JMJD6_CAEEL
ID JMJD6_CAEEL Reviewed; 400 AA.
AC Q9GYI4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Bifunctional arginine demethylase and lysyl-hydroxylase psr-1;
DE EC=1.14.11.-;
DE AltName: Full=Phosphatidylserine receptor 1;
GN Name=psr-1; ORFNames=F29B9.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP INTERACTION WITH CED-5 AND CED-12.
RX PubMed=14645848; DOI=10.1126/science.1087641;
RA Wang X., Wu Y.-C., Fadok V.A., Lee M.-C., Gengyo-Ando K., Cheng L.-C.,
RA Ledwich D., Hsu P.-K., Chen J.-Y., Chou B.-K., Henson P., Mitani S.,
RA Xue D.;
RT "Cell corpse engulfment mediated by C. elegans phosphatidylserine receptor
RT through CED-5 and CED-12.";
RL Science 302:1563-1566(2003).
CC -!- FUNCTION: Dioxygenase that can both act as a histone arginine
CC demethylase and a lysyl-hydroxylase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with ced-5 and ced-12.
CC {ECO:0000269|PubMed:14645848}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Worms lacking psr-1 display more cell corpses than in
CC wild-type animals.
CC -!- SIMILARITY: Belongs to the JMJD6 family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to constitute the phosphatidylserine
CC receptor, a receptor that mediates recognition of phosphatidylserine, a
CC specific marker only present at the surface of apoptotic cells, and
CC participates in apoptotic cell phagocytosis. However, some results
CC strongly suggest that it does not constitute the receptor for
CC phosphatidylserine and is not involved in apoptotic cell removal.
CC {ECO:0000305}.
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DR EMBL; FO081255; CCD70226.1; -; Genomic_DNA.
DR RefSeq; NP_001040940.1; NM_001047475.3.
DR AlphaFoldDB; Q9GYI4; -.
DR SMR; Q9GYI4; -.
DR BioGRID; 42358; 10.
DR DIP; DIP-24340N; -.
DR IntAct; Q9GYI4; 1.
DR STRING; 6239.F29B9.4c; -.
DR EPD; Q9GYI4; -.
DR PaxDb; Q9GYI4; -.
DR PRIDE; Q9GYI4; -.
DR EnsemblMetazoa; F29B9.4a.1; F29B9.4a.1; WBGene00004205.
DR EnsemblMetazoa; F29B9.4a.2; F29B9.4a.2; WBGene00004205.
DR GeneID; 177229; -.
DR UCSC; F29B9.4a.1; c. elegans.
DR CTD; 177229; -.
DR WormBase; F29B9.4a; CE27146; WBGene00004205; psr-1.
DR eggNOG; KOG2130; Eukaryota.
DR HOGENOM; CLU_016785_8_0_1; -.
DR InParanoid; Q9GYI4; -.
DR PhylomeDB; Q9GYI4; -.
DR Reactome; R-CEL-3214842; HDMs demethylate histones.
DR PRO; PR:Q9GYI4; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004205; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9GYI4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:WormBase.
DR GO; GO:0033749; F:histone H3-methyl-arginine-3 demethylase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106140; F:P-TEFb complex binding; IBA:GO_Central.
DR GO; GO:0070815; F:peptidyl-lysine 5-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:WormBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IDA:WormBase.
DR GO; GO:0018395; P:peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine; ISS:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..400
FT /note="Bifunctional arginine demethylase and lysyl-
FT hydroxylase psr-1"
FT /id="PRO_0000129378"
FT DOMAIN 146..310
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 342..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 202
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 290
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 400 AA; 46618 MW; 5E479FA53532C48F CRC64;
MSLGRDRYSL PRTYKRVSHA KDKARPELRK FGWETLGYSE SFNLPPFRDS IQRVDGNNLT
VEEFRRDFER PRIPVIITGL TDNWAAKDKW TVERLSKKYR NQNFKCGEDD NGNSVRMKMK
YYHDYMLNNK DDSPLYIFDS SFAERRKTKK LSEDYSVPKF FEDDLFHYAD DKKRPPHRWF
VMGPARSGTA IHIDPLGTSA WNSLLQGHKR WVLIPPIAPR DLVKPMAHEK GKHPDEGITW
FQTVYKRVRS PSWPKEYAPI ECRQGPGETM FVPSGWWHVV INEEYTIAVT HNYCSVENLH
LVWPKTVKGR PKLSKHWVKR LTEQRPELLE IIKSASEIPL YDMNESSSDS SSSSSSSDDS
SDESDCDDSG RCGGRKRKND DRSNECPEKM STTYFQNSLV
