ID   RSBNL_XENTR             Reviewed;         782 AA.
AC   Q28DE6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Lysine-specific demethylase RSBN1L {ECO:0000305};
DE            EC=1.14.11.- {ECO:0000250|UniProtKB:Q80T69};
DE   AltName: Full=Round spermatid basic protein 1-like;
GN   Name=rsbn1l; ORFNames=TEgg039d07.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lysine-specific demethylase that specifically demethylates
CC       methylated lysine residues of proteins. {ECO:0000250|UniProtKB:Q80T69}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q80T69};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9GRZ3};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9GRZ3}.
CC   -!- SIMILARITY: Belongs to the round spermatid basic protein 1 family.
CC       {ECO:0000305}.
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DR   EMBL; CR855556; CAJ82228.1; -; mRNA.
DR   RefSeq; NP_001017304.1; NM_001017304.2.
DR   AlphaFoldDB; Q28DE6; -.
DR   SMR; Q28DE6; -.
DR   STRING; 8364.ENSXETP00000042710; -.
DR   PaxDb; Q28DE6; -.
DR   PRIDE; Q28DE6; -.
DR   Ensembl; ENSXETT00000042710; ENSXETP00000042710; ENSXETG00000019725.
DR   GeneID; 550058; -.
DR   KEGG; xtr:550058; -.
DR   CTD; 222194; -.
DR   Xenbase; XB-GENE-5732741; rsbn1l.
DR   eggNOG; KOG4425; Eukaryota.
DR   HOGENOM; CLU_009952_0_1_1; -.
DR   InParanoid; Q28DE6; -.
DR   OMA; VQNNLRR; -.
DR   OrthoDB; 930910at2759; -.
DR   PhylomeDB; Q28DE6; -.
DR   TreeFam; TF323256; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000019725; Expressed in 2-cell stage embryo and 14 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR026306; RSBN1/Dpy-21.
DR   PANTHER; PTHR13354; PTHR13354; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..782
FT                   /note="Lysine-specific demethylase RSBN1L"
FT                   /id="PRO_0000299415"
FT   REGION          1..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..222
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..669
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         515
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT   BINDING         518
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT   BINDING         520
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT   BINDING         612
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT   BINDING         620
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
SQ   SEQUENCE   782 AA;  88747 MW;  8D2FE42B87BFF246 CRC64;
     MAELWTSIGA APAEKQEQPP KPRDVILVKS PALLSSTSSS DLHPLKKIRT DDKCLKPKRV
     NGEGGGGNSK GGPGHSSSVT WSFPQGASSS SSSLCLGNPG KTEKPTKPRE KRDKEKKRRR
     EGGGEENGEV KTAGIPCLPA ASPVTAVRNE IKIKDKEKQK EKKKHKLMNE IKKENGEVKL
     LQKGTNEKPR PNAEDLQIKK VKKKKKKKHK EGEKRKHPKM HSKSIQTICS GLVSDAENNQ
     FKEAKVEKDV YFMGLLGKTE VKKVKVEKEI PFVSLKEPRV EHKLKCLDSL EFKHLIHIEH
     QPNGGASLIH AYSSELSQLS PVEMERFSEE FVTLVFSENE NCAAFYVMGI VHGAATYLPD
     FLDYFSFNFP NSPVKMEILG KKDIETTTIS NFHAQVKRTY SHGTYRAGAM RQISLVGAVD
     EEVGDYFPEF LDMLETSPFL KRTLPWGTCS SLQLKSRKES DDGPIMWVRP GEQMIPVADM
     PKSPFKRKRT TNEIKNLQYL PRASEPREML FEDRTRAHAD HIGQGFERET TAAVGVLKAV
     HCVEWNENPR ITKDVICFHA EDFLEVVQRL QLDLHEPPLS QCVQWVDDAK LNQLRREGIR
     YARIQLYDDD IYFIPRNVVH QFKTVSAVCS LAWHIRLKMY HPESAATQNS DNLEETESGK
     ETKADIERRD KTLYSSSTYT CNVQFKDPKQ KPPQIKHEQT YPLQTSEECG NINLPTISPA
     PTECHTFETK TDYTTDTPVK NEMESTLELI NQDFADRHVT PKDTRQHILT NSVIRTEEEN
     MC