ID H0WCV6_CAVPO Unreviewed; 1258 AA.
AC H0WCV6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 63.
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:ENSCPOP00000020827.1};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000020827.1, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000020827.1}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000020827.1};
RG Ensembl;
RL Submitted (JUL-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; AAKN02036528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0WCV6; -.
DR STRING; 10141.ENSCPOP00000020827; -.
DR Ensembl; ENSCPOT00000021526.2; ENSCPOP00000020827.1; ENSCPOG00000023055.2.
DR VEuPathDB; HostDB:ENSCPOG00000023055; -.
DR eggNOG; KOG1356; Eukaryota.
DR GeneTree; ENSGT00940000160135; -.
DR HOGENOM; CLU_002991_0_0_1; -.
DR InParanoid; H0WCV6; -.
DR OMA; MDHQNIS; -.
DR TreeFam; TF324723; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000023055; Expressed in testis and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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: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 CDD; cd02208; cupin_RmlC-like; 1.
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:UP000005447}.
FT DOMAIN 995..1218
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 192..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 140570 MW; 30A0416B80AA9DC0 CRC64;
VCVEFDGESW RKRRWLEVYS LQRRAFLVEH HLVLAERKLP EISERIVQWP AIMYKSLLDK
AGLGSITSVR FLGDQQSVFL SKDLLKPIQD INNLRLSLTD NQKVSKEFQA LIVKHLDESH
LLQGDKNLVG SEVKIYSLDP STQWFSATVV NGNPTSKTLQ VNCEEIPALK IVDPSLIHVE
VVHENFVTCG NPTRMGGVKR KSSENNGSLV SKQSKSSSEA SPSVCPVQSV PTAVFKEILL
GCTAATPPSK DPRQQSTPQA ANSPPNLGAK IPQGCHKQSL PEELASCLNT KPEILRIKPD
VCKAGLLSSK SSQVGTGDLK ILSEPKSGCT QPKTNSDQEK RLESIPQPLT GLAKESLPMK
TSKAQLEIAS TPELQKHLEH APSTSDVLSN KPEVKAGVNS ASTCSGNKVE SSTLGCQPQN
LKETSVKLDN ESCSTRSNNK IQNAPARKSV LTDPAKLRKL QQSGEAFVQD DSCVNIIAQL
PKCRECRLDS LRKDKEQQKD SPVFCRFFHF RRLQFNKHGV LRVEGFLTPN KYDSEAIGLW
LPLTKNVVGT DLDTAKYILA NIGDHFCQMV ISEKEAMSTI EPHRQVAWKR AVKGVREMCD
VCDTTIFNLH WVCPRCGFGV CVDCYRMKRK NCQQGAAYKT FSWLRCVKSQ IHEPENLMPT
QIIPGKALYD VGDIVHSVRV KWGIKANCPC SNRQFKLFSK PPSKEDLKQT SSAGEKPTFS
AGLQQSPPAL EPAAVGEEAA SKAAANTKPA CPASSAPLNW LADLTSGTVN KENKEKQPVM
PTLKNEVRCL PPLPPLSKPS TVLHTFNSTI LTPVSNNNSG FLRNLLNSSA GKTENGLKNT
PKILDDIFAS LVQNKTSSDL SKRPQGLTIK PSILGFDTPH YWLCDNRLLC LQDPNNKSNW
NVFRECWKQG QPVMVSGVHH KLNTELWKPE SFRKEFGEQE VDLVNCRTNE IITGATVGDF
WDGFEDVPNR LKNDKEPMVL KLKDWPPGED FRDMMPSRFD DLMANIPLPE YTRRDGKLNL
ASKLPSYFVR PDLGPKMYNA YGLITPEDRK YGTTNLHLDV SDAANVMVYV GIPKGQCEQE
EEVLRTIQDG DSDELTIKRF IEGKEKPGAL WHIYAAKDTE KIREFLKKVS EEQGQENPAD
HDPIHDQSWY LDRALRKRLH QEYGVQGWAI VQFLGDVVFI PAGAPHQVHN LYSCIKVAED
FVSPEHVKHC FWLTQEFRYL SQTHTNHEDK LQVKNVIYHA VKDAVAMLKA SESSFSRP
//