JMJD6_HYDVU
ID JMJD6_HYDVU Reviewed; 385 AA.
AC Q6Q4H1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Bifunctional arginine demethylase and lysyl-hydroxylase PSR;
DE EC=1.14.11.-;
DE AltName: Full=Phosphatidylserine receptor;
GN Name=PSR;
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], LACK OF INVOLVEMENT IN PHAGOCYTOSIS,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 142-LYS--LYS-145; 167-LYS--ARG-169
RP AND 377-LYS--LYS-380.
RX PubMed=15193161; DOI=10.1186/1471-2121-5-26;
RA Cikala M., Alexandrova O., David C.N., Proeschel M., Stiening B.,
RA Cramer P., Boettger A.;
RT "The phosphatidylserine receptor from Hydra is a nuclear protein with
RT potential Fe(II) dependent oxygenase activity.";
RL BMC Cell Biol. 5:26-26(2004).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15193161}.
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, its nuclear
CC localization and the fact that it is not involved in phagocytosis
CC during apoptosis strongly suggest that it does not constitute the
CC receptor for phosphatidylserine and is not involved in apoptotic cell
CC removal. {ECO:0000305}.
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DR EMBL; AY559448; AAS59176.1; -; mRNA.
DR RefSeq; NP_001296707.1; NM_001309778.1.
DR RefSeq; XP_002154420.3; XM_002154384.3.
DR AlphaFoldDB; Q6Q4H1; -.
DR SMR; Q6Q4H1; -.
DR GeneID; 100209631; -.
DR KEGG; hmg:100209631; -.
DR OMA; AVSENFW; -.
DR OrthoDB; 609279at2759; -.
DR Proteomes; UP000694840; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070815; F:peptidyl-lysine 5-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0018395; P:peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine; ISS:UniProtKB.
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..385
FT /note="Bifunctional arginine demethylase and lysyl-
FT hydroxylase PSR"
FT /id="PRO_0000129380"
FT DOMAIN 141..305
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 337..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 377..380
FT /note="Nuclear localization signal"
FT COMPBIAS 337..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 197
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 285
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT MUTAGEN 142..145
FT /note="Missing: Does not affect nuclear localization."
FT /evidence="ECO:0000269|PubMed:15193161"
FT MUTAGEN 167..169
FT /note="Missing: Does not affect nuclear localization."
FT /evidence="ECO:0000269|PubMed:15193161"
FT MUTAGEN 377..380
FT /note="Missing: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:15193161"
SQ SEQUENCE 385 AA; 44240 MW; 754994A9E8AA086F CRC64;
MDKRTDDAVR ETKLKARPEL KGDEGWTRLG YANNFDLSYQ HIKDTLPRIH CKSISHDEFI
ARYEKPRIPV ILTGCTDSWL ANQKWKLSSL AKKYRNQKFK VGEDNDGFSV KMKMKYYIEY
LKHQKDDSPL YIFDGSYGEH PKKRKLLDDY HPPSFFQDDL FKYAGEKRRP PYRWIVIGPA
RSGTGIHIDP LGTSAWNALI SGHKRWMMFP TETPKHLLEV SKQDGQHQSG EGIQWFVKVY
PKVKSPTWPK EYAPLEIIQH PGETVFVPGG WWHVVLNLDQ TVAVTQNFSS PTNFHVVWHK
TVRGRPKLSQ KWLRALKIYR PEIARIAAEV DLLRQSGLAS DSSSDSSSSS SSSSSEESNS
ESEESTADSI PEQSESKRRK VDAVE
