GenomeNet

Database: UniProt/TrEMBL
Entry: D6WWA9_TRICA
LinkDB: D6WWA9_TRICA
Original site: D6WWA9_TRICA 
ID   D6WWA9_TRICA            Unreviewed;       215 AA.
AC   D6WWA9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   25-OCT-2017, entry version 38.
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:BAV32138.1};
GN   ORFNames=TcasGA2_TC005780 {ECO:0000313|EMBL:EFA09191.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Coleoptera; Polyphaga;
OC   Cucujiformia; Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA09191.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA09191.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA09191.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G.,
RA   Friedrich M., Grimmelikhuijzen C.J., Klingler M., Lorenzen M.,
RA   Richards S., Roth S., Schroder R., Tautz D., Zdobnov E.M., Muzny D.,
RA   Gibbs R.A., Weinstock G.M., Attaway T., Bell S., Buhay C.J.,
RA   Chandrabose M.N., Chavez D., Clerk-Blankenburg K.P., Cree A., Dao M.,
RA   Davis C., Chacko J., Dinh H., Dugan-Rocha S., Fowler G., Garner T.T.,
RA   Garnes J., Gnirke A., Hawes A., Hernandez J., Hines S., Holder M.,
RA   Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Jackson L., Kovar C.,
RA   Kowis A., Lee S., Lewis L.R., Margolis J., Morgan M., Nazareth L.V.,
RA   Nguyen N., Okwuonu G., Parker D., Richards S., Ruiz S.J.,
RA   Santibanez J., Savard J., Scherer S.E., Schneider B., Sodergren E.,
RA   Tautz D., Vattahil S., Villasana D., White C.S., Wright R., Park Y.,
RA   Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J.,
RA   Brown S.J., Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H.,
RA   Lorenzen M., Maselli V., Osanai M., Park Y., Robertson H.M., Tu Z.,
RA   Wang J.J., Wang S., Richards S., Song H., Zhang L., Sodergren E.,
RA   Werner D., Stanke M., Morgenstern B., Solovyev V., Kosarev P.,
RA   Brown G., Chen H.C., Ermolaeva O., Hlavina W., Kapustin Y.,
RA   Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P.,
RA   Aranda M., Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F.,
RA   Bopp D., Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E.,
RA   Ferrier D.E., Friedrich M., Gordon C.M., Jindra M., Klingler M.,
RA   Lan Q., Lattorff H.M., Laudet V., von Levetsow C., Liu Z., Lutz R.,
RA   Lynch J.A., da Fonseca R.N., Posnien N., Reuter R., Roth S.,
RA   Savard J., Schinko J.B., Schmitt C., Schoppmeier M., Schroder R.,
RA   Shippy T.D., Simonnet F., Marques-Souza H., Tautz D., Tomoyasu Y.,
RA   Trauner J., Van der Zee M., Vervoort M., Wittkopp N., Wimmer E.A.,
RA   Yang X., Jones A.K., Sattelle D.B., Ebert P.R., Nelson D., Scott J.G.,
RA   Beeman R.W., Muthukrishnan S., Kramer K.J., Arakane Y., Beeman R.W.,
RA   Zhu Q., Hogenkamp D., Dixit R., Oppert B., Jiang H., Zou Z.,
RA   Marshall J., Elpidina E., Vinokurov K., Oppert C., Zou Z., Evans J.,
RA   Lu Z., Zhao P., Sumathipala N., Altincicek B., Vilcinskas A.,
RA   Williams M., Hultmark D., Hetru C., Jiang H., Grimmelikhuijzen C.J.,
RA   Hauser F., Cazzamali G., Williamson M., Park Y., Li B., Tanaka Y.,
RA   Predel R., Neupert S., Schachtner J., Verleyen P., Raible F., Bork P.,
RA   Friedrich M., Walden K.K., Robertson H.M., Angeli S., Foret S.,
RA   Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA09191.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA09191.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic
RT   information for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
RN   [3] {ECO:0000313|EMBL:EFA09191.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA09191.1};
RA   Shelton J.M., Herndon N., Coleman C., Lu N., Brown S.J.;
RT   "Tools and pipelines for BioNano data: molecule assembly pipeline and
RT   FASTA super scaffolding tool.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:BAV32138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GA-I {ECO:0000313|EMBL:BAV32138.1};
RX   PubMed=27387523; DOI=10.1038/srep29583;
RA   Tabunoki H., Gorman M.J., Dittmer N.T., Kanost M.R.;
RT   "Superoxide dismutase 2 knockdown leads to defects in locomotor
RT   activity, sensitivity to paraquat, and increased cuticle pigmentation
RT   in Tribolium castaneum.";
RL   Sci. Rep. 6:29583-29583(2016).
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   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; LC154964; BAV32138.1; -; mRNA.
DR   EMBL; KQ971361; EFA09191.1; -; Genomic_DNA.
DR   RefSeq; XP_972440.1; XM_967347.3.
DR   STRING; 7070.TC005780-PA; -.
DR   EnsemblMetazoa; TC005780_001; TC005780_001; TC005780.
DR   GeneID; 661168; -.
DR   KEGG; tca:661168; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   InParanoid; D6WWA9; -.
DR   KO; K04564; -.
DR   Proteomes; UP000007266; Linkage group 8.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007266};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266}.
FT   DOMAIN       19     99       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      105    208       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        43     43       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        91     91       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       175    175       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       179    179       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   215 AA;  23642 MW;  9B983224E231AE21 CRC64;
     MFALRRLATA PLAGSRAAHS LPELPYAYEA LEPVISRDIM CLHHSKHHQT YVTNLNAAEE
     KLKAALSKGD ISTAISLEPA LRFNGGGHLN HSIFWQNLSP ESTQPSDALK KAIEDSFGGV
     QQLKDQLSAS SIGVQGSGWG WLGYCSKSGK LKIATCANQD PLQATTGLVP LLGIDVWEHA
     YYLQYKNVRA DYVKAIFEIV NWKDVSQRFE KAKSC
//
DBGET integrated database retrieval system