MVLTLGESWP VLVGKRFLSL
SAADGSDGGH DSWDVERVAE WPWLSGTIRA VSHTDVTKKD LKVCVEFDGE SWKKRRWIDV
YSLLRRAFLV EHNLVLAERK SPEISERIVQ WPAIMYKSLL DKAGLGSITS IRFLGDQQRV
FLSKDLLKPI QDVNNLRLSL MDNQSVSKEF QALIVKHLDE SHLLQGDKNL VGSEVKIYSL
DPSTQWFSAT IVNGNPMSKT LQVNCEEIPA LKIVDPSLIH VEVVHDNFVT CGNSTRMGAV
KRKSSENNGN LVSKQAKSCS EASPSVCPVQ SVPTTVFKEI LLGCTAATPP SKDPRQQSTP
QAANSPPNLG AKIPQGCHKQ ILPELSSCLN TKPEILRTKP DVACKVELLS SKSSQIGTGD
LQTLSEPKGS CSQLKSTDEE SSVESLPPSS TDPPKECTPI KAASVTELEI TKAPELQKHF
EHAPSTSDVL SKKPEEKAAV NSNSPNSCVE KRGEPSTLGC QSQNIKASSA KVDPESCCTR
SNNKFQNAPS RKSVLTDPAK LKKLQQSGEA FVQDDSCVNI VAQLPKCREC RLDSLRKDKE
QQKDSPVFCR FFHFRRLQFN KHGVLRVEGF LTPNKYDSEA IGLWLPLTRN VVGTDLDTAK
YILANIGDHF CQMVISEKEA MSTIEPHRQV AWKRAVKGVR EMCDVCDTTI FNLHWVCPRC
GFGVCVDCYR MKRKNCQQGA AYKTFNWLRC VKSQIHEPEN LMPTQIIPGK ALYDVGDIVH
SVRAKWGIKA NCPCSNRQFK LFSKPASKED IKQTSLTGEK ATLGTMLPQN PSGLEPVTVG
GEAASKPASS VKPACPASTS PLNWLADLTS GNVNKENKEK QPAMPILKNE IKCLPPLPPL
SKSSTVLHTF NSTILTPVSN NNSGFLRNLL NSSTGKTENG LKNTPKILDD IFASLVQNKT
CSDLPKRPQG LTIKPSILGF DTPHYWLCDN RLLCLQDPNN KSNWNVFREC WKQGQPVMVS
GVHHKLNTEL WKPESFRREF GNQEVDLVNC RTNEIITGAT VGDFWDGFED VPNRLKNEKE
PMVLKLKDWP PGEDFRDMMP SRFDDLMANI PLPEYTRRDG KLNLASRLPN YFVRPDLGPK
MYNAYGLITP EDRKYGTTNL HLDVSDAANV MVYVGIPKGQ CDQEEEVLKT IQDGDSDELT
IKRFIEGKEK PGALWHIYAA KDTEKIREFL KKVSEEQGQE NPADHDPIHD QSWYLDRSLR
KRLHQEYGVQ GWAIVQFLGD VVFIPAGAPH QVHNLYSCIK VAEDFVSPEH VKHCFWLTQE
FRYLSQTHTN HEDKLQVKNV IYHAVKDAVA MLKASESSFG KP
//
