ID   C4WTR6_ACYPI            Unreviewed;       217 AA.
AC   C4WTR6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=ACYPI003921 {ECO:0000313|EMBL:BAH71286.1};
GN   Synonyms=100162795 {ECO:0000313|EnsemblMetazoa:NP_001156153.1};
OS   Acyrthosiphon pisum (Pea aphid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC   Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon.
OX   NCBI_TaxID=7029 {ECO:0000313|EMBL:BAH71286.1};
RN   [1] {ECO:0000313|EMBL:BAH71286.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LSR1 {ECO:0000313|EMBL:BAH71286.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAH71286.1};
RA   Shigenobu S., Nakabachi A., Richards S.;
RT   "A full-length cDNA resource of the pea aphid, Acyrthosiphon pisum.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSR1 {ECO:0000313|Proteomes:UP000007819};
RA   Jiang H., Abraham K., Ali S., Alsbrooks S.L., Anim B.N., Anosike U.S.,
RA   Attaway T., Bandaranaike D.P., Battles P.K., Bell S.N., Bell A.V.,
RA   Beltran B., Bickham C., Bustamante Y., Caleb T., Canada A., Cardenas V.,
RA   Carter K., Chacko J., Chandrabose M.N., Chavez D., Chavez A., Chen L.,
RA   Chu H.-S., Claassen K.J., Cockrell R., Collins M., Cooper J.A., Cree A.,
RA   Curry S.M., Da Y., Dao M.D., Das B., Davila M.-L., Davy-Carroll L.,
RA   Denson S., Dinh H., Ebong V.E., Edwards J.R., Egan A., El-Daye J.,
RA   Escobedo L., Fernandez S., Fernando P.R., Flagg N., Forbes L.D.,
RA   Fowler R.G., Fu Q., Gabisi R.A., Ganer J., Garbino Pronczuk A.,
RA   Garcia R.M., Garner T., Garrett T.E., Gonzalez D.A., Hamid H.,
RA   Hawkins E.S., Hirani K., Hogues M.E., Hollins B., Hsiao C.-H., Jabil R.,
RA   James M.L., Jhangiani S.N., Johnson B., Johnson Q., Joshi V., Kalu J.B.,
RA   Kam C., Kashfia A., Keebler J., Kisamo H., Kovar C.L., Lago L.A.,
RA   Lai C.-Y., Laidlaw J., Lara F., Le T.-K., Lee S.L., Legall F.H.,
RA   Lemon S.J., Lewis L.R., Li B., Liu Y., Liu Y.-S., Lopez J., Lozado R.J.,
RA   Lu J., Madu R.C., Maheshwari M., Maheshwari R., Malloy K., Martinez E.,
RA   Mathew T., Mercado I.C., Mercado C., Meyer B., Montgomery K., Morgan M.B.,
RA   Munidasa M., Nazareth L.V., Nelson J., Ng B.M., Nguyen N.B., Nguyen P.Q.,
RA   Nguyen T., Obregon M., Okwuonu G.O., Onwere C.G., Orozco G., Parra A.,
RA   Patel S., Patil S., Perez A., Perez Y., Pham C., Primus E.L., Pu L.-L.,
RA   Puazo M., Qin X., Quiroz J.B., Reese J., Richards S., Rives C.M.,
RA   Robberts R., Ruiz S.J., Ruiz M.J., Santibanez J., Schneider B.W.,
RA   Sisson I., Smith M., Sodergren E., Song X.-Z., Song B.B., Summersgill H.,
RA   Thelus R., Thornton R.D., Trejos Z.Y., Usmani K., Vattathil S.,
RA   Villasana D., Walker D.L., Wang S., Wang K., White C.S., Williams A.C.,
RA   Williamson J., Wilson K., Woghiren I.O., Woodworth J.R., Worley K.C.,
RA   Wright R.A., Wu W., Young L., Zhang L., Zhang J., Zhu Y., Muzny D.M.,
RA   Weinstock G., Gibbs R.A.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:NP_001156153.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2022) 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. {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. {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; AK340739; BAH71286.1; -; mRNA.
DR   RefSeq; NP_001156153.1; NM_001162681.2.
DR   AlphaFoldDB; C4WTR6; -.
DR   SMR; C4WTR6; -.
DR   STRING; 7029.C4WTR6; -.
DR   EnsemblMetazoa; NM_001162681.2; NP_001156153.1; LOC100162795.
DR   GeneID; 100162795; -.
DR   KEGG; api:100162795; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   HOGENOM; CLU_056632_4_0_1; -.
DR   InParanoid; C4WTR6; -.
DR   OMA; GARYACG; -.
DR   OrthoDB; 3470597at2759; -.
DR   Proteomes; UP000007819; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   2: Evidence at transcript level;
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:UP000007819};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..217
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014569006"
FT   DOMAIN          41..176
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   217 AA;  22140 MW;  88946D2ED0468E95 CRC64;
     MAPKIMLLIT LSVASAVLVS AASPPFQERK AIVVLKGPGQ VSGNVTFIQA NRGGPVMITG
     VVSGLTEGPH GFHVHEKGDV TNGCISTGSH FNPQGNKHGG PNDETRHAGD LGNIQADNTG
     VAQFSYSDSL ISLVGAHNIL GRAVVVHADT DDMGRGGFTD SLTTGHAGSR VACGVIGILD
     PITPWDKSAG HRSPSTSHVL LLTAVAAIAS MLAANSI
//