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Database: UniProt/TrEMBL
Entry: F6VK78_MONDO
LinkDB: F6VK78_MONDO
Original site: F6VK78_MONDO 
ID   F6VK78_MONDO            Unreviewed;       154 AA.
AC   F6VK78;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   25-APR-2018, entry version 49.
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:ENSMODP00000026310};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000026310, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000026310, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L.,
RA   Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J.,
RA   Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A.,
RA   Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L.,
RA   Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M.,
RA   Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E.,
RA   Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M.,
RA   Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E.,
RA   Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A.,
RA   Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J.,
RA   Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J.,
RA   Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S.,
RA   Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A.,
RA   Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C.,
RA   Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P.,
RA   Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C.,
RA   Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K.,
RA   Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D.,
RA   Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G.,
RA   Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E.,
RA   Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C.,
RA   Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E.,
RA   Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K.,
RA   Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A.,
RA   Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R.,
RA   Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A.,
RA   Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N.,
RA   Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S.,
RA   Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F.,
RA   Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P.,
RA   Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D.,
RA   Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in
RT   non-coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000026310}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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   RefSeq; XP_001365144.1; XM_001365107.3.
DR   STRING; 13616.ENSMODP00000026310; -.
DR   PRIDE; F6VK78; -.
DR   Ensembl; ENSMODT00000026778; ENSMODP00000026310; ENSMODG00000021041.
DR   GeneID; 100014993; -.
DR   KEGG; mdo:100014993; -.
DR   CTD; 6647; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00530000063226; -.
DR   InParanoid; F6VK78; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   TreeFam; TF105131; -.
DR   Proteomes; UP000002280; Chromosome 4.
DR   Bgee; ENSMODG00000021041; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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:UP000002280};
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:UP000002280};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  15933 MW;  A9031805D4928A31 CRC64;
     MVLKAVCVLK GDGPVQGTIF FEQKQVGEPV ELSGSIKGLA EGDHGFHVHE FGDNTQGCTS
     AGAHFNPHSK KHGGPTDEER HVGDLGNVTA NKDGVATVSI KDSHIELSGP MSIIGRTMVV
     HEKADDLGKG GNAESEKTGN AGPRLACGVI GIAK
//
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