GenomeNet

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   05-JUL-2017, entry version 44.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSMODP00000026310}.
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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:1904115; C:axon cytoplasm; IEA:GOC.
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:0070062; C:extracellular exosome; 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:0043209; C:myelin sheath; 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:0043234; C:protein 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:0000187; P:activation of MAPK activity; IEA:Ensembl.
DR   GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
DR   GO; GO:0007569; P:cell aging; IEA:Ensembl.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; 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:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; 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:0008217; P:regulation of blood pressure; 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:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; IEA:Ensembl.
DR   GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
DR   GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
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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