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Database: UniProt
Entry: A0A1S3QDZ6_SALSA
LinkDB: A0A1S3QDZ6_SALSA
Original site: A0A1S3QDZ6_SALSA 
ID   A0A1S3QDZ6_SALSA        Unreviewed;       306 AA.
AC   A0A1S3QDZ6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Lysine-specific demethylase {ECO:0000256|RuleBase:RU369087};
DE            EC=1.14.11.65 {ECO:0000256|RuleBase:RU369087};
GN   Name=LOC106591006 {ECO:0000313|RefSeq:XP_014037654.1};
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_014037654.1};
RN   [1] {ECO:0000313|RefSeq:XP_014037654.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014037654.1};
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_014037654.1; XM_014182179.1.
DR   AlphaFoldDB; A0A1S3QDZ6; -.
DR   STRING; 8030.ENSSSAP00000039687; -.
DR   PaxDb; 8030-ENSSSAP00000039687; -.
DR   KEGG; sasa:106591006; -.
DR   OrthoDB; 3473445at2759; -.
DR   Proteomes; UP000087266; Unplaced.
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:SF6; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 2C-RELATED; 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          41..266
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|RefSeq:XP_014037654.1"
SQ   SEQUENCE   306 AA;  34745 MW;  24042CE9289B7DC4 CRC64;
     SPVLSPVFPP QLSERPKSKD GDTVVYRLKD WPSGEEFMAL MPSRYDDLMR NLPLPEYCDP
     EGNLNLASHL PSFFVRPDLG PRLCCAYGVA ASQEQDFGTA NLHMEVSDIV SVLVYVGVAK
     GNGVLSKTGV LKRLEEEDLD DSVKKRLKDS SETPGALWHI YISRDVEKIK EFLHKQVAKE
     QGAEISAEHD PIREPGWYLS RKLRQRLWEE HDVQGLTVVQ FLGDSVLIPA GALHQVQNLH
     SCVQVINDFV SPEHVFHSFH LTQELRSSRE EPNYEDKLQV KNILFHSVKD ALTSLKRYSQ
     EEEENS
//
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