ID A0A3Q2HH39_HORSE Unreviewed; 1356 AA.
AC A0A3Q2HH39;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
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:ENSECAP00000033009.2,
GN ECO:0000313|VGNC:VGNC:19335};
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:ENSECAP00000033009.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000033009.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000033009.2,
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:ENSECAP00000033009.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000033009.2};
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|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 Ensembl; ENSECAT00000064347.2; ENSECAP00000033009.2; ENSECAG00000007369.4.
DR VGNC; VGNC:19335; KDM3A.
DR GeneTree; ENSGT00940000160135; -.
DR Proteomes; UP000002281; Chromosome 15.
DR Bgee; ENSECAG00000007369; Expressed in inner cell mass and 23 other cell types or tissues.
DR ExpressionAtlas; A0A3Q2HH39; baseline.
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:UP000002281}.
FT DOMAIN 1093..1316
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 340..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1356 AA; 151267 MW; 5A9488115A97BB51 CRC64;
MVLTLGESWP VLVGKRFLSV SAADGSDGGH DSWDVERVAE WPWLSGTIRA VSHPDVTKKD
LKVCVEFDGE SWRKRRWIEV YSLLRRAFLV EHNLVLAERK SPEISERIVQ LPAIMYKSLL
DKAGLGSITS IRFLGDQQRV FLSKDLLKPI QDVNSLRLSL MDNQNVSKEF QALIVKHLDE
SHLLQGDKNL VGSEVKIYSL DPSTQWFSAT VVNGNPASKT LQVNCEEIPA LKIVDPSLIH
VEVIHDNFVT CGNSTRIGAV KRKSSENNGS LVSKQAKSCS EGGTIAMTGI EDLQGKLFSY
SVQHILDSVF RAARASPSMC PVQSVPTPVF KEILLGCTAA TPPSKDPRQQ STPQAANSPP
NLGAKIPQGC HKQSLPEELS SCLNTKPEIL RTKPDVCKVG LLSSKSSQIG TGDLKTLSEP
KGSYTQLKTT TDEENRLESV PQPSTGLPKE CLPTKASSTA ELEIANTPEL QKHLEHAPST
SDVLSNKPEE KADVNSDNPN SCVGKKGEPS TLGCRSQNVK ESSVKVENES CCTRSNNKIQ
NAPSRKSVLT DPAKLKKLQQ SGEAFVQDDS CVNIIAQLPK CRECRLDSLR KDKEQQKDSP
VFCRFFHFRR LQFNKHGVLR VEGFLTPNKY DSEAIGLWLP LTKNVVGTDL DTAKYILANI
GDHFCQMVIS EKEAMSTIEP HRQVAWKRAV KGVREMCDVC DTTIFNLHWV CPRCGFGVCV
DCYRMKRKNC QQGAAYKTFS WIRCVKSQIH EPENLMPTQI IPGKALYDVG DIVHSVRAKW
GIKANCPCSN KQFKLFSKPA SKEDIKQTSL AGEKPTLGAV LQQAPLVLEP VAVAGEAASK
PAGSMKPTCP ASTSPLNWLA DLTSGNVNKE NKEKQPTMPI LKNEIKCLPP LPPLSKSSTV
LHTFNSTILT PVSNNNSGFL RNLLNSSTGK TENGLKNTPK ILDDIFASLV QNKTSSDLSK
RPQGLTIKPS ILGFDTPHYW LCDNRLLCLQ DPNNKSNWNV FRECWKQGQP VMVSGVHHKL
NTELWKPESF RKEFGNQEVD LVNCRTNEII TGATVGDFWD GFEDVPNRLK NEKEAMVLKL
KDWPPGEDFR DMMPSRFDDL MANIPLPEYT RRDGKLNLAS RLPNYFVRPD LGPKMYNAYG
LITPEDRKYG TTNLHLDVSD AANVMVYVGI PKGQSDQEEE VLKTIQDGDS DELTIKRFIE
GREKPGALWH IYAAKDTEKI REFLKKVSEE QGQENPADHD PIHDQSWYLD RSLRKRLHQE
YGVQGWAIVQ FLGDVVFIPA GAPHQVHNLY SCIKVAEDFV SPEHVKHCFW LTQEFRYLSQ
THTNHEDKLQ VKNVIYHAVK DAVAVLKASE SSFGKP
//
