ID A0A1S3SUR9_SALSA Unreviewed; 1591 AA.
AC A0A1S3SUR9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Lysine-specific demethylase {ECO:0000256|RuleBase:RU369087};
DE EC=1.14.11.65 {ECO:0000256|RuleBase:RU369087};
GN Name=LOC106611934 {ECO:0000313|RefSeq:XP_014068091.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014068091.1};
RN [1] {ECO:0000313|RefSeq:XP_014068091.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014068091.1};
RG RefSeq;
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}.
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DR RefSeq; XP_014068091.1; XM_014212616.1.
DR GeneID; 106611934; -.
DR KEGG; sasa:106611934; -.
DR OrthoDB; 3473445at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
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:UP000087266}.
FT DOMAIN 1320..1551
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..140
FT /note="Polar 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 296..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1591 AA; 170474 MW; 7BFE9A59852FE598 CRC64;
MLAEDHFDEK GKNARRRKES DGGKGESGRR RRTASEGEED MTLKRFKGSG EGAADGQNGS
GSTKASEEGM VTWGAELAGG GRRVNSSSSE VTQVYASPNS TSSQMDQSNT PPRYTKENGR
ALSTQDRQGS ADSTTTATPT PPPLKQAPSP FSNTSFPSLG QMPSLVPGAL APKPSPAGPT
LEREEPSQST NPKMAALVSP GLVTISSPSQ ASSTSVALAA SLGFSPKPPV WKGTTNQSEG
SKTPILAAAG FRLPQSKPAG ASVFGEVSSK TSASSNTPSA SQDSSRPFGF AFGGTKNNKA
QPQQQDQNLF FQCMTGQKTG QNPGGPNQNQ TLGQSQSKDT NYFTAVSESL SKKPPSLFKP
SVLAPASAGL FSSATASLKE QSKVPETQSA GNGVLNKHFA GDILLPSFSS GSGGMRCSGL
GMGAMDTPLA LASGALGGAN NRSGTNGVAV GGFGTKTDSH QNLFLQGSKE PSNPFLAYGE
KLSHSPFSGK PAPLEPETLG PSSASESKSN LFTMVELPKG ILSSPFASLS AAAASSSSSP
APGFTQRPQS VTSSKPKEGS STGDQGSSAE SGSLDDRPSS TSGFPMFGSA VAGGSGENAP
MPFDQAQKFA LEERGQASKR DSDSSDNSDL SDLSETEEGL ERGHAPGGLA GPVKEGAMLL
QKGKGPGVAK SRPRNKPFKV GQSVLKDVTK VRRLKQSGES FLQDGSCINV APHLHKCREC
RMERYRKYRE QEPDDDDPNV ACRFFHFRRL AFTRKGILRV EGFLSPQQSD AMAMGLWLPS
PSVQEGLDLD TSKYILANVG DQFCQLVMSE KEAMMMVEPH QKVAWKRAVR GVREMCDVCE
TTVFNIHWVC RKCGFGVCLD CYRQRRNRPM EEVDEGPDDE VFSWLKCVKG QRHEPQNLMP
TQIIPGTALY NIGDMVHSAR GKWGIKANCP CTSRHHRPLV RPSAPNGISQ QSAVSSSTGS
SGSGSITGGG GPAGSTTPKP EGAEMTVVKT EPTSTTTSSE GGGGGVDTNG ANHTSAPPNP
AQTPTPKDPR PSTGEGNSTA LHWLADLATQ KAKVEDTKDS GSLRSVMGRD TRSPFGLDSF
SALSKPSSSS SSPKLFNSLL LGSSNTQPKP EGSSLRDLLN SGPGRLPQGP GDSGVTFPSV
FSTSAAGDKL KGSLPNFLDH IIASVVETKK AEGRRLGEGG SELGAVGRRD GVMGLSVLDP
HTSHSWLCDG RLLCLQDPSN TNNWKIFREC WKQGQPVLVS GIHKRLKGAL WRPEAFSEEF
GDQDVDLVNC RNCAIISDVK VRDFWDGFQI ISKRLKGSDG QPMVLKLKDW PPGEDFRDMM
PTRFDDLMDN LPLPEYTKRD GRLNLASRLP NFFVRPDLGP KMYNAYGLME TEDRSVGTTN
LHLDVSDAVN VMVYVGIPEG EGDHVKEMDI AGCKEVMTTI EEGDVDEMTK RRVYEAKEKP
GALWHIYSAK DAEKIRELLR KVGEEQGQEN PPDHDPIHDQ SWYLDGVLRR RLYEEYGVQG
WAIVQFLGDA VFIPAGAPHQ VHNLYSCIKV AEDFVSPEHV KHCFRLTQEF RHLSTTHSNH
EDKLQVKNII YHAVKDAVGT LRAHEPKLAR S
//
