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Database: UniProt
Entry: G3VNM4_SARHA
LinkDB: G3VNM4_SARHA
Original site: G3VNM4_SARHA 
ID   G3VNM4_SARHA            Unreviewed;       156 AA.
AC   G3VNM4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   16-JAN-2019, entry version 46.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=SOD1 {ECO:0000313|Ensembl:ENSSHAP00000004779};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000004779, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000004779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E.,
RA   Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q.,
RA   Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A.,
RA   Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S.,
RA   Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y.,
RA   Kreiss A., Woods G.M., Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered
RT   marsupial Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000004779}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) 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:RU000393}.
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|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; AEFK01104292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01104293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01104294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01104295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; G3VNM4; -.
DR   STRING; 9305.ENSSHAP00000004779; -.
DR   Ensembl; ENSSHAT00000004827; ENSSHAP00000004779; ENSSHAG00000004195.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00940000155551; -.
DR   InParanoid; G3VNM4; -.
DR   OMA; MAMKAVC; -.
DR   TreeFam; TF105131; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR   GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; IEA:Ensembl.
DR   GO; GO:0048365; F:Rac GTPase binding; IEA:Ensembl.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0007569; P:cell aging; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; IEA:Ensembl.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR   GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR   GO; GO:0045859; P:regulation of protein kinase activity; IEA:Ensembl.
DR   GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007648};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    152       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   156 AA;  16323 MW;  FB84EBEF5240FB01 CRC64;
     MVLKAVCVLK GDGPVQGTVF FEQKQVGEPV ELSGSIKGLA EGYHGFHVHE FGDNTQQIGC
     TSAGAHFNPH SKKHGGPDDD ERHVGDLGNV KADKDGVATV SMKDPLIQLS GPMSIIGRTM
     VVHEKPDDLG KGGNEESEKT GNAGPRLACG VIGIAK
//
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