GenomeNet

Database: UniProt
Entry: H0WCV6_CAVPO
LinkDB: H0WCV6_CAVPO
Original site: H0WCV6_CAVPO 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system