ID A0A452R3H1_URSAM Unreviewed; 259 AA.
AC A0A452R3H1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:ENSUAMP00000012831.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000012831.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000012831.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452R3H1; -.
DR STRING; 9643.ENSUAMP00000012831; -.
DR Ensembl; ENSUAMT00000014403.1; ENSUAMP00000012831.1; ENSUAMG00000010370.1.
DR GeneTree; ENSGT00390000011877; -.
DR OMA; DSLINWD; -.
DR OrthoDB; 4839at2759; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
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 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|RuleBase:RU000414}; Nitration {ECO:0000256|ARBA:ARBA00023074};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 62..143
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 150..253
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
SQ SEQUENCE 259 AA; 28544 MW; 680188CDE63176BF CRC64;
MEDGGVLAAR RGVRICVRRA VGAEPAALRR GLAAVLAMLS RAARSTSRTL VPALGSLGSR
QKHSLPDLPY DYGALEPHIN AQIMQLHHSK HHATYVNNLN AIEEKYLEAL EKGDITAQVA
LQPGLKFNGG GHINHSIFWT NLSPKGGGEP KGELLEAIKC DFGSFEKFKE KLTTVSVGVQ
GSGWGWLGFN KEQGRLQIAA CSNQDPLQGT TGLIPLLGID VWEHAYYLQY KNVRPDYLKA
IWNVINWENV TERYMACKK
//