JARD2_CHICK
ID JARD2_CHICK Reviewed; 1233 AA.
AC Q5F363;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein Jumonji;
DE AltName: Full=Jumonji/ARID domain-containing protein 2;
GN Name=JARID2; Synonyms=JMJ; ORFNames=RCJMB04_32g20;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Regulator of histone methyltransferase complexes that plays
CC an essential role in embryonic development, including heart and liver
CC development, neural tube fusion process and hematopoiesis. Acts as an
CC accessory subunit for the core PRC2 (Polycomb repressive complex 2)
CC complex, which mediates histone H3K27 (H3K27me3) trimethylation on
CC chromatin. Binds DNA and mediates the recruitment of the PRC2 complex
CC to target genes in embryonic stem cells, thereby playing a key role in
CC stem cell differentiation and normal embryonic development (By
CC similarity). In cardiac cells, it is required to repress expression of
CC cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3
CC (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases.
CC Also acts as a transcriptional repressor of ANF via its interaction
CC with GATA4 and NKX2-5. Participates in the negative regulation of cell
CC proliferation signaling. Does not have histone demethylase activity (By
CC similarity). {ECO:0000250|UniProtKB:Q62315,
CC ECO:0000250|UniProtKB:Q92833}.
CC -!- SUBUNIT: Associates with the PRC2 complex.
CC {ECO:0000250|UniProtKB:Q92833}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with the PRC2 complex
CC on chromatin. {ECO:0000250|UniProtKB:Q92833}.
CC -!- DOMAIN: The ARID domain is required to target the PRC2 complex to its
CC target genes. {ECO:0000250|UniProtKB:Q92833}.
CC -!- SIMILARITY: Belongs to the JARID2 family. {ECO:0000305}.
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DR EMBL; AJ851787; CAH65421.1; -; mRNA.
DR RefSeq; NP_001012880.1; NM_001012862.1.
DR AlphaFoldDB; Q5F363; -.
DR SMR; Q5F363; -.
DR STRING; 9031.ENSGALP00000020711; -.
DR PaxDb; Q5F363; -.
DR GeneID; 420839; -.
DR KEGG; gga:420839; -.
DR CTD; 3720; -.
DR VEuPathDB; HostDB:geneid_420839; -.
DR eggNOG; KOG1246; Eukaryota.
DR InParanoid; Q5F363; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; Q5F363; -.
DR PRO; PR:Q5F363; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0031061; P:negative regulation of histone methylation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR004198; Znf_C5HC2.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Developmental protein; Differentiation; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1233
FT /note="Protein Jumonji"
FT /id="PRO_0000391907"
FT DOMAIN 546..587
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 610..702
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 873..1037
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..168
FT /note="Sufficient for interaction with the PRC2 complex"
FT /evidence="ECO:0000250|UniProtKB:Q92833"
FT REGION 165..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 102..108
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q92833"
FT MOTIF 863..867
FT /note="GSGFP motif"
FT /evidence="ECO:0000250|UniProtKB:Q92833"
FT COMPBIAS 82..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1233 AA; 138110 MW; 6386F8A089BBA7B7 CRC64;
MSKERPKRNI IQKEYDDSDG IPWSEERVVR KVLYLSLKEF KNAQKRQHGD GISGSLKAVN
GLLTNGQSKG LESEQLENEK DDASQVSSTS NDISSSDFEE GPSRKRPRLQ AQRKFAQSQP
NSPSTTPIKI VEPLLPPPAT QISDLSKRKP KTEDFLTFLC LRGSPALPSN MVYFGSSQDD
EDEEEEEEET EDTKTATNNA SSSCQSTPRK GKTHKQVPNG QVFNGSSKSL KEKEPAQKHK
SKEATPGKEK NSEHKAESRK DQAAANHHPT TNTGSSTKGL TANNHHTLHR SAQDLRKQVS
KVNGITRMSS PSANAASAKK MRDVRPSPSK TVKYTATVTK GTVTYTKAKK ELVKETKLNH
HKPSSPVNHT ISGKLESSNA KTRKQVLSLG ASKSNNTAVN GVKVNGKLNQ KTCTKEVGRQ
LREGLRNSKR RLEETNHIDK IQSPTKRMKG AVNLAEAASK KAVVEKPLLN GHLKKEVPEK
NLERNRPKRA TAGKSTPGKQ AHGKTENASC ENRSTSQAES LHKPQDSMGK HEKGSSKSGW
GMLGEIPILR PSTKEFHDPL IYIESVRAQV EKYGMCRVIP PPDWRPECKL NDEMRFVTQI
QHIHKLGRRW GPNVQRLACI KKHLKSQGIT MDELPLIGGC ELDLACFVQL INEMGGMQQV
TDLKKWNKLA DMLRIPKTAQ DRLAKLQEAY CQYLLSYDSL SPEEHKKLEK EVLLEKEILE
KRKGPLEGHS ENAYKFHSLP RFEPKNGLIN GVVHKNGFRN KLKEVDVPLK TGRRRLFAQE
KETTKDDEEE EEEGVLSDLH KCIYKGRSVS LTTFYRTARN IMNMCFTKEP TVAEVEQEYW
RLVEQKDSHV AVHCGKVDTN THGSGFPVGK SEPFSRHGWN LTVLPNNTGS ILRHLGAVPG
VTIPWLNIGM VFSTSCWSRD QNHLPYIDYL HTGADCIWYC IPAAEENKLD DVVHTLLQAN
GTPGLEMLES NVMISPEILC KEGIRVHRTV QQSGQFVVCF PGSFVSKVCC GYSVSETVHF
ATTQWTSMGF KTAKEMKRRR IAKPFSMEKL LYQIATAEAK KENGPTLSTI SSLLGELRDT
ELRQRRQLYE AGLHSSARYG SHDSSSTAMD GKKKPRKWLQ LETSERRCQI CQHLCYLSMV
VQENENVVFC LECALRHVEK QKSCRGLKMM YRYDEEQIIS LVNQICGKVS GKNGSIENCI
SKPTPKRGPR KRATVDVPSS RLSSSSSSKS ASS
