ID W5ULV5_ICTPU Unreviewed; 224 AA.
AC W5ULV5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN Name=SOD2 {ECO:0000313|EMBL:AHH42921.1};
GN Synonyms=sod2 {ECO:0000313|RefSeq:XP_017311503.1,
GN ECO:0000313|RefSeq:XP_047007067.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH42921.1};
RN [1] {ECO:0000313|EMBL:AHH42921.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed {ECO:0000313|EMBL:AHH42921.1};
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
RN [2] {ECO:0000313|RefSeq:XP_017311503.1, ECO:0000313|RefSeq:XP_047007067.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017311503.1,
RC ECO:0000313|RefSeq:XP_047007067.1};
RG RefSeq;
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; JT418992; AHH42921.1; -; mRNA.
DR RefSeq; XP_017311503.1; XM_017456014.2.
DR RefSeq; XP_047007067.1; XM_047151111.2.
DR STRING; 7998.ENSIPUP00000034129; -.
DR Ensembl; ENSIPUT00000035466; ENSIPUP00000034125; ENSIPUG00000022934.
DR Ensembl; ENSIPUT00000035469; ENSIPUP00000034129; ENSIPUG00000022934.
DR GeneID; 100304675; -.
DR KEGG; ipu:100304675; -.
DR CTD; 6648; -.
DR OMA; SAHCATQ; -.
DR OrthoDB; 4839at2759; -.
DR Proteomes; UP000221080; Chromosome 25.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0001780; P:neutrophil homeostasis; IEA:Ensembl.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0051597; P:response to methylmercury; 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 2: Evidence at transcript level;
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 Nitration {ECO:0000256|ARBA:ARBA00023074};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 27..108
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 115..218
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 52
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 100
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 185
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 189
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 224 AA; 25003 MW; 4996601F1B4B49AF CRC64;
MLSRIGHVRR CAAGLNPLLG ILASRQKHTL PDLPYDYGAL EPHISAEIMQ LHHNKHHATY
VNNLNVTEEK YQEALAKGDV TAQVALQAAL KFNGGGHINH TIFWTNLSPN GGGEPQGELM
EAIKRDFGSF QKMKEKMSSA TVAVQGSGWG WLGYDKENGR LRIAACANQD PLQGTTGLVP
LLGIDVWEHA YYLQYKNVRP DYVKAIWNIT NWENVNERFQ AAKK
//
