ID G1RJQ3_NOMLE Unreviewed; 222 AA.
AC G1RJQ3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN Name=SOD2 {ECO:0000313|Ensembl:ENSNLEP00000013460.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000013460.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000013460.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000013460.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|RuleBase:RU000414}.
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000256|ARBA:ARBA00002170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001605,
CC ECO:0000256|RuleBase:RU000414};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR EMBL; ADFV01068012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01068013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01068014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01068015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003271807.1; XM_003271759.3.
DR AlphaFoldDB; G1RJQ3; -.
DR STRING; 61853.ENSNLEP00000013460; -.
DR Ensembl; ENSNLET00000014127.3; ENSNLEP00000013460.1; ENSNLEG00000011061.3.
DR GeneID; 100585174; -.
DR KEGG; nle:100585174; -.
DR CTD; 6648; -.
DR eggNOG; KOG0876; Eukaryota.
DR GeneTree; ENSGT00390000011877; -.
DR HOGENOM; CLU_031625_2_1_1; -.
DR InParanoid; G1RJQ3; -.
DR OMA; DSLINWD; -.
DR OrthoDB; 4839at2759; -.
DR TreeFam; TF105132; -.
DR Proteomes; UP000001073; Chromosome 3.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR GO; GO:0032364; P:intracellular oxygen homeostasis; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:1905932; P:positive regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000349-1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nitration {ECO:0000256|ARBA:ARBA00023074};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 25..106
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 113..216
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 183
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 222 AA; 24736 MW; 648025C390E1E47B CRC64;
MLSRAVCGTS RQLAPALGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN
NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHTI FWTNLSPNGG GEPKGELLEA
IKRDFGSFDK FKEKLTAASV GVQGSGWGWL GFNKERGHLQ IAACPNQDPL QGTTGLIPLL
GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYMAC KK
//
