ID H0UYC9_CAVPO Unreviewed; 1711 AA.
AC H0UYC9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 55.
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|Ensembl:ENSCPOP00000002138.3};
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:ENSCPOP00000002138.3, 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:ENSCPOP00000002138.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000002138.3};
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|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}.
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; AAKN02009860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02009861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCPOT00000002386.3; ENSCPOP00000002138.3; ENSCPOG00000002353.4.
DR VEuPathDB; HostDB:ENSCPOG00000002353; -.
DR GeneTree; ENSGT00940000158095; -.
DR HOGENOM; CLU_002991_0_0_1; -.
DR TreeFam; TF324723; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000002353; Expressed in pituitary gland and 13 other cell types or tissues.
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:UP000005447};
KW Transcription {ECO:0000256|ARBA:ARBA00023163}.
FT DOMAIN 1448..1671
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 206..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1711 AA; 187112 MW; 6BFB6ABA03DC5780 CRC64;
LKLNSDPPAS ASQVLGLQTC ATMIFVEFDG CNWKQHSWVK VHAEEVIVLL LEGSLVWAPR
KDPRVSIAQW PALTFTPLVD KLGLGSVVPV EYLLDRELRF LSDTTGLHLF QMGTDSQNQI
LLEHAALRET VNALISDQKL QEIFSRGPYS VQGHRVKVYQ PEGEEGWIYG IVSHQDSITR
LMEVSITESG EIKSVDPRLI HVMLVDSSTP QSEGGTLKAV KSSKGKKKRE SIEGKDGRRR
KSASDSGCDP SSKKLKGDRG EVDSNGNDGS EASRGPWKEG NASGEPGLDQ RAKQPSSTFV
PQINRNIRFA TYTKENGRTL VVQDEPMGGD TPVSFTPYST ATGQTPLAPE VGGAENKEAG
KTLEQVGQGM VASAAVVTTA SSTPTTVRIS DSGLATGIGP EKQKGWSQAS GEISRNSILG
SSGFGASLPS LSQPLTFGSG RNQSNGVLIT ENKPLGFSFG CGSAPEAQKD SDLSKNLFFQ
CMSQTLPTSN YFTTVSESLA DDSSSRDSFK QSLESLSSGL CKSRSTLGAD TKLGSKAGSS
VDRKVPAESM PTLTPAFPRS LLNTRTPESH ENLFLQPPKL SREEPSNPFL AFVEKVEHSP
FSSFASQASS SSATTVTSKA APSWPESHSS TDSTCLTKKK PLFITTDSSK LVPGVLGSTL
STGSPSLSAM GNGRSSSPTS SLTQPIEMPT LSSSPTEERP TVGPGQQDNP LLKTFSNVFG
RHSGSFLSSP ADFSQENKAP FEAVKRFSLD ERSLACRQDS DSSTNSDLSD LSDSEEQLQA
KTGLKGIPEH LMGKLGPNGE RTAELLLGKG KGKQTPKGRP RTAPLKVGQS VLKDVSKVKK
LKQSGEPFLQ DGSCINVAPH LHKCRECRLE RYRKFKEQEQ DDSTVACRFF HFRRLIFTRK
GVLRVEGFLS PQQSDPDAMN LWIPSSSLAE GIDLETSKYI LANVGDQFCQ LVMSEKEAMM
MVEPHQKVAW KRAVRGVREM CDVCETTLFN IHWVCRKCGF GVCLDCYRLR KSRPRSETEE
MGDEEVFSWL KCAKGQSHEP ENLMPTQIIP GTALYNIGDM VHAARGKWGI KANCPCISRQ
NKSVLRPAVT NGMSQLPSIN PSASSGNETT FSGGGGTATG TAPEPSHGPK GDGTDVRPEE
TLRADGSASN SNSELKAIRP PCPDTTPPSS ALHWLADLAT QKAKEETKEA GSLRSVLNKE
SHSPFGLDSF NSTAKVSPLT PKLFNSLLLG PTASNNKTEG SSLRDLLHSG PGKLPQTPLD
TGIPFPPVFS TSSAGVKSKA SLPNFLDHII ASVVENKKTS DASKRACNVT DTQKEVKEMV
MGLNVLDPHT SHSWLCDGRL LCLHDPSNKN NWKIFRECWK QGQPVLVSGV HKKLKSELWK
PEAFSQEFGD QDVDLVNCRN CAIISDVKVR DFWDGFEIIC KRLRSEDGQP MVLKLKDWPP
GEDFRDMMPT RFEDLMENLP LPEYTKRDGR LNLASRLPSY FVRPDLGPKM YNAYGLITAE
DRRVGTTNLH LDVSDAVNVM VYVGIPIGEG AHDEEVLKTI DEGDADEVTK QRIHDGNEKP
GALWHIYAAK DAEKIRELLR KVGEEQGQEN PPDHDPIHDQ SWYLDQTLRK RLYEEYGVQG
WAIVQFLGDA VFIPAGAPHQ VHNLYSCIKV AEDFVSPEHV KHCFRLTQEF RHLSNTHTNH
EDKLQVKNII YHAVKDAVGT LKAHESKLAR S
//
